Genentech, Inc v Ludwig Institute for Cancer Research and Human Genome Sciences, Inc (Corrected Version)
[2006] APO 20
•5 June 2006
ABSTRACTS OF DECISIONS
DECISION OF A DELEGATE OF THE COMMISSIONER OF PATENTS
Application : No. 710696 in the name of Genentech, Inc.
Title: VEGF-Related Protein
Action: Opposition under section 59 of the Patents Act 1990 by the Ludwig Institute for Cancer Research and Human Genome Sciences, Inc.
Decision: Issued 5 June 2006 .
Abstract
The invention relates to a human VEGF-related protein, antibodies that react with this protein and methods and therapeutic applications involving use of this protein.
The opposition was partially successful on the ground that claims 1-7, 15, 16, 19 to 26, 28 to 33, 39 and 40 lack novelty, but was unsuccessful on all other grounds.
Costs were awarded against the applicant.
PATENTS ACT 1990
DECISION OF A DELEGATE OF THE COMMISSIONER OF PATENTS
Re:Patent Application No. 710696 by Genentech, Inc and opposition under section 59 of the Patents Act 1990 by the Ludwig Institute for Cancer Research and Human Genome Sciences, Inc.
BACKGROUND
Patent Application 710696 (70128/96) in the name of Genentech, Inc (hereafter referred to as Genentech) was filed as PCT application WO 1997/009427 on 30 August 1996 claiming priority from US 60/003,491, which was filed on 8 September 1995. The application was advertised as accepted on 30 September 1999. The Ludwig Institute for Cancer Research (hereafter referred to as Ludwig) and Human Genome Sciences, Inc (hereafter referred to as HGS) filed notices of opposition on 30 December 1999 and 7 January 2000 respectively. Both opponents served their statements of grounds and particulars on 29 March 2000, with Ludwig subsequently amending their statement on 16 November 2004 to add s18(1)(c) as a further ground of opposition. Service of evidence in support was completed by Ludwig on 30 October 2000 and by HGS on 27 April 2001.
Amendments to the claims and specification were filed on 10 January 2002. The amendments were incorporated into the specification on 16 September 2002.
Evidence in answer to Ludwig’s and HGS’s evidence in support was completed on the 17 December 2002 and 18 December 2002 respectively. Evidence in reply was completed by Ludwig on 17 March 2004 and by HGS on 14 May 2004.
The specification that was the subject of the hearing was the specification as accepted and including the amendments of 10 January 2002.
The matter was heard in Canberra on 14 and 15 March 2004. Genetech was represented by Mr Ben Fitzpatrick of Counsel, assisted by Dr Ian Rourke of FB Rice. Ludwig was represented by Mr David Yates of Counsel, assisted by Dr Martin O’Brien and Dr John McCann of Spruson and Ferguson. HGS was represented by Mr David Catterns of Counsel, assisted by Mr Gary Cox of Wray and Associates and Ms Melissa Pytel.
THE EVIDENCE
Ludwig’s evidence in support consists of:
·Statutory Declaration of John Francis McCann, together with exhibits JFM 1-16;
·Statutory Declaration of Peter Adrian Walton Rogers, together with exhibit 1;
·Statutory Declaration of Francis John Ballard, together with exhibit 1.
HGS’s evidence in support consists of:
·Statutory Declaration of Piroska Elizabeth Rakoczy, together with exhibits PER 1-4;
·Statutory Declaration of Brandon John Wainwright, together with exhibits BJW 1-2;
·Statutory Declaration of Gary Baxter Cox, together with exhibits GBC 1-4.
The evidence in Answer consists of:
·Statutory Declaration of Peter Philip Gray in response to Ludwig, together with exhibits PPG 1-8;
·Statutory Declaration of Peter Philip Gray in response to HGS, together with exhibits PPG 1-4;
·Statutory Declaration of Peter Robert Schofield in response to Ludwig, together with exhibits PRS 1-8;
·Statutory Declaration of Peter Robert Schofield in response to HGS, together with exhibits PRS 1-5.
Ludwig’s evidence in reply consists of:
·Statutory Declaration of Kari Alitalo, together with exhibits KA 1-6;
·Statutory Declaration of Peter Adrian Watson Rogers, PR 1-9;
·Statutory Declaration of Francis John Ballard.
HGS’s evidence in reply consists of:
·Statutory Declaration of Piroska Elizabeth Rakoczy.
THE SPECIFICATION
The specification relates to isolation and characterisation of a VEGF-related protein (VRP). VRP is expressed in endothelial cells where it binds to, and phosphorylates the Flt4 tyrosine kinase receptor. The VRP/Flt4 interaction is involved in angiogenesis, embryogenesis, tumour formation and wound healing. The specification exemplifies the isolation and characterisation of cDNA clones encoding human VRP and recombinant expression of one of these clones to produce recombinant VRP. Figure 1 of the specification provides the sequence of the nucleic acid encoding VRP and the 419 amino acid sequence deduced from the nucleic acid sequence.
Human VRP is explicitly defined at page 5 of the specification as a polypeptide sequence containing the amino acid sequence disclosed in figure 1 of the specification, as well as biologically active deletional, insertional, or substitutional variants of this sequence having at least 265 amino acids and/or residues 1 to 29, inclusive, of figure 1. This section of the specification also states that the term VRP excludes all forms of VEGF and PIGF, two related peptides that are ligands for other members of the Flt tyrosine kinase receptor family.
The description of preferred embodiments in the specification includes a description of covalent modification of VRP and therapeutic formulations and uses for VRP, particularly uses associated with disorders of vasculogenesis and angiogenesis and with wound healing. The description also discusses the generation of anti-VRP antibodies and their use as antagonists of VRP function.
The specification ends with 7 examples, which relate to the isolation and recombinant expression of VRP. Recombinant VRP is shown to bind to, and phosphorylate the Flt4 receptor and to have a mitogenic effect on endothelial cells in vitro.
THE CLAIMS
The specification ends with 40 claims, all of which relate to the VRP peptide. The 13 independent claims can be divided into two groups, with the first group defining the claimed protein by explicit reference to the amino acid sequence disclosed in figure 1. Although the second group of claims does not explicitly refer to figure 1, use of the term VEGF-related protein (VRP) in the claims provides a reference to figure 1 through the definition of VRP at page 5 of the specification. Page 5, lines 12 to 17 defines VRP as:
“a polypeptide sequence containing at least residues -20 to 399, inclusive, or residues +1 to 399, inclusive, of the amino acid sequence shown in Figure 1, including residues -5 to 399, inclusive, and residues -4 to 399, inclusive, of the amino acid sequence shown in Figure 1, as well as biologically active deletional, insertional, or substitutional variants of the above sequences having at least 265 amino acids and/or having at least residues +1 through 29, inclusive, of Figure 1.”
