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
Election/Restrictions
Applicant’s election without traverse of Group I, claims 3, 5, 8, 10-15, 18-19, and 23 and species: SEQ ID NOs: 1, 7, 3, 4, 5, 6, 22, 23, 26, and 27, (Fab’)2 fragment, and a method for preventing or treating a B7-H3-related disease or disorder in the reply filed 03/06/2026 is acknowledged.
Claims 21-22 are withdrawn from consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions and species, there being no allowable generic or linking claims. Election was made in the reply filed 03/06/2026.
Claims 3, 5, 8, 10-15, 18-19, and 23 are now under consideration in the instant Office Action.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code, www. See MPEP § 608.01. Specifically page 14 of the disclosure states: “available at http://www.gcg.com” twice.
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 3, 5, 8, 10-15, 18-19, and 23 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.
Instant claims 3, 5, 8, 10-15, 18-19, and 23 recite the CDRs and heavy and light chain variable region sequences of the claimed antibody as “… an amino acid sequence set forth in SEQ ID NO:…” It is unclear what is meant by “an amino acid sequence set forth in” as the use of “an amino acid” broadens the scope of the claim as it does not explicitly define all embodiments of the sequence. For example, this terminology of “an amino acid” can be interpreted as a subset of amino acids contained within the listed sequence identity number. Applicant is encouraged to amend the claim language to read as “…comprising SEQ ID NO:…” or “…comprising the amino acid sequence of SEQ ID NO:…” at every iteration to obviate this rejection.
Instant claims 3, 5, 8, 10-15, 18-19, and 23 recite both transitional phrases “comprises” and “consists of” in the claims to encompass the sequences for the antibody. The scope of the claim is unclear because both of the terms denote different scopes and cannot be used interchangeably. Applicant is encouraged to select one of the terms and adjust the language claiming the amino acid sequences accordingly.
Instant claims 10, 14-15, 19 recites the term “optionally”. The phrase “optionally” is interpreted as "for example" which renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. For the purposes of examination, the instant claims will be interpreted without the optional limitations as they are not required or claimed as necessary to the invention.
Claim Rejections - 35 USC § 112
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 3, 5, 8, 10-15, 18-19, and 23 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.
Claims 3, 5, 8, 10-15, 18-19, and 23 are directed to any antibody that binds to B7-H3. As such, the claim is directed to an antibody defined entirely by function (binding). See MPEP §2163(I)(A) which states:
"The claimed invention as a whole may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art recognized correlation or relationship between the structure of the invention and its function. A biomolecule sequence described only by a functional characteristic, without any known or disclosed correlation between that function and the structure of the sequence, normally is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence.”
In this case, antibodies generally share certain characteristics such as Fc regions or hinge regions. However, these structures are not correlated with the binding function of the antibody. The hyper variable regions (HVRs), i.e., complementarity determining regions (CDRs) of an antibody, are well established in the art as the portion of the binding region which imparts the specificity of an antibody. However, there is no way to a priori look at an antigen sequence (B7-H3) and envisage the combination of six CDRs that will bind that antigen. First, even highly related CDRs may not bind the same target. See for example Kussie (instant PTO-892) who demonstrates that a single amino acid change in the heavy chain of an antibody which binds p-axophenylarsonate (Ars) completely abrogates the ability of the antibody to bind Ars but adds the functionality of binding the structurally related p-azophenylsulfonate (e.g., abstract). Second, even when provided with several related antibodies that bind the desired target, this does not represent the astronomical and potentially unknowable breadth of all possible amino acid sequences which will result in the desired binding properties. This is exemplified by the Court decision in Abbvie (Abbvie v Janssen 759 F.3d 1285 (Fed. Cir. 2014)), where Abbvie developed over 200 antibodies that shared 99.5% identity in the variable regions (p.7) and which bound the target, but in no way allowed one to envisage the unique structure of Centocor’s antibodies which bound the same target but shared only 50% sequence similarity (see table on page 11).
Thus, the art recognizes that the CDRs define the binding properties of an antibody and that even single amino acid changes to this region can completely abrogate the binding specificity of an antibody. As a further example, see Chen et al., 1995 (instant PTO-892) which demonstrates single amino acid changes in the VH CDR2 sequence can increase binding, decrease binding, destroy binding, or have no effect on binding when compared to the wild-type antibody.
See also Koenig 2017 (instant PTO-892), which provides a large mutation analysis study where every amino acid in both variable regions are substituted with every other amino acid. Looking at figure 1 of Koenig, the bottom half of each section (labeled VEGF) relates to the ability of the mutant to bind the original target, with blue meaning a reduced affinity and black meaning a complete loss of binding ability. In VH-CDR2, for example, mutating any given residue to cysteine, which is encompassed by the instant claims, resulted in reduced binding at 12 residues and a complete loss of binding at 5 residues. That is, at 100% of the positions, mutation to cysteine reduced or ablated the antibody’s ability to bind the target. Looking at a specific position, in 100% of the mutations of residue 55, binding was reduced (15/19) or eliminated (4/19). While residues 56-65 appear more tolerant of change, residues 50-55 are generally intolerant of change.
