University of Rochester v the University of Queensland and CSL Limited
[2005] APO 34
•13 July 2005
ABSTRACTS OF DECISIONS
DECISION OF A DELEGATE OF THE COMMISSIONER OF PATENTS
Application : No. 688759 in the name of University of Rochester;
Title: Production of Human Papillomavirus Capsid Protein and Virus-Like Particles
Action: Opposition under section 59 by The University of Queensland and CSL Limited
Decision: Issued 13 July 2005.
Abstract
The claims as they broadly encompass VLPs from human papillomavirus were found not to be novel in light of either the Frazer and/or Kirnbauer citations published prior to the priority date. However, the claims as they relate to a specific VLP (from HPV16) were novel and inventive in light of any of those citations because neither citation identified the source of the HPV16 used.
There is another patent application from the Kirnbauer (NIH) group (683220) which was not published before the earliest priority date but is still part of the whole of contents prior art base for novelty. 683220 is also currently undergoing opposition proceedings by the same opponent. In contrast to the other citations, 683220 mentions the correct source of HPV16 and was therefore raised under regulation 5.11. The applicant in addressing the extra citation did not attempt to distinguish the claims but challenged the priority date of the related application. If the related application is not entitled to its earliest priority date, then there is a serious question about the novelty of their claims in light of the current application with respect to HPV16.
Novelty issue in either 688759 or 683220 cannot be finalised until their respective priority dates can be determined. All parties in both oppositions were invited to provide submissions and a second separate decision will issue limited to this issue.
PATENTS ACT 1990
DECISION OF A DELEGATE OF THE COMMISSIONER OF PATENTS
Re:Patent Application No. 688759 by University of Rochester; and opposition thereto under section 59 by The University of Queensland and CSL Limited.
BACKGROUND
Patent application 688759 was filed under the provisions of the PCT on 8 March 1994 in the name of University of Rochester claiming priority from two US basic applications (28517 and 207309) filed on 9 March 1993 and 7 March 1994 respectively. The inventors were listed as Robert C Rose, William Bonez and Richard C. Reichman.
The Australian application was advertised accepted on 19 March 1998 and on 17 June 1998, an opposition was filed in the name of The University of Queensland and CSL Limited. The main evidentiary stages in the opposition were completed by 17 December 2001. The opponent made two subsequent requests for leave to serve further evidence. The applicant objected to both requests and the Commissioner in hearing these objections allowed some extra evidence to be admitted with the applicant being given an opportunity to respond (see University of Rochester v University of Queensland and CSL Ltd 2003 APO 4). The two rounds of further evidence were finally completed on 30 September 2003. Just prior to the substantive hearing, the opponent filed evidence relating to the publication date of certain documents. The applicant did not object to this material but provided a short declaration in response at the hearing.
The substantive hearing was held in Canberra on 19 August 2004. The applicant was represented by Mr Bruce Caine SC instructed by Dr Steven Borovec and Mr Raymond Evans patent attorneys of Phillips Ormonde & Fitzpatrick, Melbourne. Mr Mark Goldman, registered US patent attorney from Nixon Peabody LLP also appeared on behalf of the applicant. The opponent was represented by Mr David Yates SC assisted by Mr Robin Kelly, patent attorney of Fisher Adams Kelly, Brisbane. Mr John Cox and Mr Peter Turvey of CSL also attended on behalf of the opponent.
SPECIFICATION
The specification relates to papillomaviruses and the expression of the L1 major capsid protein from such viruses to produce virus like particles (VLPs) which are able to induce neutralising antibodies against the native virus.
Papillomaviruses infect the epithelia of a wide variety of species of animals (including humans), generally inducing benign and fibro-epithelial tumours or warts. However some viruses cause genital warts in humans and a proportion of these can undergo malignant progression leading to cervical cancer. This is particularly true if the warts arise from infection with certain human papillomavirus genotypes, such as HPV16.
The described invention relates to a method of expressing the human papillomavirus (HPV) L1 major capsid protein coding sequence using the baculovirus expression system, production of HPV virus-like particles (VLPs) and use of these VLPs in production of antibodies which recognize epitopes on HPV, and for HPV vaccine development, and for development of serological tests for the detection of HPV infection. The main embodiments involved the production of human papillomavirus type-6 (HPV6) and HPV11 but the production of HPV16 and HPV-18 VLPs was also disclosed (see, for instance, examples XI and XII) and the specification showed electron micrographs of the VLPs produced from all 4 serotypes (see figures 2, 6, 7 and 16). The specification noted that the VLPs were morphologically similar to the native viruses (see, for example, page 7, lines 1-5; example 3, page 20).
VLPs from HPV11 were assessed in example 13 (page 29) for their ability to detect specific antibodies in patients' sera already confirmed to react to HPV-11 whole virus particles in an ELISA (see page 30). The specification also confirmed neutralisation activity of an anti-VLP serum on a infectious HPV11 viral suspension (example 9, page 25). The specification therefore concluded that their VLPs had similar antigenic characteristics to the native infectious papillomavirus.
The specification ends with 32 claims, including a number of independent claims which read as follows:
1. An isolated non-infectious human papillomavirus virus-like particle or capsomere comprising a human papillomavirus L1 capsid protein which is conformationally correct and is recognized by antibodies present in sera obtained from human patients infected with human papillomavirus.
8. A method of producing an isolated non-infectious human papillomavirus virus-like particle or capsomere in a cell comprising:
transfecting a cell with a recombinant expression vector containing a human papillomavirus capsid protein coding sequence under conditions facilitating expression of said capsid protein, thereby producing a non-infectious papillomavirus virus-like particle or capsomere comprising an L1 capsid protein for the human papillomavirus, which is conformationally correct and is recognized by antibodies present in sera obtained from patients infected with the human papillomavirus.
19. A method of producing an isolated non-infectious human papillomavirus virus-like particle or capsomere in an insect cell comprising:
cloning a human papillomavirus capsid protein coding sequence into a baculovirus transfer vector;
co-transfecting insect cells with said baculovirus vector and Autographa california nuclear polyhedrosis virus genomic DNA;
recovering recombinant baculoviruses; and
infecting said insect cells with said recombinant baculoviruses under conditions facilitating expression of the capsid protein, thereby producing a non-infectious papillomavirus virus-like particle or capsomere comprising an L1 capsid protein for the human papillomavirus, which is conformationally correct and is recognised by antibodies present in sera obtained by patients infected with the human papilloma virus.
