DETAILED ACTION
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 .
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1-2, 10-20, 23-25, and 27) as well as the species of anti-CD47 antibody with a VH of SEQ ID NO. 13 and VL of SEQ ID NO. 14 and anti-EpCAM antibody with CDRH1-3 of SEQ ID Nos. 54, 55, and 56 respectively, and LCDR1-3 of SEQ ID Nos. 90, 91, and 92 respectively, with full VH of SEQ ID NO. 24 and VL of SEQ ID NO. 36, with the target cancer cells being colon adenocarcinoma, in the reply filed on 10/08/2025 is acknowledged.
Claim 69 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected subject matter, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 10/08/2025.
Claim Status
Claims 3-9, 21-22, 26, and 28-68 are canceled.
Claim 69 is withdrawn.
Claims 1-2, 10-20, 23-25 and 27 are under examination on the merits.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date as follows:
The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of 35 U.S.C. 112(a) or the first paragraph of pre-AIA 35 U.S.C. 112, except for the best mode requirement. See Transco Products, Inc. v. Performance Contracting, Inc., 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994).
The disclosure of the prior-filed application, Application No. PCT/CN2020/086815, fails to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, first paragraph for one or more claims of this application. It is first noted that a certified copy is provided for the above application and it is in English. However, the examiner sees no evidence that the exact species of the claims under examination above are present in this document. This is owed in part to the fact that SEQ ID NO. 15 varies between the priority document and the instant case. See Table 6 of the PCT above. Also, the PCT above is not a hit in the STIC fusion sequence search that contains SEQ ID NO. 15. These evidence that the species of instant claims do not have 112a support in the priority document. Applicant should outline where support can be found if it is present. Furthermore, for the same reasons below that claims under examination fail the 112a requirements, so too fails the priority document as it contains no more information over the instant claims than the instant case.
Taken all together, the U.S. effective filing date of all claims under examination is set at 04/23/2021.
Information Disclosure Statement
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
The information disclosure statements (IDS) submitted on 01/04/2023, 06/07/2024, 12/19/2024, and 10/08/2025 are being considered by the examiner.
Specification
The title of the invention is not descriptive. A new title is required that is clearly indicative of the invention to which the claims are directed. Both target antigens of the antibody claimed should be present.
The use of the terms SEPHAROSE (0316), EXPI293F (0316), SUPERDEX (0316) and ALEXAFLUOR (0318), which is a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
The disclosure is objected to because of the following informalities: At 0313 the specification cites and incorporation of PCT/CN2019/113296. This document is not on any IDS. This document was not provided as potential art. This document does not appear on the WIPO website and so may not have been published. In conclusion, no one would know what is incorporated by the current recitation.
Appropriate correction is required.
Claim Interpretation
The examiner notes here that bispecific antibody is defined to include multispecific antibodies with more than two specificities at 0152.
The examiner also notes that human and humanized antibodies are defined to be the same and both take the standard meaning of human antibody. See 0164.
Claim Objections
Claim 16 is objected to because of the following informalities: The term KiH should be deleted as it is an abbreviation not repeated in the claim set and so serves no real purpose.
Claim 24 is objected to as letters should delineate each species recited in the group. The same objection is made for claim 25.
Claim 27 is objected to as “a combination thereof” in line 3 should be “the combination thereof”. Furthermore, the claim’s use of the combination above, barring rationale from Applicant is a duplicate of the EpCAM-positive tumor cell limitation. The tumor already has CD47 in claim 1. Any duplicate limitation must be removed.
Appropriate correction is required.
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 1-2, 10-20, 23-25 and 27 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.
All claims above recite a bispecific antibody with multiple binding domains. However, bispecific antibody here includes bispecific oligoclonal antibodies in the broadest reasonable interpretation. Therefore, the claims can be interpreted to require all binding domains be on one molecule or they can be interpreted to permit binding domains to be on different antibody molecules, as is the case of oligoclonal antibodies in which multiple and different monoclonal antibodies are mixed together in solution. The presence of multiple structural interpretations renders the claims indefinite.
Claim 17 is further indefinite for reciting antibody residue positions but stating numbering is according to the EU index of Kabat et al. First, it is not clear which reference Applicant means published by Kabat and so this renders the claim indefinite. Even if Applicant had properly stated EU index, it is not clear if all the positions are defined with this system or just Y407V. The presence of multiple interpretations renders the claims indefinite.
See Ex parte Miyazaki, 89 USPQ2d 1207 (BPAI 2008) ("[R]ather than requiring that the claims are insolubly ambiguous, we hold that if a claim is amenable to two or more plausible claim constructions, the USPTO is justified in requiring the applicant to more precisely define the metes and bounds of the claimed invention by holding the claim unpatentable under 35 U.S.C. §112, second paragraph, as indefinite.").