Group 1 – claims that include an explicit reference to figure 1.
This group contains independent claims 1-3, 19, 26 and 35.
Claim 1 recites
An isolated protein comprising residues 1 through 399 of Figure 1 having the ability to bind and stimulate phosphorylation of a Flt4 receptor.Claim 2 recites
An isolated VEGF-related protein (VRP) comprising residues -20 through 399 of Figure 1 having the ability to bind and stimulate phosphorylation of a Flt4 receptor.Claim 3 recites
An isolated VEGF-related protein (VRP) comprising at least 351 amino acids in which the amino acid residue corresponding to amino acid residue 394 of the amino acid sequences shown in Figure 1 is a lysine, the protein having the ability to bind and stimulate phosphorylation of a Flt4 receptor.Claims 4 to 8 define specific lengths for the proteins recited in claim 3 and pharmaceutical compositions for the proteins of any one of claims 1 to 3.
Claim 19 recites
A monoclonal antibody which binds to the N-terminal portion from residues -20 through 137, inclusive, or from residues 1 through 137, of the amino acid sequence shown in Figure 1..Claims 20 to 22 define compositions comprising the monoclonal antibody of claim 19. Claim 23 defines use of the antibody for the manufacture of a medicament for treating vascular diseases or dysfunctional states characterised by lack of activation or lack of inhibition of a VRP receptor.
Claim 24 defines a method of using the peptide of claims 1-5 for stimulating phosphorylation of the Flt4 receptor. Claim 25 defines a chimaeric protein comprising the peptide of claims 1 to 5 fused to a tag sequence.
Claims 28 to 33 recite isolated nucleic acids coding for the peptide of claims 1-5 and vectors and expression systems for the production of this peptide.
Claim 26 defines the native signal peptide for human VRF. It recites
A peptide consisting of an amino acid sequence shown in residues -20 through -1, inclusive of Figure 1Claims 35 recites
A sustained-release preparation comprising (i) a monoclonal antibody that binds specifically to a protein comprising the amino acids provided as -20 to 399 in Figure 1, and a semipermeable matrix of solid hydrophobic polymer.
Group 2 – claims that do not explicitly refer to figure 1
The second group of claims consists of independent claims 9, 18, 27, 34, 36, 38 and 39.
Claim 9 recites
A pharmaceutical composition useful for promotion of vascular endothelial cell growth comprising (i) a therapeutically effective amount of a human VEGF-related protein (VRP) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor,(ii) a further cell growth factor, and (iii) a pharmaceutically acceptable carrier.Claims 10-14 define specific lengths for the proteins defined in claim 9 and claim 15 recites use of the VRP protein defined in any of the previous claims for the manufacture of a medicament for treating trauma affecting the vascular endothelium.
Claims 15 to 17 define use of the VRP protein defined in any of the preceding claims for the manufacture of a medicament for treating a dysfunctional state characterised by lack of activation or lack of inhibition of a receptor for VRP.
Claim 18 recites
Use of (i) a human VEGF-related protein (VRP) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor, and (ii) a further cell growth factor other than (i) for the manufacture of a medicament for treating a dysfunctional state characterised by lack of activation or lack of inhibition of a receptor for VRP in a mammal .Claim 27 recites
A method of treating Kaposi’s sarcoma in a mammal comprising administering to the mammal an effective amount of a VRP antagonist.Claim 34 recites
A sustained-release preparation comprising (i) a human VEGF-related protein (VRP) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor, and (ii) a semipermeable matrix of solid hydrophobic polymer.Claim 36 recites
A microcapsule containing a human VEGF-related protein (VRP) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor.Claim 37 defines the microcapsule of claim 36 as a liposome.
Claim 38 recites
A gel formulation comprising (i) a human VEGF-related protein (VRP) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor, and (ii) a water soluble polysaccharide or polyethylene glycol.Claim 39 recites
A human VEGF-related protein (VRF) comprising at least 265 amino acids having the ability to bind and stimulate phosphorylation of a Flt4 receptor, wherein the protein is covalently modified.Claim 40 defines a number of specific forms of covalent modification for the protein of claim 39.
OTHER MATTERS
Immediately prior to the hearing the applicant provided a set of amended claims. The amendments seek to:
·delete claim 26, which recites the VRP signal peptide consisting of residues -20 through to -1;
·amalgamate claims 39 and 40 to result in a single claim directed to a covalently modified human VRP with a discrete range of covalent modifications, which range excludes covalent modification via glycosylation; and
·amend claims 16 to 18 and 23 to restrict the claims to treatment of dysfunctional states associated with lack activation of a VRP receptor.
At the hearing the applicant explained that they only wished to pursue the subject matter in the claims as proposed to be amended and confirmed that they would file a request to make the proposed amendments either after the hearing or after the decision was issued. On the basis of this the opponent restricted their submissions to the claims as proposed to be amended. As a consequence I too have focused my discussion on the subject matter in the claims including the amendments proposed at the hearing, and have only briefly mentioned the subject matter that the applicant proposes excising.
At the hearing Ludwig also provided an amended statement of grounds and particulars that was consistent with the claims as amended by the amendments incorporated in the specification on 16 September 2002. The amendments bring the statement into line with the current claims and do not raise any new matters or seek to introduce any new documents.
CONSTRUCTION
Before considering the substantive issues in this opposition it is important to understand the scope of the term VEGF-related protein and its abbreviation VRP as used in independent claims 9, 18, 27, 34, 36, 38 and 39.
Ludwig submitted that there was little in the specification to define the boundaries of the term VRP. In particular Ludwig submitted that it was not clear whether the term extended to include proteins other than those derived from the human VRP sequence presented in figure 1 of the specification.
However, page 5 of the specification provides an explicit definition of VRP. The definition requires that VRP and VRP variants retain at least 265 residues of the amino acid sequence shown in figure 1, or residues +1 to 29 of the figure 1 amino acid sequence, as well as the ability to bind to, and stimulate the phosphorylation of, the Flt4 receptor. The same page also discloses a range of conventional assays that can be used to characterise binding and phosphorlyation of the Flt4 receptor.
