Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Status of the claims
Claims 1-29 are examined on merits in this office action.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1-29 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claims 1 and 27 recite “modified antibody” and “specific antibody” in the detection and suppression method steps. Claim 15 is directed to a detection reagent for detecting a target antigen requiring a “modified antibody” and a “specific antibody”. Specification teaches that “specific antibody in the present invention may be any antibody specific to antigen to be measured”. Thus as claimed, a specific antibody may include an antibody having single amino acid substitution in the light chain or heavy chain variable regions wherein the antibody is capable of specifically binding to the antigen. Therefore, without any binding specificity, the distinction between the modified antibody and the specific antibody in the detection process is unclear. The process of detection when the specific antibody and the modified antibody have the same binding specificity is unclear in the process of detection of claim 1.
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-29 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claim 1 is directed to a detection method and composition for detection of a target antigen in a sample by bringing simultaneously a modified antibody and a specific antibody specific for the antigen wherein the modified antibody is an antibody in which part or all of variable region of an antibody light chain (hereinafter abbreviated as L chain) and/or an antibody heavy chain (hereinafter abbreviated as H chain) of the specific antibody is modified. Claims 28 and 29 are directed to a specific antibody specific for the antigen wherein the modified antibody is an antibody in which part or all of variable region of an antibody light chain (hereinafter abbreviated as L chain) and/or an antibody heavy chain (hereinafter abbreviated as H chain) of the specific antibody is modified.
The instant claims are drawn to a broad genus of all monoclonal and polyclonal antibodies which binds to a large number of antigens. As claimed, the process, composition and antibody claims encompasses various monoclonal antibodies and polyclonal antibodies directed to various types on antigens wherein the monoclonal antibody or the polyclonal antibody have different types of modifications (substitution, insertion, deletion and attachment of other molecules) at part or all of the variable region of the light chain or heavy chain, for which the specification does not have a descriptive support with the scope of various antibodies directed to various antigens and various types of modifications as encompassed by the claims.
Throughout the specification, there are only two antibodies disclosed with only a few modifications at the variable regions wherein the antibody is strictly limited to monoclonal antibody directed to brain natriuretic peptide (BNP) and soluble interleukin-2 receptor (sIL-2R) wherein the specific modifications (substitution) significantly reduced reactivity of the antibodies as compared to the unmodified wild type antibody. For anti-BNP, the specification discloses one monoclonal antibody 33236 (produced by hybridoma NITE ABP-03799) wherein the antibody has been modified to a 33236-(W51A) (CDR2 WAS to AAS) modified antibody, a 33236-(CDR3-A) (CDR3 KQSYNLYT to AAAAAAAA) modified antibody and a 33236 - (K95A) (CDR3 KQSYNLYT to AQSYNLYT) modified antibody (paragraphs [0014], [0085] and Fig. 16). For anti-sIL-2R, the specification disclosed one monoclonal antibody 92204R (hybridoma with deposit # NITE BP-02123) wherein the antibody has been modified to 92204R-L-(CDR3-A) (L chain CDR3 amino acid replaced with alanine) antibody, modified to 92204R-H-(105-107-A) (H chain 105-107th amino acids replaced with alanine) modified antibody and modified to 92204R_H0394Δ105-107 (H chain 105-107th amino acids deleted) antibody, of which 92204R_H0394Δ105-107 and 92204R-L-(CDR3-A) antibody showed significant reduced reactivity (Fig 14).
An adequate written description must contain enough information about the actual makeup of the claimed products—“a precise definition, such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other materials,” which may be present in “functional” terminology “when the art has established a correlation between structure and function.” Ariad, 598 F.3d at 1350. But both in this case and in our previous cases, it has been, at the least, hotly disputed that knowledge of the chemical structure of an antigen gives the required kind of structure-identifying information about the corresponding antibodies. See, e.g., J.A. 1241 (549:5–16) (Appellants’ expert Dr. Eck testifying that knowing “that an antibody binds to a particular amino acid on PCSK9 . . . does not tell you anything at all about the structure of the antibody”); J.A. 1314 (836:9–11) (Appellees’ expert Dr. Petsko being informed of Dr. Eck’s testimony and responding that “[m]y opinion is that [he’s] right”); Centocor, 636 F.3d at 1352 (analogizing the antibody- antigen relationship as searching for a key “on a ring with a million keys on it”) (internal citations and quotation marks omitted).
Amgen Inc. v. Sanofi further notes, pointing to Ariad Pharms., Inc. v. Eli Lilly & Co., 94 USPQ2d 1161 (Fed Cir. 2010):
To show invention, a patentee must convey in its disclosure that it “had possession of the claimed subject matter as of the filing date.” Id. at 1350. Demonstrating possession “requires a precise definition” of the invention. Id. To provide this “precise definition” for a claim to a genus, a patentee must disclose “a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Id.
Amgen at pages 7-8.
