Genetics Systems Corporation v United Biomedical Inc
[1993] APO 60
•12 October 1993
official notice
decision of a delegate of the commissioner of patents
Application: No. 597884 in the name of GENETICS SYSTEMS CORPORATION.
Title: Synthetic Antigens for the detection of AIDs-related disease
Action: Opposition under Section 59 of the Patents Act 1952 by UNITED BIOMEDICAL INC.
Decision: Issued . the opposition failed on the grounds of prior claiming, prior publication, obviousness and otherwise not novel, but, succeeds on the ground of lack of compliance with section 40. Claims to peptides from particular regions of a known viral sequence are not fairly based without a clear description and disclosure of the particular and specific sequence of amino acids of the fragments involved.
Costs awarded against Genetics Systems Corporation.
patents act 1990
decision of a delegate of the commissioner of patents
Re:Application No. 597884 by GENETICS SYSTEMS CORPORATION and an Opposition by UNITED BIOMEDICAL INC. under the Patents Act 1952.
Background
Patent application No. 597884 by Genetics Systems Corporation (Genetics) was lodged under the Patents Act 1952 on 21 April 1986 as a section 58B international application. It was advertised accepted under the Patents Act 1952 on 14 June 1990. A Notice of Opposition was filed on 12 September 1990 by United Biomedical Inc. (United). As a consequence, the opposition is proceeding as provided for in section 234(3) of the 1990 Act and regulation 23.3 of the 1991 Regulations.
All evidence stages were completed by 25 February 1993 and the matter heard in Canberra on 26 July 1993.
The grounds relied upon in the Notice of Opposition are subsections 59(1)(c) and (d) - prior claiming, 59(1)(e) - prior publication, 59(1)(g) - obviousness, 59(1)(h) - otherwise not novel and 59(1)(i) - lack of compliance with section 40 of the Patents Act 1952.
Genetics was represented at the hearing by Mr D Catterns QC of counsel supported by Mr P Jones and Dr D Yin Foo of Phillips Ormonde & Fitzpatrick (patent attorneys) Melbourne. United were represented by Dr A Bennett of counsel, Ms A Slayter of Shelston Waters (patent attorneys) Sydney and Coors Westgarth, Solicitors, Sydney.
THE SPECIFICATION
The specification is described on page 3 as relating to peptide sequences capable of immunologically mimicking proteins encoded in the gag and/or env regions of the LAV/HTLV-III retrovirus. They are reagents for use in the screening of blood and blood products for prior exposure to the retrovirus. The peptides are of at least 5 amino acids and can be used in various binding assays for the detection of antibodies to LAV/HTLV-III virus, for the detection of LAV/HTLV-III antigens, or as immunogens.
Amendments have been proposed, under section 104 of the 1990 Act, to limit the peptides used in the invention to those containing "8 to 50 amino acids in a sequence; said peptide having at least 8 contiguous amino acids" rather than "at least 5 amino acids in a sequence" as presently claimed.
As the proposed amendments are not as yet allowed I will consider the specification as unamended but will refer to the proposed amendments where necessary, to explain my decision.
There are 34 accepted claims.
The independent claims are as follows:
Claim 1.In a method for detecting the presence of LAV/HTLV-III virus or antibody to LAV/HTLV-III virus where a sample is combined with a composition having epitopic sites immunologically competitive with LAV/HTLV-III epitopic sites, whereby antibodies bind to said protein composition to form at least one specific binding pair complex and the amount of complex formation is determined, the improvement which comprises:
employing in the assay medium as a reagent said composition, containing at least one peptide which has at least five amino acids in a sequence which comes within the sequence of at least one of the following peptide sequences:
(I) (15)
Y-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu- Glu-Met-Met-Thr-Ala-Cys-X
(II) (17)
Y-Leu-Lys-Glu-Thr-Ile-Asn-Glu-Glu-Ala-Ala-Glu-Trp-Asp-Arg-Val-His- Pro-Val-His-Ala-Z-X
(III) (92)
Y-Asp-Arg-Val-His-Pro-Val-His-Ala-Gly-Pro-Ile-Ala-Pro-Gly-Gln-X
(IV) (90)
Y-Tyr-Ser-Pro-Thr-Ser-Ile-Leu-Asp-Ile-Arg-Gln-Gly-Pro-Lys-Glu- Pro-Phe-Arg-Asp-Tyr-Val-Asp-Arg-Phe-Tyr-Lys-Thr-Leu-Arg-Z-X
(V) (88)
Y-Asn-Trp-Nor-Thr-Glu-Thr-Leu-Leu-Val-Gln-Asn-Ala-Asn-Pro-Asp-Cys- Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu-Glu-Nor- Nor-Thr-Ala-Cys-X
(VI) (97)
Y-Arg-Glu-Leu-Glu-Arg-Phe-Ala-Val-Asn-Pro-Gly-Leu-Leu-Glu-Thr-Ser- Glu-Gly-Cys-Arg-Gln-Ile-Leu-Gly-Gln-Leu-Gln-Pro-Ser-Leu-Gln-Thr-X
(VII) (71)
Y-Asp-Thr-Gly-His-Ser-Ser-Cln-Val-Ser-Gln- Asn-Tyr
(VIII) (36)
Val-Lys-Ile-Glu-Pro-Leu-Gly-Val-Ala-Pro- Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg- Glu-Lys-Arg-Ala-Z-X
(IX) (56)
Ile-Lys-Gln-Leu-Gln-Ala-Arg-Ile-Leu- Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Gln-Gln-Z-X
(X) (39)
Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu-Lys- Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly-Cys- Ser-Gly-Lys-Leu-Ile-Cys-X
(XI) (40)
Y-Lys-Ser-Leu-Glu-Gln-Ile-Trp-Asn-Asn- Met-Thr-Trp-Met-Glu-Trp-Asp-Arg-Glu- Ile-Asn-Z-X
(XII) (23)
Y-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn- Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu- Glu-Leu-Asp-Lys-Trp-Z-X
(XIII) (79) Y-Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly- Cys-Ser-Gly-Lys-Leu-Ile-Cys-X,
where X is OH or NH2. and Y and Z, when present, are amino acids added to facilitate coupling, 35 and where said peptide is free of other peptides or conjugated to a macromolecule for which antibodies in human sera are substantially absent.