It is also worth noting that the requirement for binding and stimulation of Flt4 also inherently necessitates an association between VRP and the sequence in figure 1. The primary amino acid sequence of a protein is key to the protein’s secondary, tertiary and quaternary structure, which in turn determines the protein’s biological properties. Therefore, Flt4 binding and stimulation necessarily require that the subject protein contains at least some of the residues depicted in figure 1.
The definition at page 5 is also consistent with further information provided in the body of the specification and with the peptides that are the subject of the examples. Based on this, I am satisfied that the boundaries of the invention are clearly stated in the specification and that VRP in its broadest context should be construed as relating to a protein that necessarily contains some of the residues depicted in figure 1 and that also retains the ability to bind to, and stimulate Flt4 phosphorylation.
Ludwig also submitted that it was not clear whether the invention is restricted to peptide variants derived from human VRP. In his first declaration Ludwig’s expert Associate Professor Rogers stated that it was not clear whether the term was used to describe only variants derived from human VRP, or whether it encompassed non-human VRP orthologs, for example naturally occurring mouse and quail VRP orthologs as described in one of the citations put forward by Ludwig.
The specification is silent with respect to anything other than human derived VRP and it provides no discussion of other species variants or experiments conducted to identify VRP equivalents in species other than humans. As submitted by Mr Fitzpatrick, any suggestion that the invention was intended to extend beyond human derived variants to include non-human VRP orthologues would ignore the focus of the specification. This construction is also consistent with reference to VRP in all but one of the claims where there is either explicit definition of “human” VRP or definition of the peptide in terms of a protein that contains a substantial portion of the exact human sequence depicted in figure 1.
With respect to claim 3, the one claim that does not recite “human VRP”, although it could be argued that the claim might include VRP derived from peptides other than the human peptide this would ignore the consistent use of the term VRP in the specification to describe only proteins that are referable to the human sequence disclosed in figure 1 and that are defined at page 5. I believe the problems with claim 3 stem more from a clumsy attempt by the applicant to amend the claims as originally accepted to better avoid the prior art, rather than any real intention to define a substantially different protein to that recited in the other claims. Given this, although claim 3 could be better drafted, I am satisfied that it is reasonable to also construe this claim as relating to a human VRP as defined at page 5 of the specification
Associate Professor Rogers also submitted that it was not clear whether the term “human VRP” restricted the invention to naturally occurring human VRP and naturally occurring variants derived from humans. Again reference to the specification can resolve this issue. Page 11 and example 6 clearly disclose production of variant VRP proteins in non-human prokaryotic and eukaryotic expression systems. This reflects standard practice in the art where a known peptide sequence is modified and the resultant variant protein is either expressed in standard non-human expression systems or produced by synthetic peptide synthesis. This is also supported by Professor Grey in his first declaration where he states that the skilled person would readily appreciate that the term human VRP would include both naturally occurring variants and man-made variants such as recombinant and synthetic proteins.
Given this I believe that the specification provides a clear definition for the term VEGF-related protein and its abbreviation VRP and that there is nothing to suggest that this definition extends to VRP orthologues derived from non-human species. I am also satisfied that the specification does not intend for the invention to be restricted to only naturally occurring VRP and VRP variants and that it is appropriate to regard the invention as extending to include recombinant and synthetic VRP variants derived from the sequence in figure 1.
DECISION
S40 ISSUES
CLARITY
All but one of the initial clarity matters raised by both Ludwig and HGS have fallen away either as a consequence of the amendments of 10 January 2005 and those proposed at the hearing or because they relate more to issues of fair basis and full description. In addition, one of the principle clarity issues pursued by both parties and relating to the scope of the term human VRP has been resolved by the construction exercise in the previous section. Given this I have confined my discussion to the one clarity issue remaining.
VRP antagonist
The first clarity issue relates to the term “VRP antagonist” as used in claim 27. Ludwig submitted that there was no definition of this term in the specification and that it was not clear whether the “VRP antagonist” is an antagonist of the protein of claims 1 to 5.
Firstly, I am satisfied that the skilled person would readily understand the meaning of the term VRP antagonist and appreciate the types of molecules that might function as a VRP antagonist. The term antagonist is a standard term in the art used to describe a second compound that interferes with, or prevents the action of a first compound. Ludwig’s expert Associate Professor Rogers and HGS’s expert Dr Rakocyz both describe antagonists that are consistent with this description and that are also consistent with the anti-VRP antibody and Flt4 receptor derived antagonists disclosed at page 8 of the specification. As such I am satisfied that the skilled person would be familiar with this term and that usage of the term in the specification and the claims is consistent with usage of the term in the art.
Given this, I am satisfied that the claims are clear with respect to the term VRP antagonist.
FAIR BASIS
HGS did not pursue fair basis at the hearing. As a consequence I have restricted my discussion to the fair basis matter raised by Ludwig.
Ludwig’s submissions of fair basis focus on the argument that:
“When the specification as a whole is read, it is clear beyond reasonable argument that the alleged invention around which the claims are drawn is the alleged novel protein of claims 1 to 5, characterised by; (a) a length of at least 351 amino acids, (b) a sequence of residues referable to amended Fig 1 of the specification, and (c) the ability to bind and stimulate phosphorylation of a Flt4 receptor.”
I agree with Ludwig that parts (b) and (c) are features of the invention. These features are defined at page 5 of the specification and are present in each of the claims. However, I do not believe that the specification teaches that VRP must be at least 351 amino acids. As discussed in the construction section, the specification simply teaches that the invention must comprise either residues 1 to 29 of figure 1, or at least 265 residues of figure 1, and also include sufficient residues to bind and phosphorylate Flt4. There is nothing further in the specification to suggest that these properties are only present in a peptide of at least 351 amino acids, nor has Ludwig provided any evidence to suggest that 351 amino acids are essential for Flt4 binding and phosphorylation. As such I am satisfied that VRP as claimed and as defined at page 5 is consistent with VRP as described in the specification as a whole.
Given this, I am satisfied that the claims are fairly based on the invention as disclosed in the specification.
