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 .
Claims 1-5, 9, and 11-28 are pending and will be examined on the merits.
Claim Objections
Claims 4, 5, 14 and 16 all contain parenthetical references to one or more figure in the Drawings of the instant disclosure. All of the parenthetical references in question immediately follow recitation of one or more amino acid sequence identifiers and cites a figure depicting the corresponding amino acid sequence. Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table "is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim. Incorporation by reference is a necessity doctrine, not for applicant’s convenience." Ex parte Fressola, 27 USPQ2d 1608, 1609 (Bd. Pat. App. & Inter. 1993). In the instant case incorporation by reference is not necessary because the disclosure already contains all of the complete amino acid sequences of all claimed amino acid sequences in the Sequence Listing file.
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 5, 15-18, 25 and 27-28 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 15-16, 25 and 27-28
Regarding claims 15, 25, 27, and 28 each recitation of the phrase “optionally" independently renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
Note: for examination, all of claims 15-16, 26 and 27-28 will be examined as if the limitations indicated as optional are not required limitations.
Claim 5
Regarding claim 5, the phrase “e.g., at least 95% or 98%) or 100%” (following “at least 90%” in the discussion of beta 1 and beta 2) renders the claim indefinite because it is unclear whether the limitations are part of the claimed invention. See MPEP § 2173.05(d).
Note: for examination, any sequence having at least 90% sequence identity to the recited beta 1 and beta 2 sequences will be treated as reading on claim 5.
Claim 17-18
Claim 17 is directed to MAPPs comprising at least one MOD, variant MOD, pair of MODs and/or pair of variant MODs in tandem at positions 1, 1’, 2, 2’, 3, 3’, 4, 4’, 4’’’, 5 and/or 5’. Claim 18 is dependent on claim 17 and recites positions 1 and 1’ only. There is nothing in claim 17, claim 18 or any of the claims upon which claim 17 depends (or even in the claim set) that specifies where positions 1, 1’, 2, 2’, etc.… are located. Additionally, Fig 1A and 1B of the Drawings does contain MAPP structures with some termini labeled 1, 1’, 2’, 2’, etc.…, however none of the drawings contain the 4’’’ position recited in claim 17. As such, the metes and bounds of claims 17 and 18 are not clear because it is not clear where the MOD units recited are permitted to be positioned.
Note: For the purposes of examination, MAPPS comprising the MOD types above located at any position of the MAPP will be interpreted as reading on claims 17-18
Claim Rejections - 35 USC § 103
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 (i.e., changing from AIA to pre-AIA ) 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.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1-5, 9, 11-19, 21 and 25-29 is/are rejected under 35 U.S.C. 103 as being unpatentable over Seidel (Seidel, et al., US 2019/0062400 A1; Published 2/28/2019; Priority to 3/2/2016 via US 62/302,654) in view of Zhu (Zhu, et al., Eur. J. Immunol 1997 27:1933), Levin (Levin, et al., CA 2802017 A1; Published 12/15/2011; Priority to 6/9/2010 via US 61/352,873) and Faner (Faner, et al., Eur. J. Immuno. 2010 40:91).
Seidel teaches multimeric T cell modulatory polypeptides and methods of using the same (Seidel, Abstract). Regarding 1, Seidel teaches a multimeric polypeptide comprising: A) a first polypeptide comprising, from N-terminus to C-terminus: 1) an epitope and 2) a first MHC polypeptide and B) a second polypeptide comprising, from N-terminus to C-terminus: 1) a second MHC polypeptide and 2) a scaffold that is an IgG Fc polypeptide or a non-Ig scaffold, wherein the multimeric polypeptide comprises one or more immunomodulatory domain situated at the carboxy or amino terminus of the first or second polypeptide (Seidel, ¶ 0005). Further regarding the structural limitations of claim 1, Seidel also teaches that the multimeric polypeptides of Seidel comprise first and second MHC sequences on the first and second polypeptides that are either: 1) beta-2-microglobulin paired with an MHC I heavy chain or 2) an MHC II alpha chain paired with an MHC II beta chain and that the first and second polypeptides in the multimeric polypeptide of Seidel are covalently linked or noncovalently associated (Seidel, ¶ 0005). Regarding the HLA type limitations of claims 4-5, Seidel teaches that the MHCII embodiments of Seidel comprise a HLAII DR alpha polypeptide paired with a HLAII DR beta polypeptide (Seidel, ¶ 0122-0126). Regarding claims 11-12 and 14, Seidel teaches that the multimeric polypeptides of Seidel comprise Ig Fc regions (a non-interspecific multimerization sequence as per claim 12) (Seidel, ¶ 0005).