Claim 6. A method for determining the presence of antibodies to LAV/HTLV-III in a physiological fluid, said method comprising:
introducing a human serum, plasma or blood sample into a sample container coated at least in part with at least one peptide having at least five amino acids which comes within the sequence of at least one of the following peptide sequences:
(I) (15)
Y-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu- Glu-Met-Met-Thr-Ala-Cys-X
(II) (17)
Y-Leu-Lys-Glu-Thr-Ile-Asn-Glu-Glu-Ala-Ala-Glu-Trp-Asp-Arg-Val-His- Pro-Val-His-Ala-Z-X
(III) (92)
Y-Asp-Arg-Val-His-Pro-Val-His-Ala-Gly-Pro-Ile-Ala-Pro-Gly-Gln-X
(IV) (90)
Y-Tyr-Ser-Pro-Thr-Ser-Ile-Leu-Asp-Ile-Arg-Gln-Gly-Pro-Lys-Glu- Pro-Phe-Arg-Asp-Tyr-Val-Asp-Arg-Phe-Tyr-Lys-Thr-Leu-Arg-Z-X
(V) (88)
Y-Asn-Trp-Nor-Thr-Glu-Thr-Leu-Leu-Val-Gln-Asn-Ala-Asn-Pro-Asp- Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu- Glu-Nor-Nor-Thr-Ala-Cys-X
(VI) (97)
Y-Arg-Glu-Leu-Glu-Arg-Phe-Ala-Val-Ash-Pro-Gly- Leu-Leu-Glu-Thr-Ser-Glu-Gly-Cys-Arg-Gln-Ile- Leu-Gly-Gln-Leu-Gln-Pro-Ser-Leu-Gln-Thr-X
(VII) (71)
Y-Asp-Thr-Gly-His-Ser-Ser-Gln-Val-Ser-Gln- Asn-Tyr
(VIII) (36)
Val-Lys-Ile-Glu-Pro-Leu-Gly-Val-Ala-Pro- Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg- Glu-Lys-Arg-Ala-Z-X
IX) (56)
Ile-Lys-Gln-Leu-Gln-Ala-Arg-Ile-Leu- Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Gln-Gln-Z-X
(X) (39)
Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu-Lys- Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly-Cys- Ser-Gly-Lys-Leu-Ile-Cys-X
(XI) (40)
Y-Lys-Ser-Leu-Glu-Gln-Ile-Trp-Asn-Asn- Met-Thr-Trp-Met-Glu-Trp-Asp-Arg-Glu- Ile-Asn-Z-X
(XII) (23)
Y-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn- Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu- Glu-Leu-Asp-Lys-Trp-Z-X
(XIII) (79)
Y-Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly- Cys-Ser-Gly-Lys-Leu-Ile-Cys-X,
where X is OH or NH2 and Y and Z, if present, are amino acids added to facilitate coupling, wherein said peptides are free of other peptides or conjugated to a macromolecule for which antibodies in human sera are substantially absent; incubating for a sufficient time for complex formation to occur; and determining the formation of complex by employing a labelled specific binding protein which binds to said complex and provides a detectable signal.
Claim 11. A method for determining the presence of antibodies to LAV/HTLV-III in a physiological fluid, said method comprising:
combining a human serum, plasma or blood sample with at least one labelled peptide having at least five amino acids in a sequence which comes within the sequence of at least one of the following peptide sequences:
(I) (15)
Y-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu- Gly-Pro-Ala-Ala-Thr-Leu-Glu-Glu-Met-Met- Thr-Ala-Cys-X
(II) (17)
Y-Leu-Lys-Glu-Thr-Ile-Asn-Glu-Glu-Ala- Ala-Glu-Trp-Asp-Arg-Val-His-Pro-Val-His- Ala-Z-X
(III) (92)
Y-Asp-Arg-Val-His-Pro-Val-His-Ala-Gly-Pro- Ile-Ala-Pro-Gly-Gln-X
(IV) (90)
Y-Tyr-Ser-Pro-Thr-Ser-Ile-Leu-Asp-Ile-Arg- Gln-Gly-Pro-Lys-Glu-Pro-Phe-Arg-Asp-Tyr-Val- Asp-Arg-Phe-Tyr-Lys-Thr-Leu-Arg-Z-X
(V) (88)
Y-Asn-Trp-Nor-Thr-Glu-Thr-Leu-Leu-Val-Gln- Asn-Ala-Asn-Pro-Asp-Cys-Lys-Thr-Ile-Leu-Lys- Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu-Glu-Nor- Nor-Thr-Ala-Cys-X
(VI) (97)
Y-Arg-Glu-Leu-Glu-Arg-Phe-Ala-Val-Asn-Pro-Gly- Leu-Leu-Glu-Thr-Ser-Glu-Gly-Cys-Arg-Gln-Ile- Leu-Gly-Gln-Leu-Gln-Pro-Ser-Leu-Gln-Thr-X
(VII) (71)
Y-Asp-Thr-Gly-His-Ser-Ser-Gln-Val-Ser-Gln- Asn-Tyr
(VIII) (36)
Val-Lys-Ile-Glu-Pro-Leu-Gly-Val-Ala-Pro- Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg- Glu-Lys-Arg-Ala-Z-X
(IX) (56)
Ile-Lys-Gln-Leu-Gln-Ala-Arg-Ile-Leu- Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Cln-Gln-Z-X
(X) (39)
Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu-Lys- Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly-Cys- Ser-Gly-Lys-LeU-Ile-Cys-X
(XI) (40)
Y-Lys-Ser-Leu-Glu-Cln-Ile-Trp-Asn-Asn- Met-Thr-Trp-Met-Glu-Trp-Asp-Arg-Clu- Ile-Asn-Z-X
(XII) (23)
Y-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn- Gln-Gln-Glu-Lys-Asn-Glu-Gln-Glu-Leu-Leu- Glu-Leu-Asp-Lys-Trp-Z-X
(XIII) (79)
Y-Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly- Cys-Ser-Gly-Lys-Leu-Ile-Cys-X,
where X is OH or NH2 and Y and Z, if 25 present, are amino acids added to facilitate coupling, and said peptides are conjugated to a protein for which antibodies in human sera are substantially absent or unconjugated to a protein; incubating for a sufficient time for complex 30 formation to occur; and determining the formation of complex as a result of change in a detectable signal resulting from complex formation.