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claims 10 and 27 are rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 10 recites the bispecific antibody of claim 1 wherein the CD47 binding domain has a VH and VL. This is inherent to the antibody of claim 1 as said domain must have three heavy and three light chain CDRs, which reside on the VH and VL respectively. These are present in an antibody which is claimed. Therefore, claim 10 does not further limit the claim on which it depends.
Claim 27 recites CD47+ tumor cell but claim 1 already provides this target and so not all limitation of claim 27 further limit claim 1 on which it depends.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form so long as no duplicate is made, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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 24-25 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for bispecific antibodies against CD47 and EpCAM in which all binding domains comprise all parental CDRs, does not reasonably provide enablement for similar structures in which any binding domain contains mutated parental CDRs untested against antigen. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims.
The breadth of the claims is found in claim 24 drawn in part to the bispecific antibody of claim 1 against CD47 and EpCAM wherein the EpCAM binding domain has CDRs at least 90% identical to SEQ ID Nos. 54-56 and 90-92.
The nature of the invention is a bispecific antibody against CD47 and EpCAM useful in treating tumors.
The level of skill of one skilled in this art is high.
The claims first allow for CDR mutation owed to their recitation of percent identities and such is not predictable or enabled as discussed below. In addition, claim 24 recites the CDR sequences should be placed in an ordered set but then recites choices of sequences from species in a group in which each species does not provide the placement of each sequence. Therefore, as broadly as currently claimed, any sequence in this claim can be any CDR (e.g. HCDR1, LCDR2, etc.) and this also amounts to CDR mutation by lack of stipulation of proper CDR placement in the antibody domain.
The state of the prior art is such that it is well established in the art that the formation of an intact antigen-binding site of antibodies generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs or hypervariable regions, which provide the majority of the contact residues for the binding of the antibody to its target epitope (Paul, Fundamental Immunology, 3rd Edition, 1993, pp. 292-295, under the heading “Fv Structure and Diversity in Three Dimensions”). The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity, which is characteristic of the immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (Paul, page 293, first column, lines 3-8 and line 31 to column 2, line 9 and lines 27-30).
Additionally, Bendig M. M. (Methods: A Companion to Methods in Enzymology, 1995; 8:83-93) reviews that the general strategy for “humanizing” antibodies involves the substitution of all six CDRs from a rodent antibody that binds an antigen of interest, and that all six CDRs are involved in antigen binding (see entire document, but especially Figures 1-3). It is noted that Bendig used Kabat CDRs in their humanization process (Pg. 86, Column 2, Paragraph, second). Similarly, the skilled artisan recognized a “chimeric” antibody to be an antibody in which both the heavy chain variable region (which comprises the three heavy chain CDRs) and the light chain variable region (which comprises the three light chain CDRs) of a rodent antibody are recombined with constant region sequences from a human antibody of a desired isotype (see entire document, but especially Figures 1-3).
Thus, the state of the art recognized that it would be highly unpredictable that a specific antibody comprising less than all six parental CDRs would have antigen binding function. The minimal structure which the skilled artisan would consider predictive of the function of binding the antigen of a murine or human antibody includes six CDRs (three from the heavy chain variable region and three from the light chain variable region) in the context of framework sequences which maintain their correct spatial orientation and have the requisite binding function. One of skill in the art would neither expect nor predict the appropriate functioning of the mutated antibody binding domains of the instant claims as broadly currently claimed.
In the case of antibodies, it is especially important to disclose which residues are permissive to mutation. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Proceedings of the National Academy of Sciences USA, Vol., 79, Pg. 1979-1983, 1982). Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (Abstract).
Not knowing, absent further experimentation, which modifications function and which do not, when, as set forth above, even a single change of an encoded amino acid can unpredictably affect antibody structure and function, leads to one having no predictability or expectation of success for the function of any given antibody modification. Such random experimentation to identify at a later time what structure or fragment or modification is or is not functional and is embraced by Applicant’s claims is undue experimentation.
Since the claims above read on antibodies comprising a binding domain with mutated parental CDRs, which would not predictably bind antigen, the claims are rejected here.
Furthermore, claim 24 recites SEQ ID NO. 90 which can act as LCDR1 in the anti-EpCAM binding domain. A complete set of CDRs for patent purposes should include CDRs that are known to confer antigen binding to a non-parental framework. As mentioned above in the works of Bendig, Kabat CDRs can be moved to a different framework, such as during humanization, and confer antigen binding.