FULL DESCRIPTION
HGS included lack of full description among their grounds of opposition. However, they did not provide any submissions on full description at the hearing. Ludwig provided written submissions on claims 16, 18, 23 and 27 and their dependent claims, but chose not to address claims 16, 18 and 23 in the oral proceedings based on the applicant’s commitment to amend these claims. Claims 16, 18 and 23 are Swiss-type claims that currently recite the preparation of a medicament for the treatment of a dysfunctional state associated with lack of activation or lack of inhibition of a VRP receptor. The foreshadowed amendments remove the reference to lack of inhibition of a VRP receptor and restrict the claims to dysfunctional states characterised by lack of activation of the VRP receptor.
At the hearing Mr Yates confirmed that the proposed amendment would resolve the issue discussed in Ludwig’s submissions and it was agreed that these claims need not be considered in relation to full description based on the applicant’s undertaking to file the proposed amendments following issue of the decision.
Ludwig also made submissions with respect to claim 27. Claim 27 defines a VRP antagonist to treat Kaposi’s sarcoma. Ludwig submitted that the specification does not describe what genus of molecules work as antagonists, or what to do with them. However at page 8 the specification describes Flt4 or its extracellular domain, or an antibody to VRP as VRP antagonists. The specification also devotes pages 24 to 28 to a discussion of various standard methods for preparing and administering VRP and VRP antagonists for the treatment of various dysfunctional states and at page explicitly refers to Kaposi’s sarcoma when describing diseases amenable to treatment with VRP or VRP antagonists. As such, I am satisfied that the specification meets the requirements for full description as set out in Kimberly-Clark Australia Pty Ltd v Arico Trading International Pty Ltd.
PRIORITY
The pivotal issues in this decision reflect the closely run race between Genentech, Ludwig and HGS to isolate VRP. The closeness of this race is demonstrated in the following table, which provides the earliest priority (EPD), complete filing and publication (OPI) dates for the opposed application and for the two most relevant citations, which are patent applications filed by Ludwig and HGS respectively.
Application
EPD
Complete Filing
OPI
Applicant
714484
6 June 1995
6 June 1996
24 December 1996
HGS
711578
1 August 1995
1 August 1996
26 February 1997
Ludwig
710696
8 September 1995
30 August 1996
27 March 1997
Genentech
Both Ludwig and HGS submitted that 710696 was not entitled to rely on its earliest priority date of 30 August 1996 as a consequence of the amendments filed on 10 January 2002. These amendments altered the VRP peptide sequence by replacing the threonine residue at position 94 in figure 1 and SEQ ID NO 3 with a tyrosine. Both opponents submitted that the altered VRP comprising the tyrosine residue was not disclosed in the priority document or the specification as filed.
However, the VRP DNA sequences in figure 1, and in SEQ ID NO 2, in both the priority document and the specification as filed, have a TAT codon at position 94. TAT codes for tyrosine rather than threonine, with AC(TCA or G) being the standard codons for threonine. As such, although both documents misidentify the amino acid at position 94 as a threonine, both documents disclose a nucleic acid sequence that would necessarily encode a peptide with a tyrosine at position 94. There is also good reason to consider the nucleic acid sequence, rather than the amino acid sequence as the correct sequence. As explained by Mr Fitzpatrick at the hearing, both the priority document and the complete specification clearly state that the amino acid sequence is deduced from the nucleic acid sequence. Where there are inconsistencies between a nucleic acid sequence and its deduced amino acid sequence the skilled person would understand that the errors will have arisen from incorrect translation and can remedied by reference to nucleic acid sequence.
The question of errors in specifications and priority dates was considered in Merck and Co., Inc. v Sankyo Co., Ltd. (1992) 23 IPR 415 where the Judge considered whether an amendment to correct an error in the chemical formula of a compound amounted to disclosure of a new substance. Although this case relates to the allowability of an amendment to the complete specification, as confirmed by the Judge in Merck and Co., Inc. v Sankyo Co., Ltd the Courts have applied basically the same test when considering whether amendments introduce new matter into a complete specification and whether a complete specification is fairly based on the disclosure in a provisional specification.
In the case of Merck and Co.’s application the Judge held that a corrected formula did not amount to new matter because the reaction described in the specification as filed had always produced the compound represented by the corrected formula, irrespective of the compound originally having been misidentified. The Judge stated:
“The iso-propyl substituent had always been present in the starting materials and was always produced irrespective of it originally having been misidentified. I accept the evidence that in the circumstances, correcting the name of the substituent at the 25-position in the “b” compounds from n-propyl to iso-propyl did not mean that a new substance had been disclosed; it merely meant that the true structure had been determined. It follows, in my opinion, that the amendment made in the application as accepted did not result in the disclosure of any new matter.”
Similarly, in the current situation, the correct peptide had always been present in both the priority document and the specification as filed by reference to the nucleic acid sequences in figure 1 and SEQ ID NO 2 and as such correction of the error does not result in disclosure of a new peptide.
At the hearing Mr Yates referred to Case T0923/92-3.3.4, Boards of Appeal of the European Patent Office, Genentech, Inc. Decision 8 November 1995. In this case the board considered an application where DNA sequencing errors had led to differences between peptide sequences in two priority documents and in the complete specification as filed. The board held that claims to the peptide sequence were not entitled to the earlier priority dates because
“the skilled reader, while realizing that possibly some error were made in reporting the sequences, is not in a position to establish which one of the two reported sequences of human t-PA is the correct one”.
However, not withstanding that this is a European Patent Office decision the reasoning of which may not necessarily apply to Australian law, the decision relates to an application where sequencing errors led to an incorrect DNA sequence. This differs from the current case where there is no evidence of DNA sequencing errors and where the specification clearly discloses that the reference sequence was the nucleic acid sequence and that the peptide sequence was subsequently deduced from a translation of the nucleic acid sequence. As such I do not believe that this case has any bearing on the priority date of the opposed application.
Given this, I am satisfied that not only was the correct VRP peptide present in both the priority document and the specification as filed but also that the correct VRP peptide sequence could have been readily determined from the nucleic acid in both the priority document and the specification as filed. Given this, I am satisfied that the invention as claimed is entitled to the priority date of 13 March 1997.
NOVELTY
The basic test for novelty is the “reverse infringement” test as stated in General Tire & Rubber Co v Firestone Tyre & Rubber Co Ltd, (1972) RPC 457 at pages 485, 486.:
“If carrying out the directions contained in the prior inventor's publication will inevitably result in something being made or done which, if the patentee's patent were valid, would constitute an infringement of the patentee's claim”.