29. An isolated non-infectious recombinant human papillomavirus virus-like particle or capsomere produced according to the method comprising:
infecting a cell with a recombinant expression vector containing a human papillomavirus type-6 L1 protein coding sequence or a human papillomavius type-11 L1 capsid protein coding sequence under conditions facilitating expression of said L1 capsid protein, thereby producing a non-infectious human papillomavirus virus-like particle or capsomere comprising a human papillomavirus type-6 L1 capsid protein sequence or a human papillomavirus type-11 L1 capsid protein sequence, which is conformationally correct and is recognised by antibodies present in sera obtained from human papillomavirus type-6 infected patients or human papillomavirus type-11 infected human patients, respective (sic), and isolating said particle.
30. A purified, non-infectious human papillomavirus virus-like particle or capsomere produced from the expression of the human papillomavirus capsid protein coding sequence, said capsid protein consisting of the L1 capsid protein, wherein said particle or capsomere is recognised by antibodies present in sera obtained from human patients infected with the human papillomavirus.
I note that HPV6 and HPV11 were specifically mentioned in the claims but HPV16 or HPV18 were not. I also note (from the hearing) that it was clear that the applicant intended the word “conformationally correct” as used in the specification to mean “morphologically correct”. I will therefore use the term “conformationally correct” to mean “morphologically correct” in my novelty/inventive step considerations but discuss later whether that definition is clear from the specification.
KEY AREAS OF DISPUTE
Despite the large amount of evidence in this case, the parties were able to confine their arguments to a small number of key points with clear submissions provided both at (and after) the hearing. This was extremely useful as it consolidated the evidence and helped to provide much needed focus for the hearing.
The opponent only pursued three grounds of objection to the grant of a patent based on the claims as currently drafted (although they indicated at the hearing that they might have further section 40 problems to raise if the claims were amended to specifically refer to HPV16):
i.If the claims are entitled to their earliest priority date of 9 March 1993, then all the claims apart from claims 12 and 22 lack novelty in light of:
Australian patent application 23666/92 (published as WO 93/02184 on 4 February 1993) and now granted as patent 651727 in the name of the University of Queensland and CSL limited. Jian Zhou and Ian Frazer are listed as the inventors of this citation which will be referred to hereafter as the "Frazer citation";
Kirnbauer et al (1992) Proceedings of the National Academy of Sciences 89 12180-12184 ("Kirnbauer 92")
Hagensee (1993) Journal of Virology 67 pages 315-322 ("Hagensee")ii.If the claims are entitled to a later priority date [based on the filing dates of either the second priority document (7 March 1994) or the opposed specification (8 March 1994)], then all the claims (apart from claims 12 and 22) are also not novel based on:
Kirnbauer et al (1993) Journal of Virology 67: 6929-6936 ("Kirnbauer 93")
Rose et al (1993) Journal of Virology 67: 1936-1944 ("Rose 93")iii.The claims as a whole are unclear because the term "conformationally correct" is unclear
iv.The claims as a whole lack fair basis because the phrase "capsomeres, fragments or portions" was too broad.
At the hearing, I also observed that patent application 683220 which was subject to an opposition by the same opponent appeared to be part of the prior art base for "whole of contents" novelty whatever priority was claimed by the current applicant. This was clearly a close citation, and I used the provisions of regulation 5.11 to bring this document into the current proceedings. The applicant was provided time after the hearing to address this document. They filed extra evidence in November 2004. No further material was provided by the opponent.
DECISION
Novelty
The test for novelty is the "reverse infringement test" as set out in Meyers Taylor Pty Ltd v Viccar Industries ( 1977) 137 CLR 228 at page 235 where Aickin J stated:
"The basic test for anticipation or want of novelty is the same as that for infringement and generally one can properly ask oneself whether the alleged invention would if the patent were valid, constitute an infringement."
Infringement is said to occur where "each and every one of the essential features of that claim have been taken" (Rodi and Wienenberger AG v. Henry Showell Ltd (1969) RPC 367).
A prior disclosure will only invalidate a claim if, after having read it, the skilled addressee would rather than could have produced all the essential integers of the claim. Thus, in General Tire & Rubber Co v Firestone Tyre & Rubber Co Ltd, (1972) RPC 457, the court noted at page 485:
"To anticipate the patentees claim, the prior publication must contain clear and unmistakable directions to do what the patentee claims to have invented ... A signpost, however clear, upon the road to the patentee's invention will not suffice. The prior inventor must be clearly shown to have planted his flag at the precise destination before the patentee."
And later (at page 486):
"If ... the prior publication contains a direction which is capable of being carried out in a manner which would infringe the patentee's claim, but would be at least be as likely to be carried out in a way that would not do so, the patentee's claim will not be anticipated."
Prior Art Background
The evidence indicates that there were at least four separate groups of scientists working on VLPs in HPV at around the priority date of the current application - the Frazer, Hagensee, Rose and Kirnbauer groups. For convenience, I will refer to these different groups using the parties' main nomenclature (the Frazer, Hagensee, Kirnbauer (NIH) and Rochester groups). All of the citations relied on by the opponent in this and the related opposition on 683220 are sourced from one of these 4 groups. Three of the groups went on to file patent applications in Australia with close priority and publication dates. I have summarised the details of these applications in the table below:
Number Inventive Group earliest priority date dates of other priority documents filing date publication date 651727 Frazer (opponent) 19 July 1991 nil 20 July 1992 4 Feb 1993 683220 NIH (Kirnbauer) 3 Sept 1992 16 Mar 1993 3 Sept 1993 17 Mar 1994
688759 Rochester (Rose) (current applicant) 9 Mar 1993 7 Mar 1994 8 Mar 1994 15 Sept 1994
The opponent has opposed both the current application by Rochester and the related application by NIH. Neither Rochester nor NIH has opposed the Frazer application which has now been sealed as a patent in Australia.
Frazer work
The current opponent relied very heavily on their own work to argue that the claims of both the Rochester and NIH patent applications lack novelty. There were 3 publications from the Frazer group prior to the earliest priority date of the current claims:
Australian patent 651727 in the name of University of Queensland and CSL Ltd (referred to in the table above) published 4 Feb 1993 (the Frazer patent)
Zhou, J et al, (1991) Expression of vaccinia recombinant HPV16 L1 and L2 ORF proteins in epithelial cells is sufficient for assembly of HPV virion-like particles J. Virology 185:251-257 (Zhou 1).
Zhou, J et al, (1992) Human Papillomavirus Type 16 virions produced by a recombinant Vaccinia virus J. Virology 189(2) 592-599 (Zhou 2).
