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Applicant’s previous election of species in the reply filed on 07/28/2025 is withdrawn and the previously withdrawn claims 38-40 are rejoined.
Claim Status
Claims 1-2, 7-8, 13, 18, 20, 23, 25-26, 35-37, 45-47, 49-51, and 53-55 are cancelled. Claims 3-6, 9-12, 14-17, 19, 21-22, 24, 27-34, 38-44, 48, 52, and 56-66 as filed on 24 March 2026 are pending and are under examination.
Rejections Withdrawn
Rejection of claims 3-6, 9-12, 14-17, 19, 21-22, 24, 27-34, 41-44, 46, 48, 52, and 56-66 under 35 U.S.C. 102(a)(1) over Thanos (US 12024709 B2) (IDS) is withdrawn with disqualification by applicant under 102(b)(2)(c).
Rejection of claims under Double Patenting over U.S. Patent No. 12024709 B2, Application No. 17747689, and Application No. 17934166.
Applicant’s arguments, see Remarks and explanation below, filed 03/24/2026, with respect to claim rejections have been fully considered and are persuasive. The rejection of claims 3, 10-12, 14, 21-22, 34, 41, 43-44, 48, 52, and 56-59 under 35 U.S.C. 103 has been withdrawn.
First, applicant was correct in Petit (WO 2015/126921 A1) (Of Record) not teaching the required mutation of the claims.
Further applicant has pointed unexpected results unknown in the art. The claims as written are to immunostimulatory bacterium comprising one of the following genetic modification combinations: Δasd/ /ΔFLG/ ΔpagP/ΔimsbBI /ΔansB/ ΔcsgD/F-Δpurl or Δasd/ /ΔFLG/ ΔpagP/ ΔmsbB/ ΔansB/ ΔcsgD/F-Δpurl/ ΔthyA and the F-Δpurl is a full deletion of the purI locus.
Applicant has shown that ansB deletion improved anti-tumor response in a tumor microenvironment promotes adaptive immunity and enhanced T-cell function. Bacterial production L-asparaginase II inhibits T-cell activity and downregulates T-cell receptors. The deletion of ansB in strains by applicant did not induce immunosuppression. (Specification Section 5 pages 152-154 and applicant Remarks 03/24/2026 Page 13 as numbered by applicant in pars 1-2).
Applicant has shown that the full deletion of purI resulted in improved effectiveness as a cancer therapeutic. First, applicant has shown that the full deletion versus disruption of purI has distinct phenotypes as known in the art disruption allows for reversion and restoration of purI in the bacteria (Remarks page 14 as numbered by applicant in pars 2-3 and Example 19). Second, applicant has shown purI in bacteria in combination with the mutations of the claims produced a bacteria with controlled growth in the extracellular space in tumor tissue improving tumor control and decreasing the risk of side effects (Examples 2 and 19).
New Rejection Necessitated By Rejoinder of Previously Withdrawn Claims
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 38-40 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.
MPEP § 2163 states that 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, or it may be satisfied by the 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. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
Scope of the Claimed Genus
The claims are to an immunostimulatory bacterium that encodes a bi-specific T-cell engager that binds DLL3 and CD3.
Claims 38-39 do not define any of the sequences of the bi-specific T-cell engager antibodies. Only requiring the binding activity to DLL3 and CD3.
Claim 40 comprises a combination of any of subparts a-f.
Subpart a requires a light chain of at least 95% identity to amino acids 154-260 of instant SEQ ID NO: 487, the amino acids of 154-260 of instant SEQ ID NO: 487 without variation are to the light chain of the DLL3 binding antibody SC16.15.
Subpart b requires a heavy chain that comprises at least 95% identity of amino acids 22-138 of instant SEQ ID NO: 487, the amino acids of 22-138 of instant SEQ ID NO: 487 without variation are to the heavy chain of the DLL3 binding antibody SC16.15.
Subpart c requires a light chain of at least 95% identity to amino acids 155-261 of instant SEQ ID NO: 489, the amino acids of 155-261 of instant SEQ ID NO: 489 without variation are to the light chain of the DLL3 binding antibody SC16.34.