It is appreciated that Koenig is studying one specific antibody and there is no evidence that the instant antibodies would react in the same way. However, this is part of the problem. It is entirely unclear from the specification which residues of Applicant’s CDRs are tolerant or intolerant to change, and whether those tolerant positions are only tolerant to conservative mutations. The fact that some residues might tolerate mutation does not convey to the skilled artisan that Applicant knew which of the claimed residues were tolerant of such, i.e., does not convey that Applicant was in possession of those sequences which are mutated yet preserve the claimed function. In other words, the specification fails to convey possession of an invention commensurate in scope with what is now claimed and therefore fails to meet the written description requirement. Looking at Koenig figure 2A, ~200 mutations in the CDR region of the VH chain completely abrogates any binding. While 2B appears to indicate that the CDRs of VL are more tolerant of change than the heavy chain CDRs, still over half of the mutations reduce binding compared to the parent.
Thus, making changes to the CDR sequence of an antibody is a highly unpredictable process and the skilled artisan could not a priori make any predictions regarding such mutations with any reasonable expectation of success nor envisage the breadth of structurally unrelated CDR combinations that would still possess the required functions.
The specification discloses several antibody sequences in Tables A-C on pages 22-25. However, as discussed above, without any way to determine how broad the genus of such antibodies are, there is no way to determine if these antibodies represent the full breadth of what is claimed. The disclosure of these specific antibodies would not convey to the artisan that Applicant was in possession of the full genus of all antibodies which possess the required functions nor does it allow the skilled artisan to envisage the specific structure of such antibodies.
Instant claims 3, 5, 8, 10-15, 18-19, and 23 recite the heavy and light chain CDRs and variable region sequences of the antibody that binds to B7-H3 with the terminology “an amino acid sequence set forth in”. There is no limitation or exclusion in the claim language that prevents the modifications from occurring within the CDR region due to the claim language of “an amino acid sequences set forth in”, which widens the scope of the claim to encompass an immense number of unknown molecules that share some identity to the claimed sequences and can bind to the claimed receptor. Applicant has not demonstrated that they are in possession of all the molecules that fall within the immense scope of the claim that are able to achieve the claimed function.
The use of “an amino acid sequence set forth in” can be interpreted as comprising the whole sequence or only comprising some of the amino acids contained within the sequence. As currently recited, the language of “an amino acid sequence” reads on less than the amino acids listed in the sequence identity number that are capable of binding to any isolated antigen. The minimum requirement of any sequence that would meet the limitations of the claim as written only requires a few amino acids in common with the claimed sequence. There is a lack of support for all of the potential amino acid sequence as claimed that is capable of binding to any antigen as written. Applicant is encouraged to amend the claim language to “… region comprising the amino acid sequence of SEQ ID NO: … ” in the instant claims to obviate this rejection.
Further note the decision in Amgen v. Sanofi 2017, where the Court supported previous decisions (Centocor 2011; Abbvie 2014) that defining an antibody solely by what it binds does not satisfy the written description requirement, stating that this would allow patentees to “claim antibodies by describing something that is not the invention, i.e., the antigen”. This decision has precipitated guidance to the Office instructing that the portion of MPEP 2163 regarding the “newly characterized antigen test” (indicating a well-characterized antigen is sufficient to satisfy written description for antibodies which bind that antigen) should no longer be used and that contrary materials should not be relied upon as reflecting the current state of the law.
It is appreciated that certain claims do include at least one CDR, e.g., claim 1 requires any one CDR or “an amino acid sequence set forth” of that one CDR, with the sequence interpreted as being open to modification due to the open claim language to include no particular structure so long as the function is retained.
However, as above, arbitrarily altering any amino acid in the CDR of an antibody is unpredictable and the specification does not convey possession of any CDRs other than those of the disclosed antibodies. Further, it is well-known in the art that specificity of an antibody stems from the interaction of six CDRs. Moreover, CDRs are not generally recognized as interchangeable, such that using one CDR from one antibody would not be reasonably expected to confer the same binding properties or even the same binding target when combined with two to five CDRs from other antibodies. For example, WO 2008068048 (instant PTO-892) discloses an antibody with a heavy chain comprising three CDRs (SEQ ID NO: 2) that binds secreted aspartyl protease from Candida sp. US 20170355756 (instant PTO-892) describes the same three CDRs in the heavy chain (C10-VH3) combined with a different light chain that binds human TDP-43. There is no evidence in the instant specification that a single CDR placed in the context of two to five other CDRS, regardless of what those other CDRs are, would result in the required function, nor that a single chain is correlated to the required function when combined with any other chain. As such, the specification fails to set forth a structure-function correlation sufficient to claim all possible antibodies defined by function and one-three CDRs or alterations thereof.