Claim 16. A peptide of the formula:
(I) (15)
Y-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu- Glu-Met-Met-Thr-Ala-Cys-X,
where X is OH or NH 2, and Y, if present, is an amino acid added to facilitate coupling, N-terminal acetylated I, and I linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 17. A peptide of the formula:
(II) (17)
Y-Leu-Lys-Glu-Thr-Ile-Asn-Glu-Glu-Ala-Ala-Glu-Trp-Asp-Arg-Val-His- Pro-Val-His-Ala-Z-X,
where X is OH or NH , and Y and Z, if present, are amino acids 2 added to facilitate coupling, N-terminal acetylated II, and II linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 18. A peptide of the formula:
(III) (92)
Y-Asp-Arg-Val-His-Pro-Val-His-Ala-Gly-Pro-Ile-Ala-Pro-Gly-Gln-X,
where X is OH or NH 2 , and Y, if present, is an amino acid added to facilitate coupling, N-terminal acetylated III, and III linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 19. A peptide of the formula:
(IV) (90)
Y-Tyr-Ser-Pro-Thr-Ser-Ile-Leu-Asp-Ile-Arg-Gln-Gly-Pro-Lys-Glu-Pro- Phe-Arg-Asp-Tyr-Val-Asp-Arg-Phe-Tyr-Lys-Thr-Leu-Arg-Z-X,
where X is OH or NH2, and Y and Z, if present, are amino acids added to facilitate coupling, N-terminal acetylated IV, and IV linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 20. A peptide of the formula:
(V) (88)
Y-Asn-Trp-Nor-Thr-Glu-Thr-Leu-Leu-Val-Gln-Asn-Ala-Asn-Pro-Asp-Cys- Lys-Thr-Ile-Leu-Lys-Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu-Glu-Nor-Nor- Thr-Ala-Cys-X,
where X is OH or NH2, and Y, if present, is an amino acid added to facilitate coupling, N-terminal acetylated V, and V linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 21. A peptide of the formula:
(VI) (97) Y-Arg-Glu-Leu-Glu-Arg-Phe-Ala-Val-Asn-Pro-Gly- Leu-Leu-Glu-Thr-Ser-Glu-Gly-Cys-Arg-Gln-Ile-Leu-Gly-Gln-Leu-Gln-Pro-Ser-Leu-Gln-Thr-X,
where X is OH or NH2 and Y, if present, is an amino acid added to facilitate coupling, N-terminal acetylated VI, and VI linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 22. A peptide of the formula:
(VII) (71)
Y-Asp-Thr-Gly-His-Ser-Ser-Gln-Val-Ser-Gln- Asn-Tyr
where Y, if present, is an amino acid added to facilitate coupling, N-terminal acetylated VII, and VII linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 23. A peptide of the formula:
(VIII) (36)
Val-Lys-Ile-Glu-Pro-Leu-Gly-Val-Ala-Pro- Thr-Lys-Ala-Lys-Arg-Arg-Val-Val-Gln-Arg- Glu-Lys-Arg-Ala-Z-X,
where X is OH or NH2 and Z, if present, is an amino acid added to facilitate coupling, N-terminal acetylated VIII, and VIII linked to a peptide or protein of at least 5,000 molecular weight, which 5 peptide or protein does not normally bind to antibodies present in a human host.