However, in applying this test regard must be given to whether the prior art publication has provided clear and unmistakable directions to do what patentee has claimed, as also stated in General Tire & Rubber Co v Firestone Tyre & Rubber Co Ltd at page 486.
"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."
Although both Ludwig and HGS detailed extensive lists of documents in their respective statements of grounds and particulars, only three citations were pursued at the hearing. Ludwig confined their submissions to AU 711578 and AU 694524 and HGS confined their submissions to AU 714484. As a consequence I have only provided a detailed discussion of these three citations. Of the remaining citations listed in the opponents’ grounds and particulars, one would only have been relevant if the opposed application were not entitled to its earliest priority date and the others do not disclose peptides with any significant similarity to VRP as defined in the specification.
All three of the citations pursued by the opponents are ‘whole of contents’ citations and can only be considered with respect to novelty. The prior art base with respect to “whole of contents” novelty is defined in Schedule 1 of the Patents Act 1990 in the following way.
ii.information contained in a published specification filed in respect of a complete application where:
A. if the information is, or were to be, the subject of a claim of the specification, the claim has, or would have, a priority date earlier than that of the claim under consideration; and
B. the specification was published after the priority date of the claim under consideration; and
C. the information was contained in the specification on its filing date and when it was published.
AU 711578
Ludwig submitted that all of the claims of the opposed application lacked novelty in light of the disclosure in 711578. 711578 was published in Australia on 26 February 1997, 17 months after the priority date of 710696. 711578 relies on 4 US priority documents 08/510133, 08/585895, 08/901132 and 08/671573, which were filed on 1 August 1995, 12 January 1996, 14 February 1996 and 28 June 1996 respectively. Only the first of these priority documents, 08/510133 was filed before the earliest priority date of the opposed application.
The complete specification of 711578 discloses VEGF-C, a protein whose peptide and corresponding nucleic acid sequences are identical to the VRP sequences disclosed in figure 1 of the opposed application. VEGF-C is characterised as a ligand for Flt4 and a mitogenic factor that is useful for treatment of vascular trauma and dysfunctional states relating to inappropriate VRP receptor activity. As such VEGF-C is highly relevant to the novelty of the claims.
However, 711578 can only be regarded as part of the prior art base for the purpose of ‘whole of contents’ novelty if it is entitled to its priority date. Entitlement to priority date requires that VEGF-C as disclosed in 711578 is fairly based on the VEGF-C peptide disclosed in the priority document. In the case of 711578, 711578 describes a VEGF-C peptide sequence containing the full 419 amino acids found in VRP, however the priority document 08/510133 describes a truncated VEGF-C sequence that is missing the N-terminal 69 amino acids of full length VEGF-C.
The issue that must be resolved here is whether the full length peptide was disclosed in the priority document.
In his declaration of 15 September 2003 Professor Alitalo, one of the inventors of 711578 confirms that a 1.2 kb cDNA clone disclosed in example 10 of 08/510133 contains the full length VEGF-C coding sequence. Example 11 in the priority document describes recombinant expression of this clone (pFLT4-L) and its ability to bind and stimulate Flt4 phosphorylation. This same peptide is further analysed in the complete specification of 711578, where figure 21 shows an expression product of a similar size to the recombinant VRP peptide described in the opposed application. Given this I am satisfied that the priority document discloses the full length VEGF-C nucleic acid and its corresponding peptide in the forms of the 1.2 kb cDNA and its recombinant expression product. As such, although the priority document incorrectly describes the sequence of the VEGF-C peptide, the peptide expressed from the 1.2 kb clone and disclosed in example 11 of the priority document represents full-length VEGF-C, and if sequenced would yield the full length sequence depicted in the complete specification of 711578. Given this, I am satisfied that 711578 is entitled to its priority date.
At the hearing Genentech also submitted that description of the clone in the priority document in terms of an internal designation as pFLT4-L and an unidentified Budapest Treaty deposit was insufficient disclosure for the purposes of supporting a whole of contents novelty. However this misapprehends the level of detail required in a priority document.
While UK law requires an enabling disclosure to establish a priority date (see Asahi Kasei Kogyo KK’s application [1991] RPC 485) Australian law appears to have no such requirement. The role of a priority document is to provide fair basis for a more detailed description of the same subject matter in the complete specification. As noted in Anaesthetic Supplies v Rescare Ltd 28 IPR 383 (at 401):
“All that the provisional specification needs to do is describe generally and fairly the nature of the invention, and not to enter into all the minute details as to the manner in which the invention is to be carried out. It is a mode of protecting the inventor until the time of filing the final specification. It is not intended to be a complete description of the invention, but simply to disclose the invention fairly, though in a rough state. The interval of time between the provisional and the final is intended to provide an opportunity of development and precise expression of the invention foreshadowed in the provisional.”
All that is required under Australian law is that the priority document provide fair basis for a more detailed description of the same subject matter in the complete specification. As stated in the recent High Court decision of Lockwood v Doric [2004] HCA 58, fair basis merely requires that the invention disclosed in the priority document is the same as that claimed in the complete specification. In the current circumstances the priority document meets this requirement in examples 10 and 11, where there is a description of the preparation of pFTLT4-L followed by recombinant expression of the full length VEGF-C peptide.
As such, I am satisfied that 711578 is entitled to its earliest priority date and that it represents part of the prior art base with respect to whole of contents novelty considerations for the opposed application.
Given this I am also satisfied that 711578 deprives claims 1-7, 15, 16, 19-26, 28-32, 39 and 40 of novelty.
711578 discloses not only a peptide that is identical to VRP but also recombinant expression of this peptide and its use to treat vascular trauma and endothelial disorders where there is aberrant Flt4 receptor activity, thereby disclosing subject matter that falls within the scope of claims 1-7, 15, 16, 24, 26 and 28-32.
711578 also discloses monoclonal antibodies that are reactive with the N-terminal region of VRP. Page 14 describes the process of generating monoclonal antibodies and page 51 and examples 19 and 21 teach use of a peptide corresponding to residues 84-100 of VRP to raise antibodies. Although the examples relate to the generation of polyclonal antibodies rather than monoclonal antibodies I am satisfied that the skilled person would readily apply the directions of page 14 to also prepare both monoclonal and polyclonal antibodies to the N-terminal region of VEGF-C, thereby disclosing subject matter that falls within the scope of claims 19-23..