All three citations were published prior to the earliest priority date of the current application. The Frazer patent was the closest citation of the three Frazer documents and incorporates the disclosures of the two Zhou articles which were limited to HPV16 VLPs. The Frazer patent disclosed a general method of making constructs of recombinant DNA molecules encoding the papillomavirus L1 or L1 and L2 genes and transfecting a suitable host cell to produce viral-like particles (VLPs) which could be useful as a diagnostic agent as well as forming a component of a vaccine. The citation taught that the L1 or L1 and L2 gene products were able to self-assemble into VLPs. The citation noted that the L1 protein alone is sufficient to form VLPs for bovine papillomavirus type 1 (BPV1), HPV11 and HPV6. However, HPV16 required both the L1 and L2 proteins (page 6, lines 15 et seq).
The Frazer citation analyses in detail VLPs of both HPV16 (example 1) and BPV1 (example 3). The BPV1 VLPs were found to closely resemble the native virion (page 32, lines 34-36). This was also true for the VLPs of HPV6 and HPV11 (page 30, lines 2-6). In contrast, the citation notes (page 15, lines 13-23) that HPV16 VLPs were smaller than the native virion (the diameter of the HPV16 VLP was 35nm - 40nm compared with a diameter of 50nm for the native virion).
The main examples in the Frazer citation use the vaccinia vector/mammalian cell expression system to produce VLPs, but the specification suggests that other expression systems could also be used including a baculovirus/insect cell system (page 6, line 28 et seq) and a yeast cell system (page 7, lines 1-3). One example (page 19, lines 23-30) uses the baculovirus/insect system to express the HPV16 L1 or L2 ORF. The example was only used to generate L1 or L2 recombinant proteins for use in the succeeding Western blotting assay and there was no suggestion that this example produced VLPs.
Did the Frazer patent disclose immunologically correct HPV VLPs (other than HPV16 VLPs)?
According to the applicant, the only parts of Frazer which were relevant to the current claims were the examples concerning the generation of VLPs from HPV6 and HPV11 using a mammalian expression system with a vaccinia virus vector in a CV-1 monkey kidney cell line. Even then, the applicant argued that the examples were not sufficient to deprive the current claims of their novelty and inventive step. The applicant submitted that the Frazer citation did not verify that their HPV6 and 11 VLPs were conformationally correct or reactive with patient sera (as required by all the current claims). Further, it could not reliably be concluded that the Frazer VLPs would have had these properties because the opposed specification used a different expression system (an insect expression system) to that used by Frazer in his earlier patent.
However, while the Frazer citation did not show electron micrographs of either HPV6 or HPV11 VLPs, it does successfully report that authentic VLPs were produced for the L1 protein alone (see page 33, lines 13-15) and the L1/L2 double recombinants (see page 30, lines 2-5). This could only have been verified using electron microscopy and Frazer must have done this work to make the conclusions he did on pages 30 and 33. Given this, I am satisfied that the Frazer citation established that the VLPs from HPV6 and HPV11 were morphologically correct.
In contrast, I accept that Frazer had not verified whether his VLPs were reactive with human sera from infected patients. The opponent argued that the VLPs disclosed by Frazer inherently had this cross-reactive feature (although this property was not known at the time and could not be inferred from the citation). According to the opponent, the only method disclosed in the Frazer citation for generating VLPs involves the self-assembly of L1 (or L1/L2) gene products in a suitable expression system. This single option provides the skilled worker clear directions to use that particular method to generate VLPs. If those VLPs inherently have conformational and neutralising epitopes, then the citation is an anticipation because, as noted in General Tire & Rubber Co v Firestone Tyre & Rubber Co Ltd [1972] RPC 457 at 485-486,:
"if in carrying out the directions contained in a prior inventor's publication will inevitably result in something being made or done which, if the claim of the opposed specification were a claim of a valid patent, would constitute and infringement of that claim, then that claim would have been anticipated".
The opponent never tried to replicate Frazer's work and directly verify in their evidence whether the VLPs produced in accordance with the instructions of the Frazer patent were cross-reactive with sera from infected patients. However, they suggested that later workers (including, they argued, the opposed specification) had used the Frazer methodology to generate VLPs from papillomaviruses which were cross reactive. As a result, according to the opponent, the only advance proffered by the opposed specification over the Frazer citation was the verification of certain properties of the end-product VLPs. However, discovering new properties of a known substance will not confer novelty onto that substance per se.
I note that the opposed specification (as did later workers) used a baculovirus-insect host expression system rather than the Frazer vaccinia-mammalian host expression system so the opponent's claim that later workers used the same methodology was overstated. However, I also accept that the "cross reactive" feature was not something that deliberately added to a VLP made by self assembly. In the opposed specification, the applicant merely verified that the VLPs produced by their method inherently have the features now claimed. The key question in this opposition (and the related opposition on application 683220) is whether the Frazer methodology was the same as the method disclosed in the currently opposed specification and automatically (or inevitably) generated the same entity.
The applicant argued that Frazer used a different expression system and therefore may not have produced the claimed VLP. However, this argument is inconsistent with the assertions made in the opposed specification. Page 10, lines 20-27 of the specification notes that any expression system can be used in the claimed invention provided the system can express the L1 protein coding system. According to the specification, examples of expression systems include (without limitation) any prokayotic and/or eucaryotic system with the vaccinia expression system being specifically mentioned. There is also no evidence before me (apart from the applicant's conjecture) to suggest anything to contradict this statement. I can only conclude that the formation of VLPs is not dependent on a particular expression system and that using any of the expression systems mentioned in the opposed specification will achieve the results now claimed.
Given the concession in the opposed specification, the lack of any evidence establishing that the expression system is critical, the otherwise close similarity of the methodologies of Frazer and the opposed specification and that the Frazer VLPs (for papillomavirus other than HPV16) were conformationally correct, I am convinced that the papillomavirus VLPs produced by Frazer (except for HPV16) were the same as those produced by the opposed specification and therefore inherently were cross reactive with human sera (although this was not verified at the time).
Did the Frazer work disclose conformationally correct VLPs from HPV16?
The Frazer and Zhou citations all reported difficulties generating VLPs from L1 of HPV16 and further noted that L1/L2 HPV16 VLPs were slightly smaller than the native virions. Much of the evidence in this opposition concerned whether the HPV16 VLPs produced by Frazer were (or were not) defective and thus, whether they were also likely to be recognised by antibodies present in sera obtained from human patients infected with papillomavirus.