Claim 24. A peptide of the formula:
(IX) (56)
Ile-Lys-Gln-Leu-Gln-Ala-Arg-Ile-Leu- Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Gln-Gln-Z-X,
where X is OH or NH2 and Z, if present, is 15 an amino acid added to facilitate coupling, N-terminal acetylated IX, and IX linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 25. A peptide of the formula:
(X) (39)
Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly-Cys- Ser-Gly-Lys-Leu-Ile-Cys-X,
where X is OH or NH2 N-terminal acetylated X, and X linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 26. A peptide of the formula:
(XI) (40)
Y-Lys-Ser-Leu-Glu-Gln-Ile-Trp-Asn-Asn- Met-Thr-Trp-Met-Glu-Trp-Asp-Arg-Glu- Ile-Asn-Z-X,
where X is OH or NH2, and each of Y and Z, if present, is an amino acid added to facilitate coupling, N-terminal acetylated XI, and XI linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 27. A peptide of the formula:
(XII) (23)
Y-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn- Gln-Gln-Glu-Lys-Asn-Glu-Gln-Clu-Leu-Leu- Glu-Leu-Asp-Lys-Trp-Z-X,
where X is OH or NH2 and each of Y and Z, if present, is an amino acid added to facilitate coupling, N-terminal acetylated XII, and XII linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 28. A peptide of the formula:
(XIII) (79)
Y-Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly- Cys-Ser-Gly-Lys-Leu-Ile-Cys-X,
where X is OH or NH2 and each of Y and Z, if present, is an amino acid added to facilitate coupling, 30 N-terminal acetylated XIII, and XIII linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
Claim 29. A vaccine composition comprising at least one peptide of the peptides:
(I) (15)
Y-Asp-Cys-Lys-Thr-Ile-Leu-Lys-Ala-Leu- Gly-Pro-Ala-Alk-Thr-Leu-Glu-Glu-Met-Met- Thr-Ala-Cys-X
(II) (17)
Y-Leu-Lys-Glu-Thr-Ile-Asn-Glu-Glu-Ala- Ala-Glu-Trp-Asp-Arg-Val-His-Pro-Val-His- Ala-Z-X
(III) (92)
Y-Asp-Arg-Val-His-Pro-Val-His-Ala-Gly-Pro- Ile-Ala-Pro-Gly-Gln-X
(IV) (90)
Y-Tyr-Ser-Pro-Thr-Ser-Ile-Leu-Asp-Ile-Arg-Gln-Gly-Pro-Lys-Glu-Pro-Phe-Arg-Asp-Tyr-Val- Asp-Arg-Phe-Tyr-Lys-Thr-Leu-Arg-Z-X
(V) (88)
Y-Asn-Trp-Nor-Thr-Glu-Thr-Leu-Leu-Val-Gln- 25 Asn-Ala-Asn-Pro-Asp-Cys-Lys-Thr-Ile-Leu-Lys- Ala-Leu-Gly-Pro-Ala-Ala-Thr-Leu-Glu-Glu-Nor- Nor-Thr-Ala-Cys-X
(VI) (97)
Arg-Glu-Leu-Glu-Arg-Phe-Ala-Val-Asn-Pro-Gly- Leu-Leu-Glu-Thr-Ser-Glu-Gly-Cys-Arg-Gln-Ile- Leu-Gly-Gln-Leu-Gln-Pro-Ser-Leu-Gln-Thr
(VII) (71)
Asp-Thr-Gly-His-Ser-Ser-Gln-Val-Ser-Gln-Asn-Tyr
(VIII) (36)
Val-Lys-Ile-Glu-Pro-Leu-Gly-Val-Ala-Pro-Thr-Lys-Ala-Lys-Arg-Arg- Val-Val-Gln-Arg-Glu-Lys-Arg-Ala-Z-X
(IX) (56)
Ile-Lys-Gln-Leu-Gln-Ala-Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu- Lys-Asp-Gln-Gln-Z-X
(X) (39)
Arg-Ile-Leu-Ala-Val-Glu-Arg-Tyr-Leu-Lys-Asp-Gln-Gln-Leu-Leu-Gly- Ile-Trp-Gly-Cys-Ser-Gly-Lys-Leu-Ile-Cys-X
(XI) (40)
Y-Lys-Ser-Leu-Glu-Gln-Ile-Trp-Asn-Asn-Met-Thr-Trp-Met-Glu-Trp-Asp- Arg-Glu-Ile-Asn-Z-X
(XII) (23)
Y-His-Ser-Leu-Ile-Glu-Glu-Ser-Gln-Asn-Gln-Gln-Glu-Lys-Asn-Glu-Gln- Glu-Leu-Leu-Glu-Leu-Asp-Lys-Trp-Z-X
(XIII) (79)
Lys-Asp-Gln-Gln-Leu-Leu-Gly-Ile-Trp-Gly-Cys-Ser-Gly-Lys-Leu-Ile- Cys,
where X is OH or NH2, and each of Y and Z, when present, are amino acids added to facilitate coupling, or said peptides conjugated to an immunogenic protein, said peptides or conjugates being present in an amount to provide an immunogenic response together with a physiologically acceptable carrier.
Claim 33. A method for determining the presence of antibodies to LAV/HTLV-III in a physiological fluid, substantially as herein described with reference to the Experimental.
Claim 34. A method of inducing immunity against LAV/HTLV-III comprising administering a person with an immunity-inducing amount of a composition as defined in Claim 29.
EVIDENCE
Evidence-in-support consists of declarations by:
John Vivian Wells of 87 Barrie Street Kilara, New South Wales who holds "the positions of Senior Staff Specialist in Clinical Immunology and Director, AIDS Laboratory at Royal North Shore Hospital, St Leonards, New South Wales and Deputy Director, Kolling Institute of Medical Research";
Maria Michela Labbozzetta, of 39 Martin Place, Sydney, "a solicitor in the employ of Corrs Chambers Westgarth, solicitors".
David Craig Odbert, of 39 Martin Place, Sydney, "employed by Westgarth Middletons, solicitors".
David George Reeder, Acting Biomedical Librarian of the Biomedical Library of the University of New South Wales.
Barbara Irene Troy, Associate Librarian (Technical Services) of the University of Sydney.
John Robert Graham, Manager, General reference Library of the State Library of New South Wales, Macquarie Street, Sydney.
Evidence-in-answer consists of:
a declaration by Bruce Ernest Kemp of St Vincent's Institute of Medical Research, 41 Victoria Parade, Fitzroy, Victoria who is Deputy Director and Senior Research Fellow (National Health and Medical Research Council) at St Vincent's Institute of Medical Research.