Page 51 also discloses generating GST-VEGF-C fusions to be used for characterisation of VEGF-C. As explained by Ludwig’s expert Associate Professor Rogers, GST is routinely used as a tag to aid isolation of proteins of interest. As such 711578 discloses tag fusions that fall within the scope of claim 25.
Pages 10 and 14 of also 711578 disclose covalent modification of VEGF-C in the form of linking VEGF-C fragments by way of disulfide bonding (see page 10, lines 10-12) and covalent linkage to magnetic particles, radioactive agents, biotin and avidin (see page 14, lines 31-35). As such 711578 discloses subject matter that falls within the scope of claims 39 and 40.
Therefore, I am satisfied that 711578 provide clear an unmistakeable directions to subject matter that deprives claims 1-7, 15, 16, 19-26, 28-32, 39 and 40 of novelty.
Ludwig also submitted that 711578 deprived claims 8-14, 17 and 18 of novelty. These claims define pharmaceutical compositions comprising VRP and a further growth factor and methods of using such composition for the treatment of disorders associated with inappropriate VRP receptor function. However, there is no clear teaching in 711578 to combine VEGF-C with any other growth factor. Furthermore, there was nothing in the experts’ submissions to suggest that there was anything in the specification that would direct the skilled person to prepare such a composition. As such, I am not satisfied that 711578 discloses or teaches toward any compositions that fall within the scope of claims 8-14, 17 or 18.
At the hearing Ludwig also submitted that the claims did not exclude a further growth factor comprising an altered form of VRP, for example truncated forms and short peptides such as those disclosed at page 13 of 711578. Mr Yates explained that although claims 8, 9, 17 and 18 specified that the further cell growth factor must be “other than” the VRP of the claims, this did not necessarily preclude a VRP that was other than the specific VRP defined in the claims to which claims 8, 9, 17 and 18 were appended. However, even if this were to be the case I cannot find any clear teaching in 711578 to combine different forms of VEGF-C in a single pharmaceutical formulation.
Ludwig also submitted that claim 27 lacked novelty in light of 711578. Claim 27 defines a method of using a VRP antagonist to treat Kaposi’s sarcoma. Although 711578 discloses the use of VRP antagonists such as antibodies and truncated forms of VRP to treat a range of endothelial and vascular disorders there is no mention of Kaposi’s sarcoma or of any similar disorders, where tumour formation is associated with viral infections. As such, I can find no clear and unmistakeable directions to use a VRP antagonist to treat Kaposi’s sarcoma and I am not satisfied that 711578 discloses any method that falls within the scope of claim 27.
Ludwig submitted that the specific sustained-release preparations, microcapsules and gel formulations of claims 34 to 38 are also anticipated by the description in 711578 of pharmaceutical preparation comprising VEGF-C in association with any pharmaceutically-acceptable diluent, adjuvant, excipient or carrier. In support of this, Associate Professor Rogers, in his second declaration stated that the disclosure in 711578 “embraces and conveys (to a reader with average skill in the field) the specific vehicles recited in Genentech’s application”. However, it is not sufficient that a citation disclose a general class that would include the claimed subject matter, it must also be established that the skilled person would necessarily produce the claimed subject matter on reading the citation.
In the current circumstances, Ludwig has not provided any evidence to suggest that the skilled person would regard the citation as specifically teaching toward VEGF-C in a sustained release formulation, microcapsule or gel formulation as claimed. Given this, I have no evidence to suggest that the citation provides clear and unmistakeable directions to produce any formulations that fall within the scope of claims 34 to 38.
Therefore, I have no clear evidence that 711578 provides clear and unmistakeable directions to subject matter that falls within the scope of claims 8-14, 17, 18, 27 and 34.
In summary, I am satisfied that 711578 deprives claims 1-7, 15, 16, 19-26, 28-33, 39 and 40 of novelty. However I am not satisfied claims 8-14, 17, 18, 27 and 34 lack novelty in light of this citation.
AU 694524
Ludwig also submitted that claim 27 lacks novelty in light of the whole of contents disclosure in AU 694524 (694524). 694524 was published in Australia on 4 January 1996, 4 months after the priority date of 710696. 711578 relies on a single US priority document 247754, which was filed on 9 June 1994.
694524 discloses the Flt4 receptor and use of Flt4-binding compounds to treat conditions such as metastatic cancers, lymphomas, inflammation, infections and immunological disease. Ludwig submitted that as such the citation discloses compounds representing the VRP antagonists recited in claim 27. Although I accept that this is the case, as with 711578, Mr Yates could not direct me to any clear disclosure of Kaposi’s sarcoma in the citation or any information that would directly lead the skilled person to use Flt4-binding compounds to specifically treat Kaposi’s sarcoma. As such, I have no clear evidence that 694524 deprives claim 27 of novelty.
AU 714484
HGS focused much of their evidence and their submissions at the hearing on 714484. 714484 is also a whole of contents citation. It relies on a single US priority document 08/465968, which was filed on 6 June 1995, and it has an Australian publication date of 24 December 1996, 15 months after the priority date of 710696. However, in contrast to 711578 there was no dispute about 714484’s entitlement to rely on its earliest priority date, instead the dispute centred on HGS’ submission that the peptide disclosed in 714484 was the same as the VRP peptide in the opposed application.
The compete specification of 714484 discloses a peptide, VEGF2, whose sequence is identical to the VRP sequence disclosed in 710696 with the exception of the two amino acids at positions -18 and 394 in figure 1. In 714484 there is a serine at -18, in comparison to the leucine at this position in figure 1 of the opposed application, and a glutamine at position 394, rather than the lysine found in figure 1. HGS’ submissions were based on the assertion that these differences are immaterial and that as such VEGF2 and VRP should be regarded as essentially the same peptide.
It is worth noting that HGS was not suggesting that the differences in sequence between the two peptides were the consequence of a translation or sequencing error, rather their submissions centred on the assertion that the differences between the two peptides were “trivial and inconsequential” and had no material affect on properties of the peptide and that as such the two peptides should be regarded as essentially the same compound.
In support of their submissions that VEGF2 and VRP should be regarded as the same protein HGS directed me to Dr Rakoczy’s statement in her second declaration. Dr Rakoczy stated that there was “nothing in the HGS application (714484) or the Genentech application that leads me to believe that the differences that I note make any difference to the biological activity of the two identified proteins”. However, these comments focus on a biological activity associated with binding and stimulation of Flt4 phosphorylation and do not consider other functional properties, such as immunological properties, charge and stability.