Regarding the dimer limitation of claim 13, the Ig Fc region limitation of claim 14 as well as the disulfide limitation of claim 15, Seidel teaches that the multimeric peptides of Seidel are present as homodimers depending by the Fc sequences present in the two molecules and that these Fc sequences that may comprise disulfide linkages between the Fcs (Note: all compositions of Seidel comprising Fc regions would comprise homodimers, as Seidel teaches that the Fc regions can form homodimers and it is well-known in the art that in the case of IgG1 Fcs, Fc regions dimerize) (Seidel, ¶ 0113). Regarding claim 16, Seidel teaches that the Fc regions present in the polypeptides of Seidel comprise IgG1 Fcs (same as SEQ ID NO: 4) with N77A substitutions (Seidel, ¶ 0187). Regarding claims 17 and18, Seidel teaches one or more immunomodulatory polypeptides located at the amino or carboxy termini of any one of the component peptides (Seidel, claim 4) situated in tandem (Seidel, claims 26-27), wherein the immunomodulatory peptides are CD80 immunomodulatory peptides (Seidel, claim 1). Regarding claim 25, Seidel teaches that the multimeric polypeptides are administered in methods of treating disorders that comprise self-epitopes (same as autoantigen) (Seidel, ¶ 0334) and that the multimeric polypeptides are administered in treating methods of treating an autoimmune disease (Seidel, ¶ 0035). Regarding claim 26, Seidel teaches nucleic acids encoding the multimeric peptides of Seidel (Seidel, claims 31-47). Regarding claims 27 and 28, Seidel teaches host cells expressing the multimeric peptides of Seidel (Seidel, claim 58), wherein the host cells have been modified to comprise nucleic acids encoding the multimeric peptides of Seidel (Seidel, claim 50). Regarding claim 29, Seidel teaches a method of selectively modulating the activity of an epitope-specific T cell in an individual comprising administering an effective amount of the multimeric peptides of Seidel (same as selectively delivering the CD80 MOD polypeptides of Seidel to the T cells) (Seidel, claim 66).
Note, for the sake of clarity of the record, an exemplary figure from Seidel depicting one of the multimeric polypeptides of Seidel (MHCI, Seidel offered no Figures depicting MHCII) (Seidel, Fig 1C)
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Seidel does not teach that the first and second polypeptide present in the multimeric peptide of Seidel each comprise a presenting sequence comprising, from N-terminal to C-terminal: peptide epitope, b1, b2, a1 and a2, wherein, wherein the alpha chains are from HLA-DR alpha1 and the beta chains are from HLA-DR beta 3 and wherein neither MHCII peptide comprises a transmembrane domain. Seidel does not teach that the multimeric polypeptides of Seidel comprise dimerization sequences that are a CH1 sequence present on the first polypeptide of the multimer that forms a specific, non-covalent interaction with a CK sequence present on the second polypeptide of the multimer.