The publication by Kirnbauer (which post dates the earliest priority date of the current application):
Kirnbauer et al (1993) Efficient self-assembly of Human Papillomavirus type 16 L1 and L1-L2 into Virus-Like Particles Journal of Virology volume 67, Pages 6929-6936 (December 1993) [referred to in the evidence as Kirnbauer 3]
provided the first possible insight into why these earlier workers may have failed to generate morphologically correct HPV16 VLPs. Kirnbauer 3 found that the source of HPV16 was critical to success in making VLPs. They noted that there was a prototype clone of HPV16 (the Gissman clone) which was available from a microorganism depository institution (the ATCC). This prototype clone had been isolated from a particular cervical carcinoma (Seedorf et al 1985) and differed from "wild type" HPV16 by a single point mutation gene at amino acid position 202 (His to Asp). Kirnbauer found that the wild type HPV16 L1 could self-assemble more efficiently than prototype HPV16 L1 (or Gissman clone) and further did not generate the smaller particles observed in the prior art. Kirnbauer therefore suggested that using the Gissman (or prototype HPV16) clone was causing the earlier reported failure to generate HPV16 VLPs.
Originally, the opponent had thought the problem resided with the source of the L1 HPV16 DNA used by Frazer. Some time after the hearing (which itself was 12 years after the Frazer publication), the opponent resiled from their original position. They argued instead that Frazer's problem with producing VLPs of HPV16 was not because they used the prototype clone but rather because they used the incorrect codon to initiate transcription.
It is probably not possible to determine exactly why Frazer failed to generate VLPs from HPV16. However, whatever the real explanation for Frazer's failure, the citation clearly indicates that there was a problem generating HPV16 VLPs. The opponent argued that the VLPs produced by Frazer contained a regular array of capsomers and although they were smaller, they had a similar appearance to native PV virions. Their assumption appeared to be that the HPV16 VLPs were "similar enough" to be able to generate antibodies equivalent to those found in human sera.
I accept there is a possibility that Frazer's HPV16 VLPs were reactive with human sera. The applicant's evidence was not convincing enough to prove the converse. However, a possibility that the HPV16 had the correct conformation is insufficient to prove a case of novelty. The opponent has to establish that the Frazer HPV16 VLPs were correct. In this regard, in contrast with the VLPs from other papillomaviruses, Frazer reports problems with generating the HPV16 VLPs. The citation also concedes that there may be differences in the appearance of the HPV16 VLPs. All of this raises serious questions about whether the Frazer VLPs have the same properties as those generated by later workers where the same problems have not occurred. The fact that the opponent is postulating different reasons why Frazer might have failed to generate HPV16 VLPs some 12 years after the event suggests that even now, the art is not well understood.
In these circumstances, the burden of proof falls squarely on the opponent to establish that the HPV16 VLPs were reactive with human sera and an assumption that the HPV16 VLPs would necessarily be reactive is not enough. Even visualisation comparison is insufficient given the applicant's evidence that this does not necessarily mean that the VLPs were reactive with human sera. At the very least, the opponent needed to replicate the work of Frazer and show that the VLPs produced by the exemplified Frazer methodology fell within the scope of the claim. Such work was not done by the opponent. However, I note that even if the work had been done, I have serious doubts that it could validate the opponent's assumption. It is still not clear why Frazer had difficulties in producing the VLPs and therefore it may not be possible to replicate his work to determine what product he actually generated.
My view is that the opponent has failed to establish that the Frazer HPV16 VLPs were cross reactive with human papillomavirus. Since the Zhou citations were both limited to HPV16, neither of these disclose a conformationally correct VLP which is cross reactive human papillomavirus.
Are the claims novel in light of the Frazer disclosure?
Having concluded that Frazer has disclosed conformationally correct and cross reactive VLPs from human papillomaviruses except for HPV16, the question now is whether this disclosure deprives any of the claims of their novelty.
In the current case, claims 1-8, 17, 18, 29, 30 and 31 define human papillomavirus VLPs comprising a human papillomavirus L1 capsid protein which is conformationally correct and is recognized by a antibodies present in sera obtained from human patients infected with human papillomavirus and methods of generating such VLPs. As noted above, the Frazer citation broadly discloses each of these features and therefore deprives all these claims of their novelty. There are no claims which specifically define HPV16 VLPs but all of the claims in so far as they limited to HPV16 are novel in light of the Frazer patent.
Claims 9-11, 13-16, 19-28, 32 are specifically defining methods of producing VLPs which are conformationally correct and are recognized by antibodies present in sera obtained from human patients using the baculovirus-insect host cell expression system. Frazer did not explicitly teach an insect expression system. In the general description, it taught that any expression systems could be used including a baculovirus/insect cell system (page 6, line 28 et seq) and a yeast cell system (page 7, lines 1-3). However, there are no instructions to use a insect expression system over any of the other expression systems and its preferred method used a vaccinia/mammalian cell expression system. My view is that a skilled worker reading the Frazer citation would be at least as likely (and probably more likely) to use a mammalian expression system rather than an insect one. Therefore the citation does not provide "clear and unmistakable directions" to one of the features of the claims.
Having decided that the Frazer citation does not provide “clear and unmistakable directions” to use an insect expression system, the key question then becomes whether that feature is an essential feature of the claims. While the specification does not highlight any particular advantage of this expression system, it does state that it is the preferred expression system over others (see page 10, lines 18-19). The related specification (683220) then mentions that there is an advantage in using the non-mammalian cells over mammalian cells because this avoids the problems of occult viruses (see page 11, lines 1-3). Given this, my view is that the insect expressions system contributes to the working of the invention and is therefore an essential feature in the claims in which it appears. Having accepted that the baculovirus-insect expression system is an essential feature and that the Frazer citation fails to provide “clear and unmistakable directions” to use that expression system, my view is that claims 9-11, 13-16, 19-28, 32 are novel in light of the Frazer citation.
Claims 12 and 22 also define another feature that was not disclosed in the Frazer work which was that the L1 protein sequence had a mutation or deletion of the pentanucleotide mRNA degradation signal sequence AUUUA. The specification noted that removing this sequence increased the expression level of L1 which overcame their original difficulties in having no detectable levels of L1 proteins in their early baculovirus constructs (see page 32, line 21 et seq). As this feature has an important effect on expression and hence VLP production, it is clearly an essential feature of the claims in which it appears. As the Frazer patent does not disclose this feature, claims 12 and 22 are novel in light of the Frazer patent.