HGS’ submissions also ignore the nature of the lysine/ glutamine substitution where a large positively charged amino acid is replaced with a smaller negatively charged amino acid, as well as the generally accepted view in the art that even minor substitutions may have a substantial impact on the chemical and physical properties of a peptide. As explained by the applicant’s expert Professor Grey even minor amino acid substitutions may have a significant and unpredictable effect on peptide structure and function.
This is also reflected in the European Board of appeal case, Case T0923/92-3.3.4, Boards of Appeal of the European Patent Office, Genentech, Inc. , which was discussed by Mr Yates in relation to the priority date of the opposed application. Where it was acknowledged that even a small structural modification (e.g. the substitution or deletion of one amino acid) can produce changes in structural and physico-chemical properties, which in turn will lead to changed functional characteristics.
As such, I do not believe that VEGF2 and VRP can be regarded as the same peptide, or even as two peptides with essentially the same functional characteristics. Although both peptides may share the ability to bind and stimulate phosphorylation of Flt4, this single activity is only one of the many functional characteristics that will define and distinguish each peptide. The presence of two amino acid differences between the proteins, particularly one difference that is a non-conservative, not only produces proteins with a different chemical structure, it is also likely to produce proteins with different structural and functional characteristics.
HGS also submitted that 714484 teaches proteins such as VRP through its disclosure of allelic variants and analogues of VEGF2 that retain the activity characteristic of VEGF2. However, a general disclosure of unspecified variants or derivatives will only anticipate a specific variant if it can be established that the prior art provides clear and unmistakeable directions to that specific variant or derivative. There are no such directions in 714484. Although 714484 discloses that VEGF2 includes fragments, derivatives and analogues of VEGF-C, including variants with at least 70% identity to the specific VEGF2 sequence disclosed in the citation, there is no disclosure of any specific variants and no teaching that would lead the skilled person directly to VRP.
HGS also submitted that the opposed application relates to a selection where 714484 has disclosed a class of compounds and Genentech has attempted to claim a new member of that class. HGS argued that if this were the case, the opposed application did not meet the requirements of a selection patent because it failed to disclose any unexpected advantage or unsuspected property associated with VRP. However, a requirement of the earlier disclosure is that it is enabling for the later member of the class. This is supported by the statement “all that is required is that the earlier publication is enabling for the described subject matter”, taken from Beecham Group Ltd (New Zealand/Amoxycillin) Application (1982) FSR 187, and to which HGS referred in their submissions on selection patents. As explained above, 714484 may provide the wherewithal to produce further variants and analogues of VEGF2 and to search for other members of what may be a larger class of compounds, however it does not enable the isolation or preparation of any specific VEGF2 variant or analogue. As such I do not believe that 714484 can be regarded as providing a generic disclosure. In agreement with Mr Fitzpatrick, I am of the opinion that 714484 simply discloses a new peptide, which is at best a new member of the previously disclosed larger class of VEGF proteins.
Given this, I do not believe that 714484 is relevant to the novelty of any of the claims that explicitly recite a peptide or nucleic acid comprising amino acids that span either the -18 or the 394 region disclosed in figure 1. This equates to claims 1-3 and 26, which recite peptides comprising residues 1 to 399, residues -20 to 399, a 351 amino acid peptide including residue 394 respectively and residues -20 to -1 respectively. This also includes claims 4, 5, 24-26, 28-33 and 35, which are dependent from claims 1-3.
This leaves independent claims 9, 18, 19, 27, 34, 36, 38 and 39, and dependent claims 10-14, 17, 20-23 and 37-40, which are not restricted to residues that span either -18 or 394. These claims simply recite VEGF-related protein or VRP and thus relates to VRP and VRP variants that although including at least some of the residues from figure 1 do not necessarily span the -18 or 394 regions.
Claims 9 and 18 define pharmaceutical compositions comprising VRP and a further growth factor and methods of using such composition for the treatment of disorders associated with inappropriate VRP receptor function. 714484 does not provide any clear directions to prepare pharmaceutical compositions comprising both VRP and a further growth factor. Although on page 26, 714484 discloses use of VEGF2 “in conjunction with other therapeutic compounds”, this does not provide a clear teaching to compounds with the specific properties of growth factors.
At the hearing Mr Catterns submitted that the requirement for an additional growth factor was nothing more than a “mere trivial addition or trimming”. However, this argument presupposes that the growth factor has no effect on the composition. HGS has not provided any evidence to support this argument. Furthermore, as explained by Professor Grey in his declaration in response to Ludwig’s submission, this argument is contrary to the disclosure at page 28 of the opposed specification, where the specification lists a range of growth factors that may be used in conjunction with VRP for “enhancing the activity of any of the growth factors, including VRP, in promoting cell proliferation and repair.”
Given this, HGS has failed to convince me that the growth factor is a trivial addition or trimming, or that 714484 provide clear and unmistakeable directions to a VRP formulation comprising a further growth factor. As a consequence I do not believe that 714484 deprives claims 9-18 if novelty.
Claims 19 to 23 define a monoclonal antibody which binds to residues -20 to 137 of VRP and use of this antibody to treat disorders associated with inappropriate activity of the VRP receptor. 714484 only provides a general disclosure of antibodies, both monoclonal and polyclonal at page 34 and does not direct the reader to generate antibodies to any specific portion of VEGF2. Given this there is nothing to direct the skilled person to generate antibodies toward any specific part of the VRP peptide, or to expect that antibodies raised against the entire peptide would be more likely to bind to the N terminal epitopes than to epitopes present at other parts of the peptide.
Thus, I am not satisfied that 714484 deprives claims 19-23 of novelty.
Claim 27 defines a method of using a VRP antagonist to treat Kaposi’s sarcoma. Although 714484 discloses the use of VRP antagonists such as antibodies and truncated forms of VEGF2 to treat a range of endothelial and vascular disorders including solid tumour metastasis, gliomas, retinopathy and chronic inflammation, this is an extremely broad range of conditions.