Evidence-in-reply consists of:
a declaration by John Vivian Wells.
SUBMISSIONS
In summary Dr Bennett's major submissions for the opponent are as follows:
There is no new manner of manufacture within the meaning of section 6 of the Statute of Monopolies. Support for this concept can be gained from both Werner V Bailey Aluminium 13 IPR 513 (Lockhart J) and NV Phillips V Mirabella International 24 IPR 1 (Wilcox J). If you look at the specification itself it is apparent that there has not been an invention made . There were fragments and fragments were known to bind immunologically. Peptide sequencing was not a new technique.
The specification is insufficient to enable a proper working of the invention. There is no instruction or direction as to how to choose the sub-groups or sequences of the invention and no direction as to whether which will or will not work. There is no disclosure as to why other groups should be or were dismissed. The specification is silent on how to determine which of the thousands of peptide sequences included within the scope of the claims is immunoreactive. The selection of a sequence is a hit and miss process and not predictable (Wells 2/71-72). The applicant has not provided an explanation on how to select a sequence which is immunologically effective. It was not known at the priority date nor now, how a skilled addressee might accurately predict a sequence that fulfils the promise of immunological mimicking. (Wells 2/75). Accordingly, the claims must be limited to the specific 13 sequences.
Claims are not fairly based in that the only limitation to the claims is that the peptide has at least 5 amino acids of the sequence. There is no upper limit, so the entire HIV sequence is included in the claim, or indeed any other sequence. The proposed amendments do not stop extreme claiming - the number of amino acids is still not limited.
The specification is insufficient to enable a proper working as a vaccine or to induce immunity. Claims 29 to 32 and 34 claim the use of the peptides of sequences (I) to (XIII) as vaccines. The application contains no discussion of inducing specific cytotoxic T-cells with immunologic memory for function as vaccine or immunity inducing agent and this necessity was well known (Wells 1/20(d)).
The applicants are caught between prior publication and fair basis. Either a peptide sequence is unique or it is not. If the peptide sequence is not unique, then all the peptide sequences claimed are not novel in the light of the Wain-Hobson article which discloses the complete nucleotide and amino acid sequence of HIV virus. If the sequence is unique and Wain-Hobson does not prior publish the Genetics sequences, then the applicant can only lay claim to the precise peptide sequences disclosed, not to parts thereof. The Genetics claims are not fairly based as they claim specific sequences not disclosed.
The full amino acid sequence for the human HIV peptide sequence was prior published by the exhibited Wain-Hobson article and others. If it is permissible to claim an amino acid sequence that is within a disclosed sequence, the sequences exemplified and all of the sequences and possible sequences claimed are anticipated.
The specification discloses no more than a workshop improvement or working direction over the prior art consisting of Wain-Hobson and the known fragments of the HIV virus.
The invention as claimed is prior claimed by the claims of Australian Patent No 579467 in the name of United Biomedical Incorporated, see Wells 2/96 to 116.
In summary the major submissions from Mr Catterns were as follows:
The applicant's claims are fairly based. The claims are restricted to 13 well defined peptide sequences. Each peptide is utterly specified in combinations of 8 to 21 amino acids and fully supported. There is no lack of fair basis as there is no part where the claims go beyond the disclosure. The patentee only has to make a sound prediction and the applicant has done this.
Counsel for United has mixed up the concepts of utility and sufficiency. The invention as claimed is sufficiently described. It is clear that some embodiments will work better than others. It is implicit in the specification that all peptides will work to greater or lesser degrees.
Lack of utility is not a ground of opposition.
Manner of manufacture is not a ground relied upon in the Notice of Opposition. There is plainly a manner of manufacture within the meaning of Section 6 of the Statute of Monopolies.
The invention is not obvious. United has provided no proof of common general knowledge to establish that a skilled addressee would have arrived at the specific sequences of the invention at the priority date of the claims.
Lack of novelty has not been established because there is no document provided which contains all the essential integers claimed. The huge proteins were known but not the particular selections claimed. There is a long step between the AIDS virus and the fragments claimed.
The application is not prior claimed by any claims of Biomedical patent No 579467 as the priority dates of the claims are clearly supported by the basic documents and are earlier than the Biomedical claims.
DECISION
Prior published and otherwise not novel
Claims 16 to 28 are the broadest claims. Each claims a peptide represented by roman numerals I to XIII in which X is generally OH or NH2, and Y and Z, if present, is an amino acid, added to facilitate coupling. Optionally included are N-terminal acetylated peptides I to XIII, and peptides I to XIII linked to a peptide or protein of at least 5,000 molecular weight, which peptide or protein does not normally bind to antibodies present in a human host.
The essential feature of each of claims 16 to 28 is the particular sequence of amino acids claimed.
The alternatives, in these claims, for X, Y and Z, including the "linkage to a peptide or protein of at least 5000 molecular weight which does not normally bind to antibodies present in the human host", are optional and not essential features.
Claims 29 to 32 and 34 have as an essential feature, the peptides of claims 16 to 28. Claims 1 to 15 and 33 have as an essential feature permutations of the peptide sequences of claims 16 to 28.
The invention involves the use of particular peptide sequences, that are reactive with AIDS virus antibodies in the host in an immunologoically competitive manner, as a means of detecting the presence of the AIDS virus in a host.
The documents cited in relation to these grounds are:
Scupbach J et al, Serological Analysis of a Subgroup of Human T-Lymphotropic retroviruses (HTL - III) Associated with AIDS. Science 224:503:505;
Brun-Vezinet F et al, Detection of IgG Antibodies to Lymphadenophathy - Associated with the Virus in patients with AIDS or Lymphadenophathy Syndrome. Lancet 9 June 1984.