Zhu teaches on the subject of recombinant MHCII (HLA-DR1) single chain molecules comprising a heterotrimer comprising a HLAII alpha chain, beta chain and antigenic peptide (Zhu, Abstract). Zhu teaches that natural MHC II molecules are composed of two polypeptide chains, alpha and beta, which form a peptide binding site that binds antigenic peptides, with the resulting alpha chain/beta chain/peptide heterotrimer providing a specific signal to CD4 helper T cells (Zhu, p 1934, ¶ 2). Zhu teaches that covalent linkage of these three components in a recombinant MHC molecule was performed to enhance stability and prevent peptide dissociation, thus allowing a longer term of immunization and use of peptides with a relatively low MHC affinity (Zhu, p 1934, ¶ 2). Zhu teaches that a recombinant HLA-DR cDNA fusion molecule comprising an antigenic peptides from HIV p24 GAG (GAG) were prepared via a cDNA construct encoding the entire heterotrimer comprising the peptide, GAG-linked beta chain (without the transmembrane domain) and alpha chain as a covalently linked, single chain protein molecule (Zhu, p 1934, ¶ 2) and that soluble single chain MHCII were constructed introducing a stop codon after position 192 of the alpha chain cDNA to prevent translation of the transmembrane and cytoplasmic domains of the alpha chain (Zhu, p 1936, ¶ 2). Zhu teaches that the structure of the cDNA encoding the heterotrimeric MHCII complex of Zhu comprises, from 5’ to 3’: the peptide epitope, MHCII beta chain and MHCII alpha chain (Zhu, Fig. 1). Zhu also teaches that the single chain MHCII molecules of Zhu exhibited reduced binding of bacterial superantigen while maintaining the molecule’s T cell recognition properties (Zhu, p 1940, ¶ 5) and that the presence of B7-1 (same as CD80) preserves the MHCII molecules’ abilities to stimulate T cells when the soluble/cytotoxic domains of the molecule are not present (Zhu, p 1940, ¶ 4).
Levin teaches on the subject of soluble, dimeric fusion proteins comprising a first and second fusion polypeptide linked via a dimerizing domain (Levin, Abstract). Levin teaches that the soluble polypeptide fusions of Levin comprise first and second soluble polypeptide fusions, with each polypeptide fusion comprising, from amino to carboxy terminus, P1,-L1-D-L2-P2 or P2-L2-P1-L1-D, wherein: 1) P1 is an extracellular domain of a first cell-surface receptor (or functional variant or fragment thereof) or a first cytokine or functional variant/fragment, 2) L1 is a first polypeptide linker, 3) L2 is a second polypeptide linker, 4) P2 is a second extracellular domain of a second cell-surface receptor (or functional variant or fragment thereof) or a second cytokine or functional variant/fragment and 5) D is a dimerizing domain (Levin, ¶ 010). Levin teaches that the dimerizing domains of Levin are polypeptides having affinity for a second polypeptide (that is the same or different from the first polypeptide) such that the two polypeptides associate under physiological conditions to form a dimer (Levin, ¶ 041). Levin teaches that the dimerizing domains of Levin include CH1 and CL domains (Levin, ¶ 041). Levin also teaches that the dimerizing domains comprising at least one cysteine residue such that disulfide bonds may form between the first and second domains (Levin, ¶ 041).
Faner teaches that the DRB1/3/4/5 loci encode MHCII beta chains that pair with a MHCII DR alpha chain to form DR molecules on the surface of an antigen presenting cell (APC) (Faner, Abstract). Faner also teaches that MHCII molecules comprising DRB3*0101 beta chains successfully bound several peptide antigens from tetanus toxoid (Faner, Abstract; Table 1).