Johnson and Wu (Methods in Molecular Biology, Antibody Engineering: Methods and Protocols, Vol. 248, Pg. 11-25, 2004) teach that complete CDRs of antibodies CDRH1-3 and CDRL1-3 are at least 5, 16, 8, 11, 7, and 9 amino acid residues in length respectively (Pg. 12, Paragraph, second full). In instant claim 24, CDRL1 has 10 residues. This is smaller than the CDR length of the corresponding Kabat CDR and so would not be expected to confer antigen binding to an antibody framework barring evidence to the contrary as it appears to be a mutated/truncated Kabat CDR. Mutated CDRs would not predictably bind antigen as discussed above.
Therefore, even a bispecific antibody comprising an anti-EpCAM binding domain with all the CDRs of claim 24 in the species discussed above is not enabled. Barring experimental evidence, such mutated and truncated CDRs would be insufficient to confer antigen binding function.
Moreover, claims not containing elements critical or essential to the practice of the invention, such as antibodies or antibody fragments not having all of the relevant functional complementarity determining regions (CDRs) in the proper site on an appropriate antibody heavy or light chain framework, are not enabled by the disclosure. See In re Mayhew, 527 F.2d 1229, 188 USPQ 356 (CCPA 1976).
Note that an enabling disclosure for the preparation and use of only a few analogs of a product does not enable all possible analogs where the characteristics of the analogs are unpredictable. See Amgen Inc. v. Chugai Pharmaceutical Co. Ltd. (18 USPQ 2d 1027 (CAFC 1991)).
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to make and use functional antibodies comprising any antigen binding domain with fewer than all six parental CDRs or comprising mutated versions thereof, with a reasonable expectation of success, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed antibodies are functional, commensurate in scope with the claimed invention.
Claim 27 is 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. This is a new matter rejection.
This claim recites tumor types in a Markush group and further states any of them can be EpCAM+, CD47+, or EpCAM+/CD47+. As discussed above, these limitations only mean the tumor cells can be EpCAM+/CD47+ or EpCAM-/CD47+ owed to claim 1 dependence. However, the original claims (e.g. claims 63 and 65) and the original specification (0005-0009 and 0112) teach only double positive species of these diseases. Therefore, the claim breadth overreaches the original disclosure. Thus, recitation of CD47+ alone, implying the disease can be negative for EpCAM, and so encompassing such breadth, is new matter and the claim is rejected here.
Even though the original disclosure may be sufficient to render the claimed subject matter obvious. This is not the same as original contemplation or teaching and instead proves such was not originally disclosed since it had to be made obvious.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claim(s) 1-2, 10, 12, 14-15, 23, and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Weiskopf (US2016/0333093, published 11/17/2016), in view of Mei (US2022/0403023, priority to 10/25/2019).
Weiskopf teaches agents that selectively block CD47 binding to SIRPalpha as treatment for lung cancer (Abstract). The therapy provides a multispecific antibody that targets CD47 and a second cancer cell marker such as CD47 and EpCAM (0009). Their antibody against CD47 can comprise an IgG4 Fc region (Claim 22).
Thus, it would have been obvious to a PHOSITA reading Weiskopf to produce a bispecific antibody against CD47 and EpCAM where said antibody has an IgG4 Fc region as these structures are provided for the therapeutic agent of Weiskopf and their combination would yield the predictable results of an anti-cancer therapeutic bispecific antibody.
Weiskopf does not teach the anti-CD47 binding domain of their antibody should comprise the CDRs of instant claim 1.
This deficiency is remedied by Mei.
Mei teaches anti-CD47 antibodies which are potent agents for the treatment of cancers via modulating immune functions (Abstract). Their antibody described therein comprises a VH of SEQ ID NO. 7 and VL of SEQ ID NO. 8 (0049). It can also comprise their SEQ ID Nos. 11 and 12 (claim 10) which are 97.7% and 99.5% identical to instant SEQ ID Nos. 13 and 14 respectively. It can comprise a human IgG4 (0050). It blocks CD47/SIRPalpha binding (0051) and has weak affinity for red blood cells (RBCs) (0054).
Taken together, it would have been obvious to a PHOSITA before the filing of the instant application that the anti-CD47 binding domain of Weiskopf could be replaced by either of Mei, which amounts to simply substitution of one anti-CD47 binding domain for another, to arrive at a predictably functional bispecific anti-CD47/EpCAM antibody with human IgG4 structure for use in cancer treatment. The human nature of the IgG4 is taught by Mei and would have been obvious to use in the construct of Weiskopf to a PHOSITA to avoid anti-therapeutic antibody immune responses in a human subject (0058 of Weiskopf) when using the obvious molecule to treat a human patient, which are the preferred subjects of Mei (0125). Weiskopf implies the same by stating their multispecific antibody is preferably human or humanized (0009) and so carries a human Fc region. Weiskopf explicitly states the same preference for human subjects (0065).