Subpart d requires a heavy chain of at least 95% identity to amino acids 22-139 of instant SEQ ID NO: 489, the amino acids of 22-139 of instant SEQ ID NO: 489 without variation are to the heavy chain of the DLL3 binding antibody SC16.34.
Subpart e requires a heavy chain of at least 95% identity amino acids 155-261 of instant SEQ ID NO: 485 and a light chain of at least 95% of amino acids 22-139 of instant SEQ ID NO: 485, the amino acids 155-261 and 22-139 of instant SEQ ID NO: 485 without variation are the light and heavy chain of the DLL3 antibody SC16.56.
Subpart f requires a CD3 binding light chain of at least 95% identify to amino acids 398-504 of instant SEQ ID NO: 485 and a heavy chain of at least 95% identity to amino acids 267-382 of instant SEQ ID NO: 485.
Claim 40 would include mixing and matching of heavy and light chains for the anti-DLL3 antibody and the anti-CD3 antibody and would include bispecific T-cell engagers that did not define any of the anti-DLL3 antibody or the anti-CD3 antibodies.
Summary of Species Disclosed in the original specification
Applicant discloses the following antibodies:
Anti-DLL3 of SC16.56 which comprises a VH of amino acids 22-139 of instant SEQ ID NO: 485 with a VL of amino acids 155-261 of instant SEQ ID NO: 485,
Anti-DLL3 of SC16.15 which comprises a VH of amino acids of 22-138 of instant SEQ ID NO: 487 with a VL of amino acids of 154-260 of instant SEQ ID NO: 487,
Anti-DLL3 of SC16.34 which comprises the VH of amino acids 22-139 of instant SEQ ID NO: 489 with a VL of amino acids of 155-261 of instant SEQ ID NO: 489, and
Anti-CD3 of a VL of amino acids 398-504 of instant SEQ ID NO: 485 with a VH of amino acids 267-382 of instant SEQ ID NO: 485. (Example 42)
State of the Relevant Art
It has been well established in the art that the formation of an intact antigen-binding site in a conventional antibody requires the association of the complete heavy and light chain variable regions of a given antibody, each of which comprises three CDRs (or hypervariable regions) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro et. al., Front. Immunol. 2018; 8:1751 (PTO-892) (see Section “The IgG Molecule” in paragraph 1 and Figure 1). While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule”, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7). But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure of each monoclonal antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). The epitope of an antibody does not provide structure or sequence information about the antibody that binds it.
Further, the skilled artisan has long recognized that even minor changes in the amino acid sequences of the VH and VL, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Brown et al., J. Immunol., 156(9):3285-91 (1996) (PTO-892). Brown teaches that although a single amino acid change in CDR2 of heavy chain of a particular antibody was tolerated, the antibody lost binding upon introduction of two amino acid changes in the same region. Brown, p. 3290 and Tables 1 and 2. Table 1 of Brown shows that even a conservative substitution does not ensure that functionality of the antibody is retained. These older citations are supported my more recent discoveries of why these substitutions change antibody activity. Marvin et. al., Biochemistry, 42(23):7077-7083 (2003) (“Marvin” PTO-892) teaches that changes to the heavy and light chains altered binding affinity (Table 2) with changes to the CDR having large impacts but the changes with the largest impact were from residues in the CDR, but not from ones interfacing with the antigen ( Page 7081 in col 1 “Conclusions and Discussion” and Page 7082 in Figure 4).
This is further confirmed by Chiu et al., Antibodies, 8(55):1-80. (2019) (“Chiu” PTO-892). Chiu teaches that the complementarity-determining regions (HCDRs 1-3 and LCDRs 1-3) determine antigen binding requiring specific sequences and orientation of those sequences to properly form tertiary structures that can recognize and bind antigens (Page 4 in 1.2.2 first and last paragraphs and Figure 3). Chiu teaches that antibody modeling with known LCDRs 1-3, HCDR1 and HCDR2 could not predict HCDR3. The field has shown repeatedly over decades that Structure-Based antibody engineering is unable to predict antibody sequences (Page 6 in 1.2.6, Pages 10-11 in Section 2 in particular second paragraph of page 11). Chiu notes the advancement in antibody engineering but notes it is still not possible to predict the point mutations that would improve affinity in both antibodies and multispecific molecules (Page 51 in lines 6-12).