It would be prima facie obvious to one of ordinary skill in the art to start with the MHCII-comprising, CD80 MOD comprising multimeric fusion polypeptides of Seidel, wherein the first and second fusion polypeptides are associated with one another via the association between an MHCII alpha chain on the first polypeptide and a MHCII beta chain on the second fusion polypeptide, and substitute each of the MHCII chains (alpha and beta) with a single chain MHCII peptide epitope/beta chain/alpha chain trimer of Zhu and further modify the fusion polypeptides to comprise the CH1 dimerizing domain of Levin on the first fusion polypeptide and the CL dimerizing domain of Levin on the second fusion polypeptide. The net result of this modification would be a multimeric polypeptide comprising a first and second fusion polypeptide, wherein the first fusion polypeptide comprises (from N to C): (peptide epitope)-(HLAII beta sequence)-(HLAII-alpha sequence)-(CH1 dimerizing sequence) and the second fusion polypeptide comprises (from N to C): (peptide epitope)-(HLAII beta sequence)-(HLAII alpha sequence)-(CL dimerizing sequence)-(IgG1 Fc sequence), wherein the CH1 sequence on the first fusion polypeptide associates with the CL sequence on the second fusion polypeptide, forming a dimer between the first and second fusion polypeptides and wherein the multimeric polypeptide comprises at least one CD80 MOD element taught by Seidel at any of the loci taught by Seidel). One of ordinary skill in the art would be motivated to do this in order to extend the term of immunization provided by the multimeric peptides of Seidel and allow the use of MHCII peptides having relatively low MHC affinities. The multimeric fusion proteins of Seidel possess two required design elements: 1) a MHCII epitope-presenting element and 2) a dimerization element capable of allowing the two multimeric fusion polypeptides to form a dimer with each other. In the multimeric fusion proteins of Seidel, the MHC polypeptides on the first and second fusion polypeptides of Seidel act as both the MHCII epitope-presenting element and the dimerization element. Zhu teaches that covalently linking the MHCII alpha and beta chains and a peptide epitope within a single polypeptide decreases epitope dissociation from the MHCII complex, allowing for longer immunization times as well as the use of peptides with lower MHC affinity. Additionally, Zhu also teaches that the presence of B7-1/CD80 attenuates the reduction in T cell interactions caused by the truncation of the MHCII peptides to not include the transmembrane/cytoplasmic domains and CD80 MOD elements are already present in the multimeric peptides of Seidel. One of ordinary skill in the art would immediately recognize these properties as obvious benefits, however one of ordinary skill in the art would also immediately recognize that replacing the MHCII alpha/beta chains present on the multimeric fusion proteins of Seidel without any further modifications would result in loss of the ability of the first and second fusion polypeptides to associate with one another, as this association takes place between the two MHCII polypeptides. This is a problem that the CH1/CL dimerization domains of Levin constitute a natural solution to that would also be obvious to one of ordinary skill in the art. It is well-known in the art that CH1 and CL sequences naturally associate with one another in antibodies and Levin teaches that CH1 and CL sequences were known in in the art as suitable dimerization sequences to allow the dimerization of two fusion polypeptides. As such, one of ordinary skill in the art would realize that including the CH1 domain of Levin on one of the fusion polypeptides of Seidel and the CL domain of levin on the other fusion polypeptide of Seidel would allow for the use of the single chain presenting sequence of Zhu because the two fusion polypeptides no longer require association between adjacent and complementary MHCII alpha/beta chains to form the dimer. One of ordinary skill in the art would have a reasonable expectation of success starting with the MHCII-comprising, CD80 MOD-comprising multimeric fusion polypeptides of Seidel, wherein the first and second fusion polypeptides are associated with one another via the association between an MHCII alpha chain on the first polypeptide and a MHCII beta chain on the second fusion polypeptide, and substituting each of the MHCII chains (alpha and beta) with a single