(iii)Kalyananaraman VS et al, Antibodies to the Core Protein Lymphadenophathy Associated Virus (LAV) accompanying patients with AIDS. Science 225:321 - 323.
Hann BH et al, Molecular cloning and characterisation of the HTLV - III virus associated with AIDS. Nature 312:166 - 169.
Shaw GM et al, Molecular Characterisation of Human T - cell Leukemia (Lymohotropic) Virus type III in the Acquired Immune Difficiency Syndrome. Science 226: 1165 - 1171.
Wain-Hobson S et al, Nucleotide Sequence of the AIDS Virus LAV. Cell 40:9 - 17 (January 1985).
(vii)Ratner et al, Complete Nucleotide of the AIDS virus, HTLV - III. Nature 313:277 - 284 (24 January 1985); and
(viii)Muesing MA et al, Nucleaic Acid structure and expression of the Human AIDS/lymphadenopathy retrovirus. Nature 313:450 - 458.
Barre-Sinoussi F et al, Isolation of a T-Lymphotropic Retrovirus from a Patient at Risk of Acquired Immune Deficiency Syndrome (AIDS). Science 220:868-871.
Popovic M et al, Detection, Isolation and Continuous Production of Cytopathic Retroviruses (HLTV - III) from Patients with AIDS and Pre-AIDS. Science 224:497-500.
Chang NT et al, Expression in Escherichia coli of Open Reading Frame gene segments of HTLV-III. Science 228:93-96.
(xii)Chang NT et al, An HLTV-III peptide produced by recombinant DNA is immunoreactive with sera from patients with AIDS. Nature 315:151-154.
(XIII)US Patent No. 4,520,113.
The basic test for anticipation is set out in Meyers Taylor Pty Ltd v Vicarr Industries Ltd (1977) CLR 228, at page 235. That is
"The basic test for anticipation or want of novelty is the same as that for infringement and generally one can ask oneself whether the alleged anticipation would, if the patent were valid, constitute an infringement" .
It follows from the reverse infringement test that if a citation discloses all the features of the claim, the claim will lack novelty. If the citation does not disclose all the features of the claim, the claim will still lack novelty provided the citation discloses all the essential features of the claim; but if the essential features are not disclosed in the citation, the claim is novel. (Nicaro Holdings v Martin Engineering 16 IPR 545, and Catnic Components Ltd v Hill and Smith Ltd (1982) RPC 183)
In General Tire & Rubber Company v. The Firestone Tyre & Rubber Company Limited and Others [1972] R. P.C. 457 at pages 485-486 it was stated by the Court of Appeal that
"... 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, this circumstance demonstrates that the patentee's claim has in fact been anticipated."
Again in Beecham Groups Limited's (Amoxycillin) Application [1980] R. P.C. 261 at page 287 the Court of Appeal stated
"In Flour Oxidizing Co. Ltd. v. Carr & Co. Ltd. [1908] 25 R.P.C. 428, Parker J., a judge of great authority in this branch of the law, said that to anticipate a claim in a later patent an earlier publication must contain clear and unmistakable directions to do something falling within the later claim, i.e. something which, if carried out after the date of the later patent would amount to an infringement of it."
None of the cited documents disclose the specific separated amino acid sequences claimed as essential features of Claims 16 to 38 or claims 29 to 32 and 34. I am also not satisfied that the part sequences claimed in claims 1 to 15, are disclosed in these documents.
In my view, the cited documents do not disclose "clear and unmistakable directions" to use the peptides of the opposed specification. The claims are therefore not anticipated by these documents.
Inventive step
The law in Australia in regard to obviousness under the 1952 Patents Act, was laid down in the High Court decision in Minnesota Mining and Manufacturing Company and Another v. Beiersdorf ( Australia) Limited, 144 CLR 253. This required that in order that an allegation of obviousness be made out it must be established that the information relied upon had become part of the common general knowledge, at the priority date of the application in suit, of those engaged in the particular art to which the invention belongs. At page 292, Aicken J. stated:
"The notion of common general knowledge itself involves the use of that which is known or used by those in the relevant trade. It forms the background knowledge and experience which is available to all in the trade in considering the making of new products, or the making of improvements in old, and it must be treated as being used by an individual as a general body of knowledge."
Further, in Allsop & Another v. Bintag Ltd., (1989) AIPC 90-615 at page 39331,
"Would the hypothetical non-inventive person skilled in the art faced with the problem have taken as a matter of routine whatever steps might have led from the prior art to the invention claimed?"
Wells, in paragraph 11(a) of his declaration dated 11 August 1991, says that
"The method of employing an antigen free of other peptides or conjugated to a macromolecule for which antibodies in human sera are substantially absent to measure immunoreactivity of a sample is a standard laboratory procedure well known in the Relevant Art during the Relevant Period ..."
Kemp agrees but contends in paragraph 34 that
"The invention relates to specific peptide sequences which mimic epitope sites which are immunologically competitive with LAV/HTLV-III epitope sites".
Wells in paragraph 141 of his second declaration says that
"the state of the art at the priority date evidences that immunoreactivity of peptides is not accurately predictable".
Kemp does not comment about the predictability of the immunoreactivity of peptides.
On balance, the evidence, in my view, leads away from a conclusion that "the hypothetical non-inventive person skilled in the art" would, as a matter of routine, have arrived at the specific peptide sequences of the invention, as claimed, with the common general knowledge at hand, and consequently does not satisfy the Allsop & Another v. Bintag Ltd. test (supra).