In general, absent at least the conserved structure of the CDRs of the heavy chain and light chain of an antibody, the skilled artisan generally would not be able to visualize or otherwise predict an antibody with a particular set of functional properties would look like structurally. An epitope does not inform one of skill in the art of the structure of the antibody that binds it and a partial structure of only some CDRs or some of the CDR sequences does not provide sufficient information to identify the undefined CDR identity.
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that 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.
The specification discloses 3 bispecific T-cell engagers that bind CD3 and DLL3. All three bispecific T cell engagers comprise the same CD3 binding domain and use the three disclosed DLL3 binding antibodies.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied 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. To meet this requirement in the instant case, the specification must describe structural features that the skilled artisan as of the effective filing date would have expected to convey the claimed binding activity.
The binding activity of an antibody alone as part of a bispecific antibody come from the CDRs of the antibodies of the heavy and light chains. The CDRs are the structure that provide function. A distinct combination of 6 CDRs found in the heavy and light chain of antibodies provide only the structure and function of that antibody and does not provide one of skill in the art with additional structures that would have the same function of binding an antigen. A partial structure of an antibody or bispecific antibody would not provide one of skill in the art with the full structure required for the function of a bispecific T-cell engager that binds DLL3 and CD3.
The epitope of an antibody does not provide any structure for the antibodies that bind it and a partial structure for an antibody does not provide one of skill in the art with
Conclusion:
For all of the reasons presented above, one of skill in the art would not know which combinations of heavy and light chains with varying CDRs would meet the structural and functional requirements of the claims. The applicant has not provided a representative number of species for all of the bispecific T cell engagers that would bind CD3 and DLL3. The functional structure of an antibody are its 6 CDRs that provide its binding activity based on the sequences of those CDRs, the CDRs of one antibody do not provide one of skill in the art with the functional CDRs of additional antibodies so the variability of the CDRs of the rejected claims mean there is no structure/function correlation, and the disclosed species do not provide written description for additional antibodies. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as claimed.
The rejection could be overcome by limiting the claims to the applicant disclosed heavy and light chain bispecific T cell engagers that applicant showed possession of.
Rejections Maintained – Updated as Necessitated By Applicant Amendment
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 3-6, 9-12, 14-17, 19, 21-22, 24, 27-34, 41-44, 48, 52, and 56-66 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 31-59 and 61-84 of copending Application No. 17/320,200 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites mutations to FLG, purI, msbB, asd, csgD, ansB, (claims 43 and 55-57). The reference application recites a lack of flagella. The reference application recites a strain with deletion of pagP, msbB, purI, csgD (claims 43, 45-48, and 55,). The reference recites the complete deletion of purI (claim 46).
The reference application recites an immunostimulatory protein comprising a human STING protein with a gain of function mutation of R284G and N154S, that is constitutively active with a non-human CTT including applicant’s elected CTT from a Tasmanian devil. The reference application recites the immunostimulatory bacterium comprising the modified STING confers anti-tumor immunity in the tumor microenvironment. The reference application recites the contribution to anti-tumor immunity in a tumor microenvironment. The reference application recites reduced recognition to TLR2, TLR4, and TLR5. The reference application recites the bacterium is salmonella typhimurium. The reference application recites the amino acid modifications confer constitutive production of type I IFN. (Claims 49, 52, 56).
The referent application recites the bacterium comprises one or more cytokine, chemokine, a costimulatory protein or receptor. The reference application recites IL-2, IL-7, IL-15/IL-15R alpha chain complex, or effects 4-1BB or 4-1BBL among others (claim 32-36, 42, 44, and 62).
The reference application recites a delivery vehicle and a pharmaceutical composition. The reference application recites the use of an IRES domain and a poly-A tail. (claim 58).
The reference application recites SEQ ID NO:306 which matches instant SEQ ID NO: 306 and SEQ ID NO: 353 which matches instant SEQ ID NO: 371. The reference application recites comprising a human STING protein with a gain of function mutation of R284G and N154S, that is constitutively active with a non-human CTT including applicant’s elected CTT from a Tasmanian devil (claims 66-69)
The reference application recites a human STING with a non-human CTT including applicant’s elected CTT from a Tasmanian devil including applicant’s elected species of instant SEQ ID NO: 371 which matches applicant’s SEQ ID NO: 371. The reference application recites the amino acid modifications confer constitutive production of type I IFN. The reference application recites a human STING protein with a gain of function mutation of R284G and N154S, that is constitutively active with a non-human CTT including CTT from a Tasmanian devil.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 3-6, 9-12, 14-17, 19, 21-22, 24, 27-34, 38-44, 48, 52, and 56-66 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-40 of copending Application No. 18660096 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other.