As such, the disclosure of two antibody sequences does not convey possession of other antibodies with the same binding properties; possession of the precisely defined sequence of six CDRs is required.
With respect to product claims 3, 5, 8, 10-15, 18-19, and 23, it is recognized that information which is well known in the art need not be described in detail in the specification (MPEP §2163(II)(A)(2)). See, e.g., Hybritech, Inc. v. Monoclonal Antibodies, Inc., 802 F.2d 1367, 1379-80, 231 USPQ 81, 90 (Fed. Cir. 1986). However, sufficient information must be provided to show that the inventor had possession of the invention as claimed. MPEP §2163(II)(A)(3)(a) also discusses Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004), where a method of using a PGHS-2 inhibitor did not meet the written description as the inhibitor itself was not sufficiently described, clearly indicating that written description of the compound is still required in a method of using that compound. In this case, it is clear from the specification that the invention is in a new antibody, or at the least disclosure of a new antibody that could not have been envisaged from the prior art indicates that the prior art was not in possession of all “B7-H3 antibodies”. Thus, the prior art cannot provide sufficient written description of this genus of compounds and the specification as filed, disclosing one antibody, does not sufficiently describe the genus either as there is an unknown amount of structurally distinct antibodies in this genus (see Amgen and Centocor decisions discussed above).
To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Vas-Cath, Inc., v. Mahurkar, 935 F.2d at 1563, 19 U.S.P.Q.2d at 1116. The claimed invention as a whole may not be adequately described where an invention is described solely in terms of a method of its making coupled with its function and there is no described or art-recognized correlation or relationship between the structure of the invention and its function. An antibody described only by functional characteristic, such as antibody that binds B7-H3 or one of the claimed epitopes, without any known or disclosed correlation between that function and the structure of the sequence, is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the biomolecule of interest. In re Bell, 991 F.2d 781, 26 U.S.P.Q.2d 1529 (Fed. Cir. 1993). In re Deuel, 51 F.3d 1552, 34 U.S.P.Q.2d 1210 (Fed. Cir. 1995). In the instant case, the specification provides insufficient direction or guidance concerning the relationship between the structure of the possible antibody to demonstrate possession of the breadth of the genus of B7-H3 antibodies encompassed by the instant claims, especially in view of the unpredictability of such an endeavor. The prior art as evidenced by Edwards et al., 2003 (instant PTO-892) teaches there is a substantially huge antibody diversity produced to one single antigen target. Edwards provides evidence that over 1000 antibodies, all different amino acid sequences, were generated towards one single protein antigen target (see abstract). Without a correlation between structure and function, the claims do little more than define the claimed invention by function. That is not sufficient to satisfy the written description requirement. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406 (“definition by function … does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is”).
Without this guidance or direction the skilled artisan would not consider applicant to be in possession of the claimed genus of antibodies because the skilled artisan recognizes that even seemingly minor changes made without guidance or direction as to the relationship between the particular amino acid sequence of the instantly claimed antibody and its ability to bind antigen, can dramatically affect antigen-antibody binding.
Applicant has not described the claimed invention sufficiently to show they had possession of the claimed genus of an antibody that binds B7-H3. Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester v. G.D. Searle & Co., 358 F.3d 916, 69 USPQ2d 1886 (Fed. Cir. 2004).
The written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
What constitutes a "representative number" is an inverse function of the skill and knowledge in the art. Satisfactory disclosure of a "representative number" depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features of the elements possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.
To provide adequate written description and evidence of possession of the claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. In the instant case, the only factors present in the claims are a recitation of one generic, broad genus that encompassed a diverse and huge number of possible antibodies that bind the disclosed epitope. The specification does not provide a consistent structure for all of the possible antibodies and fails to provide a representative number of species for the claimed genus. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus.
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111, clearly states that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that they invented what is claimed.” (See Vas-Cath at page 1116).
With the exception of specifically disclosed antibodies with specific CDRs, the skilled artisan cannot envision the detailed chemical structure of all of the encompassed antibodies, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The product itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016.
One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF's were found to be unpatentable due to lack of written description for that broad class. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Therefore, claims 3, 5, 8, 10-15, 18-19, and 23 do not meet the written description requirement.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 3, 10-15, 18-19, and 23 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by AbbVie Inc. (CN 109963870 A published July 2, 2019, in IDS filed 10/31/2024).