Hagensee work
The Hagensee group was the second research group working in the area around the earliest priority date of the current application. As noted above, their work was published in Hagensee (1993) Journal of Virology 67 pages 315-322 (“Hagensee”) prior to the earliest priority date of the current application. This document was never seriously discussed at the hearing because its disclosure was similar to work by Frazer but I will cover it in my decision for completeness. The opponent presented some evidence that Hagensee was publicly available on 6 January 1993, which was 3 months before the earliest priority date of the current application. I will assume this to be the date of publication as the applicant never challenged this date.
Hagensee used vaccinia vectors to express the L1 and L2 capsid proteins of HPV-1. They reported that capsids containing L1 alone were fewer and more variable in size and shape than capsids containing L1 and L2 but that L1 plus L2 capsids were indistinguishable from HPV-1 virions taken from plantar virus. However, no immunisation studies were performed to verify whether the VLPs were cross reactive with antisera against native HPV1 virions.
The variability in VLPs using L1 alone reported by Hagensee was in contrast to both the opposed specification and the Frazer citation. The opposed specification noted that L1 had the intrinsic capacity for self-assembly and did not require other papillomavirus proteins (see page 11, lines 19-20). Frazer noted that VLPs could be generated for papillomaviruses (apart from HPV16) using either L1 alone or a L1/L2 double recombinant (see page 33, lines 8-22 and page 34, lines 31-35).
It is not clear why Hagensee had problems generating VLPs from the L1 protein of HPV1-1 but again it seems to indicate that the art is not well understood. Given that Hagensee did report variability in size and shape of his VLPs using L1 alone, I am unable to conclude that his VLPs were the same as those produced by either Frazer or the opposed specification. As a consequence, my view is that Hagensee does not clearly deprive any of the claims of their novelty (as per F Hoffman-La Roche AG v New England Biolabs Inc 50 IPR 305 at [67]).
Kirnbauer work
The fourth research group working in the field of VLP generation from papillomaviruses at the relevant time was the Kirnbauer (Lowy or NIH) group. I note that while the main citation relied on by the opponent was the Frazer application above, the closest art in the opponent's evidence is actually from the Kirnbauer group. They published some of their work in the December 1992 edition of the prestigious scientific journal PNAS:
Kirnbauer (1992) Papillomavirus L1 major capsid self-assembles into virus like particles that are highly immunogenic P.N.A.S vol 89 12180-12184 [referred to in the evidence as Kirnbauer 2].
The opponent provided evidence from Kim Vandenberg of the Burnet Library in Melbourne that Kirnbauer 2 was available from their library from around 15 February 1993 (which is still prior to the earliest priority date of the current application). The applicant challenged this publication date arguing that the Burnet Library was not open to the public and that therefore the document in this library was unpublished. However, the arguments relating to the Burnet library were irrelevant to the issue. P.N.A.S. is a prestigious and reputed journal which is widely available and it is appropriate to accept its printed date of publication (December 1992) as its international publication date. If the applicant wishes to dispute this date, they have the burden to establish a different date. I therefore accept that Kirnbauer 2 was published before the earliest priority date of the current application and it is therefore part of the prior art base of novelty and inventive step.
Kirnbauer 2 expressed the L1 major capsid protein of bovine papillomavirus type 1 and human papillomavirus type 16 in insect cells via a baculovirus vector and analysed their conformation and immunogenicity. Kirnbauer 2 indicated that L1 has the intrinsic capacity to assemble into empty capsid-like structures (VLPs) which are able to induce high titre neutralising antibodies that are capable of preventing papillomavirus infection in vitro. In contrast to Frazer, this citation was able to assemble HPV16 VLPs from L1 alone and produce larger particles which were similar in morphology to the native virion. It also disclosed VLPs from BPV1 and demonstrated that these VLPs contained neutralising antibodies.
The applicant argued that Kirnbauer 2 does not teach (and there are no experiments or tests) that the particles containing the L1 protein from human papillomavirus were conformationally correct or that they would be recognised by antibodies in patient sera. I note that the citation exemplifed VLPs from both HPV16 and bovine papillomavirus 1 (BPV1) by expressing the L1 protein in a baculovirus-insect expression system. Using electron microscopy, the citation demonstrated that both the BPV1 and HPV16 particles were morphologically similar to the native virions (see pages 12182 and 12183.
The citation only performed neutralising antibody studies (demonstrating that the VLPs would be recognised by antibodies to the native virion) on the BPV1 particles (see page 12182, column 2). However, it notes the similarities between HPV1 and BPV1. It also teaches that BPV1 is a model system for papillomavirus, observing that studies on papillomaviruses have principally been conducted using that model because of a number of technical advantages (see page 12180, column 2). The citation also notes the discusses papillomaviruses in general and specifically referred to the known link between human papillomavirus infection.
My view is that the citation provides a broad teaching to express L1 protein in a baculovirus-insect expression system and thereby produce VLPs from papillomavirus. The skilled worker would clearly understand from the citation that BPV1 was used as an example of papillomavirus and that the results obtained for BPV were predictive and could be extrapolated to all papillomavirus including HPV. I believe that the applicant is reading the citation too narrowly by insisting it should be restricted to its specific examples. Based on the BPV1 model, the VLPs were shown to be both conformationally correct (by electron microscopy) and immunologically cross reactive (by neutralising antibody studies). My view is that this teaching deprives claims 1-11, 13-21, 23 - 32 of their novelty as they relate generally to human papillomaviruses VLPs.
As noted above in the discussion on the Frazer however, there are recognised problems with producing HPV16 if the L1 protein of the Gissman (prototype) clone is used instead of the wild type clone. The citation does appear to imply that the HPV16 source used in their work was the prototype HPV16 (see page 12181, 1st column, second paragraph). Given this, I accept that Kirnbauer 2 does not teach the proper source of HPV16 and is therefore not an enabling disclosure for HPV16. I therefore agree it does not deprive any of the current claims of their novelty as they relate to HPV16. I also note that Kirnbauer 2 does not disclose the additional features defined in claims 12 and 22 and so these claims are also novel in light of Kirnbauer 2.
Inventive Step
Frazer, Zhou 1, Zhou 2, Kirnbauer 2 and Hagensee are all part of the prior art base for inventive step. However, the opponent did not pursue this ground at the hearing. The opponent argued that the contested issues were properly dealt with under the ground of novelty. According to the opponent, if the prior art disclosed the claimed VLPs, then the claims lack novelty (and a consideration of inventive step would be unnecessary). Equally if the prior art did not disclose the claimed VLPs, it would not be obvious how to modify the prior art methods to produce the claimed VLPs (and they conceded that inventive step would not apply).