The reference application recites an immunostimulatory bacterium that produces the modified STING of the instant claims in a plasmid that further comprises further immunotherapeutic products.
The reference application recites deletion of FLG, purI, msbB, asd, csgD, ansB, pagP, and thyA (claims 8-9 and 36).
The reference application recites anti-cancer and therapeutic properties (claim 15).
Regarding claims 38-40, the reference application recites a bispecific T cell engager that binds DLL3 and CD3 of the heavy and light chains of the claims (claim 25).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Applicant Arguments
Applicant argues the Double Patenting Rejections are improper for the following reasons:
The pending and co-pending applications would not extend the right of exclusivity as no patents have been issued in the pending or copending cases.
The Restriction Requirement of record in this case dated 05/27/2025 prevents a double patenting rejection citing MPEP 806 and 804.01.
Applicant argues the claims to a genus do not recite the species.
Response to Arguments
Applicant's arguments filed 03/24/2026 have been fully considered but they are not persuasive.
The instant application is not a DIV that is the result of a restriction requirement of the parent case 17320200, but rather a CIP. Thus, the instant application is not protected by the 35 U.S.C. 121 shield. Copending application 18660096 is not a parent or child case of the instant application or of 17320200 and not protected by 35 U.S.C. 121 shield.
The claimed subject matter of 17/320,200 and 18660096 are overlapping in scope with the instant claims by being product claims to modified immunostimulatory bacterium with the same deletions and produce the same therapeutic products as detailed in the rejections under Double Patenting.
New Rejection Necessitated By Rejoinder of Previously Withdrawn Claims
Claims 38-40 and 44 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 31-59 and 61-84 of copending Application No. 17/320,200 (reference application) in view of Dylla (WO 2017031458 A2) (PTO-892).
The reference application recites mutations to FLG, purI, msbB, asd, csgD, ansB, (claims 43 and 55-57). The reference application recites a lack of flagella. The reference application recites a strain with deletion of pagP, msbB, purI, csgD (claims 43, 45-48, and 55,). The reference recites the complete deletion of purI (claim 46).
The reference application recites an immunostimulatory protein comprising a The reference application recites the contribution to anti-tumor immunity in a tumor microenvironment. The reference application recites reduced recognition to TLR2, TLR4, and TLR5. The reference application recites the bacterium is salmonella typhimurium. The reference application recites the amino acid modifications confer constitutive production of type I IFN. (Claims 49, 52, 56).
The reference application recites the encoding of combination therapeutic products including cancer binding antibodies (claim 36).
The reference application does not recite a bispecific T cell engager that binds DLL3 and CD3 of the instant sequences.
This deficiency is filled by Dylla.
Dylla teaches bispecific T cell engager of SC16.34 with CD3 binding domains as BiTE technology teaches its use in the treatment of cancer (abstract, page 21 ub kubes 30-32, page 52 in lines 20-24, and claims 1-4)
It would have been obvious at the time the application was filed to substitute the antibody cancer therapeutic encoded by the bacterium of the reference claims with the bispecific T cell engager of Dylla. One of skill in the art would have been motivated by the recitations of bacterium that can encode varying cancer therapeutics and wish to use it with additional known in the art cancer therapeutics. The substitution would further be prima facie obvious as substitution of art equivalent antibodies that bind cancer antigens for use in treatment of cancer (see MPEP 2183). There would have been a reasonable expectation of success as the reference application recites varying therapeutics can be encoded by their bacterium.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claims allowable.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to FRANCESCA EDGINGTON-GIORDANO whose telephone number is (571)272-8232. The examiner can normally be reached Mon - Fri 8:00 - 5:00.
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/F.E./Examiner, Art Unit 1643
/JULIE WU/Supervisory Patent Examiner, Art Unit 1643
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