chain MHCII peptide epitope/beta chain/alpha chain trimer of Zhu and further modifying the fusion polypeptides to comprise the CH1 dimerizing domain of Levin on the first fusion polypeptide and the CL dimerizing domain of Levin on the second fusion polypeptide because: 1) the MHCII polypeptides on the first and second fusion polypeptides of Seidel possess two required functions: A) associating with one another to form a dimer between the firs t and second fusion polypeptides and B) acting as a MHCII presenting complex, 2) Zhu teaches that MHCII fusion trimers comprising the MHCII alpha chain, MHCII beta chain and a peptide epitope offer the benefits of increasing immunization time and allowing for use of low MHCII affinity peptides but would eliminate the ability of the two polypeptides to form a dimer via the association of a MHCII alpha chain on one fusion polypeptide with a MHCII beta chain on the second fusion polypeptide, 3) Levin teaches that CH1 and CL domains are suitable dimerization domains that allow a first and second fusion polypeptide to form a dimer with one another, 4) one of ordinary skill in the art would realize that including the CH1 dimerization domain of Levin on one of the fusion polypeptides of Seidel and the CL dimerization domain of Levin on the second fusion polypeptide of Seidel would allow the first and second fusion polypeptides to dimerize independently of MHCII alpha/beta chain association, allowing for the inclusion of the single chain (MHCII alpha)-(MHCII beta)-(peptide epitope) trimeric presenting sequence of Zhu, thus accessing the benefits of increased immunization time and the ability to use peptides with low MHCII affinity peptides as taught by Zhu and 5) Zhu teaches that the B7.1/CD80 MOD elements already present on the multimeric fusion polypeptides of Seidel would attenuate loss of T cell stimulating function associated with the loss of the transmembrane domains present in the MHC polypeptides. Regarding claim 9 specifically, Zhu teaches the cDNA of Zhu is in the order (5’[Wingdings font/0xE0]3’): (peptide epitope)-(MHCII-beta chain)-(MHCII alpha chain) and, as such, the amino acid sequence of the corresponding translated polypeptide would comprise (from N to C): (peptide epitope)-b1-b2-a1-a2, satisfying condition (b) of claim 9. Regarding the disulfide within the dimerization sequence limitation of claim 15, it is well-known in the art that the CH1 and CL dimerization sequences of Levin each naturally comprise a cysteine moiety positioned such that a disulfide is formed between CH1 and CL when they associate and, as such, selecting CH1/CL dimerization sequence pairing would inherently lead to a disulfide between the two dimerization sequences. Note: this modification satisfies all of claims 1-3, 11-19, 21 and 25-29
It would be prima facie obvious to one of ordinary skill in the art further modify the multimeric fusion polypeptide described above such that the MHCII-DR alpha chain of taught by Zhu is paired with a MHCII-DR beta chain that is with a DRB3*01:01 (same as SEQ ID NO: 55) in view of the teachings of Faner. One of ordinary skill in the art would be motivated to do this to form a functional MHCII-DR dimer. Seidel teaches the pairing of a MHCII DR alpha chain with a MHCII DR beta chain but does not specify the HLA family or alleles. The MHCII alpha and beta chains present in the single chain MHCII trimer of Zhu is also a MHCII DR type. Faner teaches that MHCII DR alpha chains may be paired with MHCII beta chains that are DRB1, DRB3, DRB4 and DRB5 and that pairing of DRB3*0101 with DRA produced a functional MHCII DR molecule capable of recognizing several antigenic peptides present within tetanus toxoid. One of ordinary skill in the art would have a reasonable expectation of success further modifying the multimeric fusion polypeptide described above such that the MHCII-DR alpha chain of taught by Zhu is paired with a MHCII-DR beta chain that is with a DRB3*01:01 because: 1) Seidel teaches multimeric fusion polypeptides that are MHCII-DR polypeptides but does not teach the specific MHCII family/allele DRA is paired with, 2) Zhu teaches that the functional, single stranded trimeric MHCII molecule of Zhu is a MHCII-DR molecule and 3) Faner teaches that pairing DRB3*0101 with DRA forms a functional DR molecule capable of recognizing multiple MHCII epitopes from tetanus toxoid. Note: this modification satisfies all of claims 1-5, 9, 11-19, 21 and 25-29.