However, there are residual inventive step issues with respect to two sets of additional essential integers which were not disclosed in some of the prior art documents but which are specifically claimed in the dependent claims:
§ Claims 9-11, 13-16, 19-28, 32 which are limited to the baculovirus-insect expression system;
§ Claims 12 and 22 which introduced the feature that the L1 protein sequence further comprises a pentanucleotide mRNA degradation signal sequence AUUUA in the vicinity of the L1 stop codon.
The first set of claims (claims 9-11, 13-16, 19-28, 32) contain additional essential features which were not disclosed in any of the Frazer, Zhou or Hagensee citations. These claims define a baculovirus-insect expression system which has the advantage of avoiding the problems of occult viruses. While there may be an argument about whether such an advantage might be obvious to the skilled worker (and therefore not a "selective advantage"), there was therefore no evidence before me that this was the case. In any case, as the virus being expressed is mammalian, it may be that the skilled worker was more likely to use a mammalian system rather than an insect expression system and this is consistent with the teaching of Frazer, Zhou and Hagensee. There would need to be a fairly strong motivation in the common general knowledge for the skilled worker to chose a system other than the one exemplified by Frazer, Zhou or Hagensee. There was no evidence that such a motivation existed at the priority date. Hence, there is nothing before me to suggest that the skilled worker would have been directly led to choose the insect system over any other expression system. The opponent has therefore failed to establish that claims 9-11, 13-16, 19-28, 32 lack an inventive step over Frazer, Zhou or Hagensee.
The second set of claims (claims 12 and 22) contain a mutation or deletion of a degradation signal sequences which results in an increased expression of the L1 protein. This feature was not referred to in any of the prior art documents (including Kirnbauer 2). The specification conceded that these types of signals were known in the prior art (referring to particular references at page 32, line 25 - page 33, line 5). However, while there might have been some suggestion in the evidence that these sequences were part of the common general knowledge, there was no evidence before me that the skilled worker would have been directly led to delete the sequence to solve their problem of lack of detectable expression of the L1 protein. As a result, I conclude that the opponent has failed to establish that claims 12 and 22 lack an inventive step in light of any of the raised prior art for inventive step.
Regulation 5.11 - Patent application 683220
In addition to publishing their work in the non-patent literature, the Kirnbauer (or NIH group) filed a patent application in Australia. Patent application 683220 was filed in the name of the Government of the United States of America as represented by the Secretary, Department of Health and Human Services and the National Institutes of Health (NIH) on 3 September 1993. It was published on 17 March 1994 (after the earliest priority date of the current specification). However, it is an Australian patent application with a potentially earlier priority date (either 3 September 1992 or 16 March 1993) than the currently opposed application and is therefore part of the "whole of contents" novelty prior art base [Patents Act 1990 section 7(1)(c)].
The NIH application was clearly a close citation but was not referred to in the evidence by the opponent. Further, in contrast to Kirnbauer 2, the patent citation notes that the source of the L1 for HPV16 was critical. It noted that previous workers had used the prototype Gissman clone available from GenBank Accession number K02718 (see page 8, lines 24 et seq) and that this clone had a mutation and could not self assemble. Given this disclosure and the applicant's challenge to the publication dates of Kirnabuer 2, I sought to introduce the patent document under regulation 5.11 at the hearing to ensure that all relevant material was before the Commissioner. Both parties were provided with an opportunity after the hearing to provide evidence/submissions to address this new document. The applicant filed extra evidence in November 2004. The opponent was given time to respond but advised in February 2005 that they were not intending to file any further information.
The NIH application discloses the production of VLPs from papillomaviruses. The citation describes the expression of a papillomavirus L1 gene construct in a baculovirus/insect host expression system and its subsequent self-assembly into a VLP. The citation demonstrates that such VLPs resemble the native (infectious) virus under the electron microscope, contain conformational epitopes and induce neutralising antibodies.
The current applicant did not attempt to distinguish their claims from the disclosure in the NIH application in their written submissions after the hearing but rather argued that patent application 683220 was not entitled to its earliest priority date with respect to HPV16. According to the applicant, the first priority document of 683220 (filed on 3 September 1992) did not disclose which HPV16 clone should be used as the source material. They suggested that the earliest possible priority date for 683220 in respect of HPV16 was therefore 16 March 1993 which is after the earliest priority date of the 688759 (9 March 1993). This means that the NIH patent application would not be part of the prior art base for novelty for the current application with respect to HPV16. However, it also means that (if the applicant’s arguments are correct) patent application 688759 might then deprive 683220 of its novelty with regard to HPV16.
While the applicant did not directly address the papillomavirus strains other than HPV16 in their submissions, their arguments on the Kirnbauer 2 citation (discussed above) also apply to the NIH application which is from the same research group. However, as also discussed above, I do not accept the applicant’s narrow reading of either citation where they argued that the exemplified BPV1 model work does not deprive the current claims to HPV of their novelty. The teaching of the NIH patent application generally shows the expression of L1 protein in a baculovirus-insect expression system to produce VLPs. The application exemplifies the production of VLPs from both HPV16 and BPV1. While the specific immunological examples were limited to BPV1, the citations make it clear that these were intended to be a model for papillomavirus in general (see the claims, for example). Based on the BPV1 model, the VLPs were shown to be both conformationally correct (by electron microscopy) and immunologically cross reactive (by neutralising antibody studies). My view is that this teaching deprives claims 1-11, 13-21, 23 - 32 of their novelty as they broadly relate to human papillomaviruses VLPs (at least in regard to HPVs other than HPV16).
The only remaining issue is whether NIH is entitled to an earlier priority date than the current application with respect to HPV16. Of course, if NIH has a later priority date than the current application for HPV16 constructs, then this has a serious impact on the related opposition on 683220 because the NIH application may not be novel in light of the current application with regard to HPV16.
At the hearing, the opponent argued that current application was not entitled to its priority date on any of the papillomavirus VLPs. According to the opponent, the immunological data in the first document was all based on a preparation of non-recombinant and recombinant L1 stock solutions (page 14, line 20-page 15, line 9). That preparation involved inter alia a high speed centrifugal step in which the supernatant was removed and used in later immunological investigations. The opponent suggested this step was likely to have removed all the VLPs in the solution and all the subsequent immunological investigations would then have been based on the unassembled L1 recombinant molecule rather than the VLP itself.
I observe that if immunological investigations are necessary to establish priority and the allegations raised above are true then there could be serious questions about the priority of all of the applicant's HPV constructs. However, I would also observe that the immunological investigations are merely verifying properties of a VLP. Assuming the VLP is otherwise enabled, the issue does not appear to have any bearing on the priority date. In any event, I note that the argument was not properly raised (or supported) by the evidence and I am unable to deal with this argument in this opposition.