I have no clear expert evidence with which to draw the conclusion that "the hypothetical non-inventive person skilled in the art" in Australia at the priority date of the claims, given the sequence of the AIDS virus, would, as a matter of routine, have arrived at specific peptide sequences (I) to (XIII) as immunoreactive reagents for the methods claimed.
Therefore I find that the invention as claimed in claims 16 to 28 and the other claims by virtue of their relationship to claims 16 to 28 are not obvious.
Manner of new manufacture
Dr Bennett submitted that
"There is no new manner of manufacture within the meaning of section 6 of the Statute of Monopolies. Support for this concept can be gained from both Werner V Bailey Aluminium 13 IPR 513 (Lockhart J) and NV Phillips V Mirabella International 24 IPR 1 (Wilcox J). If you look at the specification itself it is apparent that there has not been an invention made . There were fragments and fragments were known to bind immunologically. Peptide sequencing was not a new technique".
In NV Phillips V Mirabella International 24 IPR 1, Wilcox J at page 35 says
"... it seems to me that it is not an invention, or a manner of new manufacture, for someone to specify the criteria required to be met, in the manufacture of a known product from known materials, in order to achieve vendability. As was said by Dixon CJ, Kitto and Windmeyer JJ in National Research Development Corp v Commissioner of Patents (1959) 102 CLR at 262: 'Unless invention is found in some new method of using the material or some new adaption of it so as to serve the new purpose, no valid patent can be granted"
NV Phillips V Mirabella International involved specifying desirable criteria for the use of known materials in a known process. In the opposed specification, as I have previously found, we are dealing with the non-obvious use of new materials.
Consequently, the opposed specification is distinguishable from the facts of NV Phillips V Mirabella International and I therefore find there is manner of new manufacture.
Prior claiming
United alleges the claims are prior claimed by the claims of United Australian Patent No 579467 (United patent). This patent is in force until 29 April 1994.
The opposed application is a convention application claiming earliest priority date of 29 April 1985 (US application No. 728052). The claims are also based on US application No. 767303 (19 August 1985) and US application No. 844485 (26 March 1986). I will consider whether the claims of the opposed specification are entitled to this date later.
The priority dates of the United patent are 11 September 1985 (USSN 774644), 4 March 1996 (USSN 837566) and 2 April 1986 (USSN 847102).
At the hearing Dr Bennett provided submissions on prior claiming in tabular form and referred to Wells' declarations. I gave the applicant the opportunity to provide comments on these submissions and the opponent an opportunity to provide comments in return.
In considering prior claiming I need to focus on which of the Australian United patent claims are likely to be prior claims and whether there is proper support for these claims in the United patent specification (see B.A.S.F. Aktiengesellschaft (Distler's) Application, (1977) FSR 137). Then I need to consider whether there is support in the basic documents for the relevant priority dates.
I have construed the claims of the United patent using the guidelines provided in Allen and Hanbury Ltd. (Hayes) Application, (1977) RPC 113. The only relevant sequence disclosed in the United patent is part of sequence (X), not the full sequence. The sequence is disclosed for all amino acids except for the last 5, that is, except -Gly-Lys-Leu-Ile-Cys.
I therefore find that none of the peptide sequences of claims 16 to 28 of the opposed application were claimed by any claim of the United patent before the earliest relevant priority date of the opposed specification or specifically disclosed in the United patent specification
The only question then, in my view, is to whether claims 1 to 15 are prior claimed by the claims of the United patent which include the part of peptide sequence (X). Basic document USSN 728052 discloses peptide sequence (X) and its use but not "parts" of peptide (X), as claimed in claims 1 to 15. Parts of peptide (X) were first disclosed in USSN 767303 on 19 August 1985. That is, peptides equivalent to peptide sequences (IXa) and (IXb) of claim 3 of the opposed specification. This is before the earliest priority date of the United patent (11 September 1985) and consequently I do no have to consider the matter further.
Therefore claims 1 to 15 of the opposed application are also not prior claimed by the United patent.
Section 40
Dr Bennett has been submitted that it is not clear whether the peptides of claims 16 to 28 are all reactive with antibodies in the host, although Kemp, in paragraph 41 of his declaration, says that he
"believes that peptides (I) to (XIII) ... are capable of acting as immunogens and antigens for example when conjugated to carriers to which antibodies can react."
It seems that I must accept the applicants statement that all these peptides are "reactive with AIDS virus antibodies in the host in an immunologoically competitive manner". To do otherwise would be to question inutility, in my view, and this not a matter for the opposition process.
Dr Bennett submitted that there has not been a method disclosed to show the addressee "how to select or locate a sequence with 5 or 8 or 12 or whatever amino acids which would be immunoreactive".
However, Wells in paragraph 9(c) of his first declaration says that
"The method of employing of peptide sequences derived from a virus to detect the presence of that virus or antibodies to it is a standard laboratory procedure well known in the relevant art during the relevant period."
Kemp in paragraph 34 of his declaration says that
"Whilst I agree that the utilization of peptide sequences from a virus to detect the presence of the virus was well known prior to the earliest priority date of the opposed specification .... The invention relates to specific peptide sequences which mimic epitope sites which are immunologically competitive with LAV/HTLV-III epitope sites".
Wells, also says in paragraph 141 of his second declaration that
"the state of the art at the priority date evidences that immunoreactivity of peptides is not accurately predictable".
I understand Kemp to mean that the opposed specification relates to a particular group of specific peptide sequences which have been found to have the desired property, that is, immunoreactivity with AIDS virus antibodies. I therefore understand the term "specific peptide sequences" to mean those peptides where the sequence of amino acids is specifically stated, that is sequences described in their entirety and not to subsets thereof. In this case, this is the peptide sequences (I) to (XIII), (VIIIa), (VIIIb), (IXa), (IXb) and (XIIIa).