Claim(s) 1-5, 9 and 11-29 is/are rejected under 35 U.S.C. 103 as being unpatentable over Seidel (Seidel, et al., US 2019/0062400 A1; Published 2/28/2019; Priority to 3/2/2016 via US 62/302,654) in view of Zhu (Zhu, et al., Eur. J. Immunol 1997 27:1933), Levin (Levin, et al., CA 2802017 A1; Published 12/15/2011; Priority to 6/9/2010 via US 61/352,873) and Faner (Faner, et al., Eur. J. Immuno. 2010 40:91) as applied to claims 1-5, 9, 11-19, 21 and 25-29 above and in further view of Lu (Lu, et al., Am. J. Cancer Res 2018 8(8):1564-1575).
The combined teachings of Seidel, Zhu, Levin and Faner are discussed above. In addition, Seidel also teaches that the multimeric fusion polypeptides of Seidel comprise a costimulatory polypeptide that is an antibody that binds to PD1 (Seidel, ¶ 0179-0180). Seidel also teaches embodiments wherein the epitope present in the multimeric fusion polypeptides of Seidel is a cancer epitope (Seidel, claim 68).
The combined teachings of Seidel, Zhu, Levin and Faner do not the teach multimeric fusion polypeptide collectively taught by Seidel, Zhu, Levin and Faner, wherein the epitope targeted by the polypeptide is a cancer epitope that is WT-1 and wherein the multimeric fusion polypeptide comprises a cancer targeting polypeptide that is a PD1 antibody.
Lu teaches on the subject of PD1 expression following administration of a WT1-targeted DC vaccine (Lu, Abstract). Lu teaches that administration of a DC vaccine targeting WT1 resulted in an upregulation of the T-cell inhibitory receptor PD1 (Lu, Abstract). Lu also teaches that treatments comprising PD1 blockade enhanced the growth and function of vaccine induced CTLs (Lu, p 1572, ¶ 3).
It would be prima facie obvious to one of ordinary art to modify the multimeric fusion polypeptide collectively taught by Seidel, Zhu, Levin and Faner to comprise the PD1-binding antibody of Seidel and the WT1 peptide epitope of Lu in view of the teachings of Lu. One of ordinary skill in the art would be motivated to do this in order to better treat gastric cancer. Lu teaches that DC vaccination with WT1 peptide epitopes induces upregulation of PD1 on T cells, which inhibit the growth and function of the resultant CTLs. Lu also teaches that PD1 blockade attenuates this effect. Since DC peptide vaccination with a peptidic epitope results in the DCs presenting the peptidic epitope to T cells on MHCII molecules, the effect of the DC vaccine of Lu and effect of the peptide epitope presented by the MHCII presenting sequences of Zhu would be highly similar. The PD1 binding antibody present on the multimeric fusion polypeptides of Seidel possesses two beneficial elements: 1) the PD1 blockade would attenuate the immunosuppressive effects associated with upregulation of PD1 following WT1 vaccination and 2) the PD1-binding antibody would act as a cancer targeting peptide by localizing the molecule in and around the tumor microenvironment due to the increased presence of T cells within the tumor microenvironment. One of ordinary skill in the art would have a reasonable expectation of success modifying the multimeric fusion polypeptide collectively taught by collectively taught by Seidel, Zhu, Levin and Faner to comprise the PD1-binding antibody of Seidel and the WT1 peptide epitope of Lu in view of the teachings of Lu because: 1) Seidel teaches that the multimeric fusion polypeptide of Seidel comprises a PD1 antibody, 2) Seidel teaches the multimeric fusion polypeptide of Seidel that comprise cancer epitopes, 3) Lu teaches that WT1 DC vaccination synergizes with PD1 blockade in the treatment of gastric cancer and 4) the immunological effect(s) of the WT1 DC vaccine of Lu would be highly similar to those of the MHCII presenting molecules of Seidel and Zhu because they are both MHCII-dependent processes.
Conclusion
Claims 1-5, 9, and 11-29 are rejected.
Claims 4, 5, 14 and 16 are objected to.
No claims are allowed.
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/SYDNEY VAN DRUFF/ Examiner, Art Unit 1643
/JULIE WU/ Supervisory Patent Examiner, Art Unit 1643