As noted above, the instant claims contain indefinite and written description issues regarding the sequences for the antibody or antigen-binding fragment. The broadest reasonable interpretation of the claims as recited, given that the sequences for the antibody are not fully defined, is any antibody or antigen-binding fragment that binds to B7-H3. The claims will be examined in the following rejection according to this interpretation.
AbbVie Inc., in examples 3-7 and 9-11, discloses that a murine anti-B7-H3 monoclonal antibody is prepared with a mouse fibroblast cell line expressing full-length human B7-H3 and a recombinant human or mouse B7-H3-ECD-human Fc fusion protein as immunogens, and the antibody can bind to human and cynomolgus monkey B7-H3; and murine variable regions are expressed in mammalian host cells in the context of a human immunoglobulin constant region to provide chAb18 chimeric antibodies, the VH (SEQ ID NO: 32), VL (SEQ ID NO: 28), LCDR1-3 (SEQ ID NOs: 29-31) and HCDR1-3 (SEQ ID NOs: 25-27) sequences are shown in Table 4, and chAb18 can bind to human non-small cell lung cancer cell line NCI-H1650 that overexpresses B7-H3. AbbVie Inc. teaches that the anti-B7-H3 antibody is of the IgG isotype, more specifically the antibody or antigen-binding portion thereof is of the IgG1 or IgG4 isotype, see reference’s claims 7-8. AbbVie Inc. discloses the anti-B7-H3 antibody or antigen-binding fragment in a pharmaceutical composition, and a pharmaceutically acceptable carrier. This meets the limitations of instant claims 3 and 23 wherein the sequences are for an antibody or antigen-binding fragment binds to B7-H3, instant claim 10 wherein the antibody is of the IgG isotype, instant claim 11 wherein the antibody is a monoclonal antibody, and instant claim 19 wherein the antibody or antigen-binding fragment is in a pharmaceutical composition and a pharmaceutically acceptable carrier.
AbbVie Inc. discloses that the term "antigen-binding portion" or "antigen-binding fragment" of an antibody (or simply "antibody portion" or "antibody fragment") refers to an antibody that retains specific binding to an antigen (eg, hB7-H3) one or more fragments of the ability. It has been shown that the antigen-binding function of antibodies can be performed by fragments of full-length antibodies. Such antibody embodiments may also be in bispecific, bispecific or multispecific formats; specifically binding to two or more different antigens. Examples of binding fragments encompassed within the term "antigen-binding portion" of an antibody include (i) Fab fragments, which are monovalent fragments consisting of the VL, VH, CL and CH1 domains; (ii) F(ab') 2 Fragment, which is a bivalent fragment comprising two Fab fragments linked by disulfide bridges in the hinge region; (iii) Fd fragment consisting of VH and CH1 domains; (iv) VL and VH of the antibody one-arm Fv fragments composed of domains; (v) dAb fragments. AbbVie Inc. also discloses that aspects of the present invention relate to anti-B7-H3 antibodies and antibody fragments, anti-B7-H3 ADCs and pharmaceutical compositions thereof, as well as nucleic acids, recombinant expression vectors and host cells for making such antibodies and fragments. This meets the limitation of instant claim 12 wherein the antigen-binding fragment can be a (Fab)’2 fragment, instant claim 13 wherein an isolated nucleic acid encodes the anti-B7-H3 antibody or the antigen-binding fragment, instant claim 14 wherein a vector comprises the isolated nucleic acid encodes the anti-B7-H3 antibody or the antigen-binding fragment, and instant claim 15 wherein a host cell comprises the vector which comprises the isolated nucleic acid encodes the anti-B7-H3 antibody or the antigen-binding fragment.
AbbVie Inc. also discloses that humanized antibodies are generated on the basis of VH and VL CDR sequences of chAb18; human germline sequences are selected for constructing CDR-grafted humanized chAb18 antibodies, wherein the CDR domains of the VH and VL chains are grafted onto different human heavy and light chain receptor sequences; the VH and VL and CDR sequences of the obtained huAb18 humanized antibodies are as shown in Table 8; the antibodies retain the ability to bind to human and cynomolgus monkey B7-H3; and an antibody drug conjugate prepared from huAb18 and a Bcl-xl inhibitor can inhibit the tumor growth in a mouse xenograft model. This meets the limitations of instant claim 18 wherein the antibody drug conjugate is an immunoconjugate comprising the antibody or antigen-binding fragment conjugated to a therapeutic agent.
Therefore, claims 3, 10-15, 18-19, and 23 are rejected by AbbVie Inc.
Conclusion
No claims are allowed.
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/SELAM BERHANE/Examiner, Art Unit 1675
/AURORA M FONTAINHAS/Primary Examiner, Art Unit 1675
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