In their submissions at the hearing HGS argued that at the priority date of the application Kaposi’s sarcoma was classified as a solid tumour metastasis and that as such the skilled person would have understood Kaposi’s sarcoma to be included within this family of disorders. However, solid tumour metastases include a wide range of disorders arising from diverse causes and responding to widely differing preventative and therapeutic treatments and HGS did not provide evidence to show why the skilled person would be directed to select Kaposi’s sarcoma from this diverse group of solid tumours.
As such, I am not satisfied that 714484 deprives claim 27 of novelty.
Claims 34 to 37 disclose specific sustained-release preparations and microcapsules comprising VRP. HGS submitted that semi-permeable polymers and microcapsules were well know as the priority date of the application and that as such the skilled person would have readily perceived their suitability for use with VEGF2. However, as stated in relation to Ludwig’s submission on these claims, it is not sufficient that a citation disclose a general class that would include the claimed subject matter, it must also be established that the skilled person would necessarily produce the claimed subject matter on reading the citation. HGS has not provided any evidence to suggest that the skilled person would regard the citation as specifically teaching toward VRP in a sustained release formulation or microcapsule. Given this, I have no evidence to suggest that the citation provides clear and unmistakeable directions to produce the formulations of claims 34 to 37.
Claim 38 discloses a gel formulation comprising VRP and a water soluble polysaccharide or polyethylene glycol. In their submissions HGS referred to page 12 of 714484, where the citation describes fusing VEGF2 with polyethylene glycol. Although this is an explicit disclosure of administration of polyethylene glycol with VEGF2, the disclosure does not necessarily relate to a gel formulation. The disclosure relates to fusion of polyethylene glycol and VEGF2 for the purpose of extending the half life of the peptide but does not specify that the fusion is then administered as gel or suggest that the polyethylene glycol is fused in a manner that necessarily results in a gel product. HGS did not provide any submissions to suggest that the disclosure in 714484 inevitably extended, or taught to gel preparation and as such I am left with no clear evidence that the claim lacks novelty in light of 714484.
Claims 39 and 40 define covalently modified VRP. In particular claim 40 recites specific covalent modifications including glycosylation, derivatisation of lysine residues and addition of radioactive tags. 714484 at page 12 discloses fusion of VEGF2 with polyethylene glycol. This process normally involves addition of polyethylene glycol to activated amino acid residues such as activated lysine. Page 24 also discloses radioactive labelling of VEGF2 and page 20 glycosylation. As such 714484 clearly discloses the covalently modified peptides of claims 39 and 40, thereby depriving these claims of novelty.
In summary, HGS has not established that VRP and VEGF-C are the same protein, or provided me with clear evidence that 714484 discloses the subject matter of any of claim 1-38. However, I am satisfied that 714484 does disclose subject matter that falls within the scope of claim 39 and 40 and that these claims lack novelty in light of 714484.
MANNER OF MANUFACTURE
Both opponents submitted that at least claims 8-14, 17 and 18 did not define a manner of manufacture because they represented nothing more than a mere collocation of known ingredients. Claims 8 to 14, 17 and 18 relate to formulations comprising VRP in association with a further growth factor that is other than VRP. At the hearing Mr Yates directed me to page 28 of the specification where it is stated that “It is within the scope hereof to combine VRP therapy with other novel or conventional therapies (……….) for enhancing the activity of any of the growth factors, including the VRP, in promoting cell proliferation and repair”. Both Mr Yates and Mr Catterns submitted that this statement did not suggest any synergistic effect when VRP is used in combination with another growth factor, and as such there was no evidence of any interaction between the two growth factors to produce a result that is greater than the sum of the two parts.
The specification does not provide any further evidence of synergy or any examples or explanation to support synergy between VRP and a further growth factor. In addition none of Genentech’s experts have provided any further information concerning synergy that is specific to VRP or even to other VEGF growth factors. As such I have no evidence or information before me that suggests that there is anything other than an additive effect when VRP and another growth factor are used in combination. However, there is a further issue that needs to considered when assessing manner of manufacture. This is whether or not the various components of the claimed formulation were “known” at the priority date of the opposed application.
At the hearing Mr Fitzpatrick submitted that VRP was not known at the priority date because neither 711578 nor 714484 had been published at the priority date of the opposed application. As such VRP, VEGF2 or VEGF-C was not publicly available or known at this date. I agree with Mr Fitzpatrick in this respect, although a whole of contents disclosure may deprive a claim of novelty, the information in the disclosure cannot be regarded as ‘known’ in terms of a public disclosure if the information has not been published until after the priority date of the claim. Given this, neither opponent has established that claims 8-14, 17 and 18 simply define a collocation of know ingredients or integers or fail to define a manner of manufacture.
INVENTIVE STEP
Neither party provided any submissions on inventive step at the hearing or in their later rounds of evidence. Given this I have no evidence to show a lack of inventive step for the claims.
UTILITY
Although HGS amended their statement of grounds and particulars on 14 November 2004 to include this ground they did not pursue this matter at the hearing. As a consequence I have no evidence before me to suggest that the claims do not meet the requirements of s18(1)(c).
CONCLUSION
The opposition was partially successful on the ground of novelty, but was unsuccessful on all other grounds.
Claims 1-7, 15, 16, 19 to 26, 28 to 33, 39 and 40 lack novelty in light of 711578. The citation discloses peptides, nucleic acid constructs, expression systems and antibodies with the features defined in the claims
Claims 39 and 40 also lack novelty in light of 714484, which discloses a covalently modified peptide VEGF-related peptide with the features defined in this claim.
However, based on the evidence I have before me claims 8 to 14, 17, 18, 27 and 34 to 38 are novel.
Neither party provided any submissions on inventive step at the hearing or in their later rounds of evidence. Given this I have no evidence to show a lack of inventive step for the claims.
In addition, neither opponent has provided me with clear evidence that the claims or specification fail to meet the requirements for fair basis, full description, manner of manufacture or utility.
Given that there is clearly patentable subject matter remaining in the application I give the applicant 60 days to provide amendments to resolve the lack of novelty for claims 1-7, 15, 16, 19 to 26, 28 to 33, 39 and 40.
COSTS
Given the amendments made to the application during the opposition proceedings, the further amendments foreshadowed by the applicant at the hearing and the partial success of the opposition I believe that it is appropriate to award costs against the applicant.
TERRY MOORE
Delegate of the Commissioner of Patents
Patent attorneys for the applicant : FB Rice & Co., Melbourne
Patent attorneys for the opponents : Spruson and Ferguson, Sydney and Wray and Associates, Perth
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