Kemp does not comment about the predictability of the immunoreactivity of peptides.
The evidence, on balance, leads me to the conclusion that peptides do not appear to be predictably immunoreactive at the priority date of the claims. As Kemp says the invention relates to "specific peptide sequences". That is, in my view, to the peptide sequences (I) to (XIII) and (VIIIa), (VIIIb), (IXa), (IXb) and (XIIIa), and not to subsets thereof.
I can find nothing in the evidence to dissuade me from the view that while the specification is sufficient for the peptide sequences specifically described in their entirety, it is not sufficient for those peptide sequences claimed in claims 1 to 15 which have not been specifically described.
Dr Bennett submits that
"The applicants are caught between prior publication and fair basis. Either a peptide sequence is unique or it is not. If the peptide sequence is not unique, then all the peptide sequences claimed are not novel in the light of the Wain-Hobson article which discloses the complete nucleotide and amino acid sequence of HIV virus. If the sequence is unique and Wain-Hobson does not prior publish the Genetics sequences, then the applicant can only lay claim to the precise peptide sequences disclosed, not to parts thereof. The Genetics claims are not fairly based as they claim specific sequences not disclosed.
In Montecatini Societa Generale per L'Industrie Mineraria e Chimica v. Hercules Powder Company, (1962) AOJP p.2901, claims which included within their scope forms which had been neither described or exemplified, were found to be not fairly based on the specification. Similar findings were made in Colgate-Palmolive Co. v. Proctor and Gamble Co., Official Journal (1964) p.1041.
Also a claim should not be wider than the consideration. In The Mullard Radio Valve Co. Ld. v. Philco Radio and Television Corp. of Great Britain Ld., (1936) 53 RPC 323 at page 346:
"A patentee is granted his monopoly in order to protect the invention which in his specification he has communicated to the public. He is not entitled to claim a monopoly more extensive than is necessary to protect that which he has himself said is his invention ... If an inventor claims an article as his invention, but the article will only achieve his avowed object in a particular juxtaposition and his inventive idea consists in the discovery that in that particular juxtaposition it will give new and useful results, I do not think that he is entitled to claim the article at large apart from the juxtaposition which is essential to the achievement of those results."
In applying these rules, I agree with Dr Bennett that in this case, for the peptide fragments to be claimed as they are in claims 1 to 15, the combinations claimed must be clearly defined and peptide sequences must be specifically described in the specification. Unless there is sufficient description of the specific peptide sequences, the claims cannot be to "at least one peptide which has at least 5 amino acids ..." or as proposed "at least one peptide which has at least 8 to 50 amino acids ...", even with the limitations imposed within the claims.
The specification, see for instance pages 5 line 22 to page 7 line 1, is drafted in very broad terms relating to how "the subject polypeptides may be subject to various changes, such as insertions, deletions and substitutions, either conservative or non-conservative". Examples of peptide sequences resulting from these changes have not been described.
As the AIDS virus sequence is known the applicant is only entitled, in my view, to claim those "specific peptide sequences" actually discovered and described to have the properties of the invention. The "sound prediction" of Olin Mathieson Chemical Corp v Biorex (1970) RPC 157 at page 193, referred to in Mr Catterns submissions is, in my view, limited in these circumstances to the specific peptide sequences actually described.
In my view, the invention in the opposed specification relates to the use of specific peptide sequences. This was the rationale I used for finding the claimed invention to be novel and inventive. I can only find clear support for the inclusion of those peptides in claims 1 to 15 where the sequences of the peptides have been specifically disclosed. That is, peptides of sequences (I) to (XIII) and peptides (VIIIa), (VIIIb), (IXa), (IXb) and (XIIIa) as claimed in claim 3.
I do not find claims to peptides from particular regions of a known viral sequence to be fairly based without a clear description and disclosure of the particular and specific sequence of amino acids in the fragments involved.
Kemp at paragraph 42 of his declaration says that he
"or any other peptide scientist in Australia would have had no difficulty in carrying out these directions at the time".
That is, the instructions on page 20 lines 22-35 of the present specification to use the conjugated peptides as a vaccine. Wells in paragraph 166 of his second declaration says
"he does not believe that the directions at page 20 lines 22 to 35 of the opposed specification" are sufficient to allow the "skilled addressee to understand and work the invention".
At page 20, the opposed specification provides a brief description of the use of the peptides of the invention in vaccines.
In the absence of any evidence to clearly establish difficulties a skilled addressee would have in preparing vaccines from the information provided I accept Kemp's view and find that the description is sufficient in this regard.
I find Dr Bennett's submission that there is "no validation that any of Genetic's peptides form a protective antibody" not to be relevant to an opposition under the Patents Act because it relates to inutility.
CONCLUSION
I have found that the opposition has failed on the grounds of prior claiming, prior publication, obviousness and otherwise not novel, but, succeeds on the ground of lack of compliance with section 40.
I afford the applicant 60 days from the date of this decision to propose amendments to overcome the section 40 deficiencies.
Costs
Normally in actions of this nature costs follow the event. I have found that the opposition succeeded only in terms of the section 40 ground, but the defects are not minor and I see no reason to vary this practice. Consequently, I award costs against Genetics Systems Corporation.
(R.J.SAWYER)
Delegate of the Commissioner of Patents
Patent attorneys for the applicant: Phillips Ormonde & Fitzpatrick, Melbourne
Solicitors for the opponent: Coors Westgarth, Sydney
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