Possession of a single species reading on the claimed genus does not put one in possession of any other antibodies. The common structural features that give rise to the desired functional properties are unknown. Recent court cases have indicated that recitation of an antibody which has specific functional properties (specific binding to antigens and competing with mutated versions) in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See AbbVie Deutschland GmbH v. Janssen Biotech. Inc. as well as Amgen v. Sanofi, as discussed above. Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not give the required kind of structure-identifying information about the corresponding antibodies, with the antibody-antigen relationship be analogized as a search for a key on a ring with a million keys on it. The description requirement of the patent statue requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736, F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate.”).
Therefore, the disclosure of two monoclonal antibodies specific for two specific antigens wherein the two monoclonal antibodies have few specific mutations with significant reduced reactivity, can not be considered representative of the inordinately a large number of antibody (monoclonal and polyclonal) having various mutations at various positions as encompassed by the claimed process and composition. Even for monoclonal antibody specific for BNP and sIL-2R, the specification does not have a representative example of various monoclonal antibodies directed to various epitopes on the designated proteins as each monoclonal antibody is distinct with respect to epitope selectivity and the CDR light and heavy chain variable sequences and thus the same amino acid mutation may not be applicable. A single polyclonal antibody is not a representative of the genus of polyclonal antibodies and genus of various mutations as encompassed by the claims.
The instant claims attempt to claim every antibody that binds different epitopes on different antigens and claiming every type of mutations on the light and heavy chain variable domains on the genus of antibodies. However, a description of a genus of antibodies may be achieved by means of a recitation of a representative number of antibodies, defined by sequence, falling within the scope of the genus or of a recitation of structural features common to the members of the genus, which features constitute a substantial portion of the genus. The written description requirement can be met by showing that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics ....i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. The court found that if the disclosed species only abide in a corner of the genus, one has not described the genus sufficiently to show that the inventor invented, or had possession of, the genus. He only described a portion of it. The specifically defined antibody sequences of two monoclonal antibody are not representative of nor predictive of any and all other antibody sequences for the broadly claimed genus. There is no common/shared structure among the antibodies having the claimed binding function.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 28 and 29 are rejected under 35 U.S.C. 102(a1) as being anticipated by Tomoyuki et al. (JP2020196741).
Claim 28 is directed to a non-specific reaction inhibitor which is an antibody in which part or all of the variable region of L chain and/or H chain of the specific antibody is modified. The recitation “used to together with a specific antibody …… in a sample” is an intended use claim of the antibody, which is considered not a part of the claimed antibody. Moreover, the recitation “A non-specific reaction inhibitor” recited in the preamble is preamble, is also considered an intended use of the antibody. Similarly the recitation “used to together with a specific antibody …… in a sample” is considered an intended use claim of the claimed antibody. An intended use that merely states the purpose of the claimed subject matter, without adding additional structure to it, is generally not treated as limiting the scope of the claim. See Boehringer Ingelheim Vetmedica, Inc. v. Schering-Plough Corp., 320 F.3d 1339, 1345 (Fed. Cir. 2003); Rowe v. Dror, 112 F.3d 473,478 (Fed. Cir. 1997). If the prior art structure is capable of performing the intended use, then it meets the claim.
Therefore, both claims 28 and 29 are directed to an antibody in which part or all of the variable region of L chain and/or H chain of the antibody is modified.
Tomoyuki disclosed antibody in which having heavy chain variable region or the light chain variable region contains amino acid modifications. Tomoyuki teaches that the position for introducing the amino acid modification is preferably a heavy chain variable region, and more preferable regions include a region exposed to the solvent and a loop region in the variable region. Of these, CDR1, CDR2, CDR3, FR3 regions, and loop regions are preferable (see Title and Description of Embodiment). Therefore, the reference is deemed to anticipate the antibody of claims 28 and 29.
Claims 28 and 29 are rejected under 35 U.S.C. 102(a1) as being anticipated by Igawa et al. (US 8562991).
Claim 28 is directed to a non-specific reaction inhibitor which is an antibody in which part or all of the variable region of L chain and/or H chain of the specific antibody is modified. The recitation “used to together with a specific antibody …… in a sample” is an intended use claim of the antibody, which is considered not a part of the claimed antibody. Moreover, the recitation “A non-specific reaction inhibitor” recited in the preamble is preamble, is also considered an intended use of the antibody. Similarly the recitation “used to together with a specific antibody …… in a sample” is considered an intended use claim of the claimed antibody. An intended use that merely states the purpose of the claimed subject matter, without adding additional structure to it, is generally not treated as limiting the scope of the claim. See Boehringer Ingelheim Vetmedica, Inc. v. Schering-Plough Corp., 320 F.3d 1339, 1345 (Fed. Cir. 2003); Rowe v. Dror, 112 F.3d 473,478 (Fed. Cir. 1997). If the prior art structure is capable of performing the intended use, then it meets the claim.
Therefore, both claims 28 and 29 are directed to an antibody in which part or all of the variable region of L chain and/or H chain of the antibody is modified.
Igawa teaches antibody molecules that bind to IL-6 receptor (Title). Igawa teaches amino acid substitutions in variable region CDRs (Fig. 1, 3,8). Igawa teaches that one or more amino acids may be substituted, deleted and/or inserted in the CDR sequences (col. 13, line 49 to col.14, line 40.). Therefore, the reference is deemed to anticipate the antibody of claims 28 and 29.
Conclusion
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/SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
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