Having said that, I raised other concerns at the hearing about whether the current application was entitled to its earliest priority date but only with regard to HPV16. I noted that although the first priority document (28517 filed on 9 March 1993) reported success in generating VLPs from HPV16, it was not until the second priority document (207309 filed 7 March 1994) that the source of the HPV16 was explicitly mentioned as being a wild type form of the virus isolated from a CIN III lesion (see example X). Even then, it is unlikely that the applicants realised the importance of this feature because they referred to the Seedorf et al (1985) prototype sequence to describe the coding capacity for their L1 recombinant molecule (see example XI of the second priority document). The first priority document refers to the Gissman clone when describing the HPV16 source (see page 9, lines 10-14). Prima facie, this appeared to infer that the skilled worker should use the Gissman clone as the source of HPV16.
The applicant argued that the passage on page 9 of the first priority document could equally be interpreted as explaining to the skilled worker that the invention could apply to a broad range of HPV types (including [erroneously] the Gissman clone). According to the applicant, the detailed protocol for HPV11 uses genomic DNA from virus particles present in a tissue source (the specification at page 12, line 18). The applicant suggested that this would direct the skilled worker to use the same (or similar) protocol for HPV16 (especially given that clinical samples were readily available).
In absence of any information contradicting the applicant’s position, I accept that the applicant is prima facie entitled to their earliest priority date (ie: 9 March 1993). However, this is still open to challenge. The current applicant has questioned the earliest priority date of another application (683220) which is subject to a related opposition. If Rochester is correct with their arguments on the related application, then potentially the current application might deprive 683220 of its novelty with respect to HPV16. In this event, the applicant of 683220 might seek to cross-challenge the priority date of the current application.
As a result, it is clearly critical to determine the respective priority dates of 683220 and 688759 in relation to HPV16. Given that this issue affects both oppositions, my view is that all parties on both oppositions should have an opportunity to provide evidence or make representations on the following questions:
· What is the first valid priority claim to immunologically correct HPV16 VLPs in both 683220 and 688759?
· If the current application was found to have a later priority date than the other application (683220), would 683220 (or Kirnbauer 3 – see below) deprive the current claims of novelty with respect to HPV16?
The parties have 21 days of the date of this decision to provide comments on these specific questions. All parties will also be given an opportunity to respond to any submissions provided by the other parties. Once the submissions are complete, I will issue a common decision for both oppositions in relation to the specific questions raised above.
I advise that if the Rochester application is found to have an earlier priority date than the current application in relation to HPV16, I intend to raise the Rochester application under regulation 5.11 in relation to the NIH opposition. Please note that the response to the question posed in the second dot point above will be the parties’ opportunity to give evidence or make representations in respect of the Rochester application as required under regulation 5.11(2)(c).
I also advise that in the event an appeal is filed on the current decision or on the related case with regard to the other substantive matters determined in this decision, I still envisage continuing with determining the priority date of both applications in relation to HPV16 and the consequential issue of novelty. Once a decision is issued on the priority date consideration, my understanding is that any appeal on this decision can be joined to the earlier appeal and the Court will be able to consider all issues relating to validity of the patent application.
Further citations
If the current application is not entitled to its priority date, then there are two additional citations (apart from 683220) which also become part of the prior art base for novelty/inventive step:
·Rose et al (1993) Journal of Virology 67: 1936-1944 (Rose);
·Kirnbauer et al Journal of Virology volume 67, Pages 6929-6936 (December 1993) [Kirnbauer 3].
Both these documents were published after the earliest priority date (but before the filing date) of the opposed application. The Rose citation was published in April 1993 and is based on the applicant’s work. The citation reports the expression of the L1 coat protein of HPV11 in Sf-9 insect cells. The resulting VLPs were shown to have conformational epitopes and to react with human sera containing antibodies to HPV. While it is a close citation, it was published after the earliest priority date of the current claims and only discloses HPV11 constructs. There is no evidence before me that suggests that constructs other than HPV16 are not entitled to their priority date. As a consequence, even if the current application is found not to be entitled to its earliest priority date for HPV16, the Rose citation would not be relevant for the purposes of novelty. I note that this was never argued otherwise at the hearing or in the evidence.
In contrast, Kirnbauer 3 discloses the expression of the L1 protein from a wild type clone of HPV16 in a baculovirus-insect expression system and confirms that there was a 3-fold higher level of efficiency using the wild type clone compared with the prototype (Gissman clone). The disclosure further exemplified the expression of L1 from HPV6 and HPV11 and confirmed that this protein alone was sufficient for self assembly of VLPs for papillomaviruses.
As conceded by the applicant at the hearing, Kirnbauer 3 is an extremely close citation. The opponent provided evidence from Kim Vandenberg of the Burnet Library in Melbourne that Kirnbauer 3 was available from their library from 14 December 1993 (which is between the earliest priority date and filing date of the current application). The applicant challenged this date (as they did the publication date of Kirnbauer 2) but for the reasons outlined above for Kirnbauer 2, I do not believe their challenge is well-founded.
If the current application is entitled to its earliest priority date, then Kirnbauer 3 does not form part of the prior art base for novelty and cannot deprive the claims of their novelty or inventive step. However, this situation changes should a successful challenge be mounted against the applicant's priority date, in which event Kirnbauer 3 could become a key novelty citation in this opposition in relation to HPV16. Given this, if the applicant of 683220 decides to mount a challenge to the priority of the current application, Rochester will need to provide submissions in response which are directed both to the priority date issue as well as the Kirnbauer 3 citation.
Section 40
clarity of the term "conformationally correct"
The opponent suggested that the term "conformationally correct" (which appears in most of the claims) is unclear. They argued that the term had a "bewildering array of possible meanings" and that "a reader of the specification would simply not know whether, or how, the claims which incorporate this feature are or could be infringed". I note that the "bewildering array of meanings" were simply a number of instances in the evidence where the applicant was apparently inconsistent with their use of the term. My view is therefore that the opponent has wildly overstated the problem but having said that, I agree there is a minor clarity problem with the term.
At the hearing, the applicant argued that "conformationally correct" as intended to mean that the VLP was morphologically (size and shape) similar to the L1 protein present in a native papillomavirus virion. According to the applicant, the "morphological" requirement was separate from the "immunological" requirement (that the VLP was recognised by sera of infected patients). However, while this is a simple distinction, it is not clearly stated in the specification and the term "conformationally correct" appeared to be used in the evidence to refer to both immunological and morphological features.