With respect to claims 1 and 27, since the structure required is met in the obvious molecule, all functional properties are equally met. “Products of identical chemical composition cannot have mutually exclusive properties.” A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). The same logic applies to a structurally identical obvious molecule as here.
With respect to claim 12, such an IgG4 based structure would have a VH and VL pair against EpCAM.
Thus, the combination of prior art above clearly renders all claims above obvious.
Claim(s) 1-2, 10-20, 23, and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Weiskopf (US2016/0333093, published 11/17/2016) and Mei (US2022/0403023, priority to 10/25/2019) as applied to claims 1-2, 10, 12, 14-15, 23, and 27 above, and further in view of Fang (US2020/0087412, published 03/19/2020) and Movahedi (US2015/0335770, published 11/26/2015).
The combined teachings of Weiskopf and Mei render obvious claims 1 and 15 for the reasons above, the first 103 being incorporated here in its entirety.
They do not teach asymmetric bispecific antibodies or wherein the bispecific antibody carries a Fab against one target and an scFv against the other.
These deficiencies are cured by Fang.
Fang teaches asymmetric bispecific antibodies for use in treating disease (Abstract) such as cancer (0026). Their tumor antigen targets include CD47 and EpCAM (0027). Figure 1 shows their invention (0026) in which a dimeric Fc region carrying knob-in-hole mutations has one Fab at its N-terminus and one scFv at its C-terminus, both binding domains being on the same peptide. The Fab targets one antigen and the scFv the other. The knob-in-hole is created by T366W on one chain and T366S, L368A and Y407V on the other (0045-0050) and such provides the advantage of decreasing homodimers (0045). These positions are recited by EU index position as referenced in the sequence identifiers at 0049-0050. A PHOSITA would have immediately seen the advantage of this molecule, as it is bispecific for two tumor antigens as taught by Weiskopf but has a reduced size compared to the conventional antibody (Figure 1 of Fang), with respect to tumor penetrance as it is well-known that antibodies with reduced size have increased tumor penetrance. Evidence of this knowledge is provided by Movahedi at 0097. Thus, it would be expected to travel deeper into a tumor and more effectively treat the same by one of ordinary skill in this art.
Taken all together, it would have been obvious before the filing of the instant application to create a bispecific molecule using the design of Fang with the VH and VL domains/CDRs of Mei to produce a molecule with the functionality desired by Weiskopf for use in treating human cancers that are CD47+/EpCAM+. Such a molecule would have high tumor penetrance and increased avidity for the tumor as it binds two tumor antigens thereon. Thus, the molecule of the claims above is obvious.
With respect to which domain is scFv and which is Fab in the obvious molecule, both are equally obvious as they will yield the functional molecule predictably and two choices is incredibly finite, making both possibilities instantly obvious. Therefore, use of an anti-CD47 Fab or scFv and the same two possible structures for the anti-EpCAM domain would have been obvious to a PHOSITA. The claims must be rejected here as obvious.
Claim Rejections - Improper Markush Grouping
Claims 24-25 are rejected on the judicially-created basis that they contain an improper Markush grouping of alternatives.
See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984).
The improper Markush grouping includes species of the claimed invention that do not share both a substantial structural feature and a common use that flows from the substantial structural feature. The members of the improper Markush grouping do not share a substantial structural feature and a common use that flows from the substantial structural feature for the following reasons:
MPEP 803.02 provides guidance on the analysis of a proper Markush group. Members of a proper Markush group are disclosed in the specification to possess at least one property in common which is mainly responsible for their function in the claimed relationship, and it is clear from their very nature or from the prior art that all of them possess this property. The MPEP further provides that in the members of a proper Markush group there should be (1) a common utility, and (2) a substantial structural feature essential to that utility.
In the instant case, the claims above recite Markush groups of anti-EpCAM binding domains. However, the substantial structural feature of antibodies essentially to their utility is the full set of CDRs. See the work of Paul above all discussion thereof incorporated here. Thus, these must all be shared among members of a proper Markush group. They are not shared among all the species here and so the species do not share a common structural feature essential to their utility and the claims are rejected here.
In response to this rejection, Applicant should either amend the claim(s) to recite only individual species or grouping of species that share a substantial structural feature as well as a common use that flows from the substantial structural feature, or present a sufficient showing that the species recited in the alternative of the claims(s) in fact share a substantial structural feature as well as a common use that flows from the substantial structural feature. This is a rejection on the merits and may be appealed to the Board of Patent Appeals and Interferences in accordance with 35 U.S.C. §134 and 37 CFR 41.31(a)(1).
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MICHAEL D ALLEN whose telephone number is (571)270-3497. The examiner can normally be reached Mon-Fri 10-6.
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/Michael Allen/ Primary Examiner, Art Unit 1642