It is not clear to me why the applicant used the word "conformationally" when they apparently mean "morphologically". I am also not convinced that this is how the term would normally be used in the art. The term "conformational" applies to well-known immunological terms such as epitopes and antibodies. In such contexts, "conformational correctness" is more likely to mean “morphologically similar and containing conformational epitopes of a native virion”. I note that there are instances in the evidence and submissions when the applicant appears to use the term “conformationally correct” in that way. In paragraph 80 in the written submissions, for example, the applicant notes that "some immunological analysis was performed but it fails to disclose conformational correctness" (my emphasis).
My view is that if the applicant considers the term "conformational correctness" simply to refer morphological correctness as set out in their written submissions, then they need to make this clear by a dictionary definition of the term in the specification. Without this clarification, the term is unclear as it may relate to either immunological or morphological similarities or some strange combination of the two. Hence, claims 1, 8, 19 and 29 which explicitly include the term "conformational correctness" are unclear. Further claims 2-7, 9-18, 20-28, 32 are also unclear because they include the term "conformational correctness" as a consequence of being dependent on one of the main claims.
There was also some debate about the exact scope of the word "correct" (in other words, how correct was correct?). I accept that there is some level of uncertainty in the term but I do not agree that it gives rise to significant problems in understanding whether an entity would fall within the scope of the claim. As the applicant argued, to construe the claim to include only VLPs identical to the native virion would be absurd. A VLP of the invention will be "conformationally correct if it is morphologically similar to the L1 protein in the native virion". As none of the experts appeared to have any real difficulties in assessing whether an entity passed this test, my view is that the scope of the term is clear.
The opponent also argued that the words "conformationally correct" were introduced by amendments filed on 19 December 1997. Their written submissions suggest that this might somehow change the priority date of the claim but it is not clear how or why this would occur. In any event, I do not see the issue as being relevant to the priority date. The specification at filing disclosed a VLP made by a particular self-assembly method. This entity would inherently have a number of properties including "conformational correctness". Adding that term to the claims does not alter the original VLP but merely specifies another property which had already existed. There is therefore no addition of extra subject matter and the introduction of the term does not affect the priority date of the claims.
Fair basis of the phrase "capsomeres, fragments or portions"
The opponent argued that the claims defined "capsomers, fragments and portions of VLPs" but that there was no experimental support for such entities and therefore the claims were speculative and not fairly based. I note that since the High Court decision in Lockwood Security Products v Doric Products Pty Ltd (2004) 62 IPR 461 this issue is a full description rather than fair basis issue. I will therefore deal with their argument under the full description "umbrella" instead.
I note that while the specification does not exemplify particular "capsomers, fragments and portions of VLPs", such entities are inherently part of the VLP itself. The opponent suggested that the specification did not disclose how the such portions could be obtained. However, the onus on the opponent is to prove their case. It is insufficient to argue that a particular aspect of the invention was not exemplified as this is not required. It i well established law that specifications can have omissions. The opponent needed to show that the skilled worker could not obtain such portions and they failed to do this. My view is that they have therefore failed to establish that the specification is not fully described in relation to claims which encompass "capsomers, fragments and portions of VLPs".
CONCLUSION
Claims 1-8, 17, 18, 29, 30 and 31 as they broadly encompass VLPs from human papillomavirus are not novel in light of the Frazer citations. However, the claims as they relate to a specific VLP (from HPV16) are novel and inventive in light of the Frazer citation because the opponent failed to establish that this citation produced VLPs from HPV16 having all the properties of the claimed VLPs. Claims 9-16, 19-28 and 32 are also novel and inventive in light of the Frazer citations because these claims are limited to the baculovirus-insect expression system and this was not sufficiently disclosed in the Frazer citation.
Claims 1-11, 13-21, 23-32 as they broadly encompass VLPs from human papillomavirus are not novel in light of the Kirnbauer 2 citation and patent application 683220. However, the claims as they relate to HPV16 are novel and inventive in light of Kirnbauer 2 as the citation appeared to teach the use of the Gissman clone to generate the HPV16 VLPs.
Claims 12 and 22 are novel and inventive in light of all the cited prior art because the opponent failed to establish that the skilled worker would have been directly led to delete the degradation signal sequence to solve their problem of lack of detectable expression of the L1 protein.
There is a minor clarity problem with the term "conformationally correct" in all the claims but otherwise the opponent did not establish any section 40 deficiencies with the specification.
This concludes my findings on the issues raised by the opponent in the opposition. However, I introduced a related patent application (683220) into the current proceedings under regulation 5.11 as a possible whole of contents novelty citation. The applicant in addressing the citation has challenged the priority date of the related application (683220) in relation to HPV16. Of course, if that application is not entitled to its earliest priority date, then there is a serious question about the novelty of the claims of 683220 which relate to HPV16 in light of the current application 688759.
I am unable to finally determine the novelty issue in either 688759 or 683220 until I can properly determine their respective priority dates with regard to the HPV16 constructs and I cannot do this until both Rochester and NIH have had the opportunity to defend their priority date. I expect to issue a second decision in due course after both parties have been given an opportunity to comment on the issue of priority date of the claims to HPV16 in 688759 and 683220. As advised above, the parties have 21 days of the date of this decision to provide comments and will be provided an opportunity to respond to any submissions provided by the other parties. Once the submissions are complete, I will issue a second decision common to both oppositions.
I note that this second decision will be limited to considering the priority date of both 683220 and 688759 and the consequential novelty issues in respect of HPV16 which might arise as a result of a changed priority date. It will not be possible for the parties to re-open any of the issues which have already been decided above. The avenue for this is through an appeal to the Federal Court (see Iluka Midwest Ltd v Technological Resources Pty Limited [2002] FCA 49 (6 February 2002) and BHP v American Can Company 29 ALR 424). In the event an appeal is filed on this decision, I envisage still continuing with the NIH/Rochester novelty consideration. Once this consideration is completed, my understanding is that the second decision can be joined to the earlier appeal and the Court will be able to consider all issues relating to validity of the patent application.
COSTS
As there is still an outstanding issue of novelty to be resolved, this is necessarily an interim decision. I will therefore defer my consideration of costs until all substantive issues have been completed.
Karen Ayers
Delegate of the Commissioner of Patents
Patent attorneys for the applicant : Phillips Ormonde & Fitzpatrick, Melbourne
Patent attorneys for the opponent : Fisher Adams Kelly, Brisbane
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