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
This action is in response to the papers filed on 10/02/2025. Claims 1-3,7-8,10-13,15-17 and 19-30 are currently pending as per claims filed on 12/30/2022.
Applicant’s election of Group I, which include claims 1-3, 7, 8, 10-13, 15, 16, 19-26, and 28-30, and election of species for Group I, a peptide as the species attached to the second peptide binding partner and DogTag and DogCatcher as the first peptide partner and the second peptide partner, respectively in the reply filed on 10/02/2025 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
After further consideration, the requirement for the election of species for a first and second binding partner has been withdrawn as there is no undue search burden.
Claims 17 and 27 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 10/02/2025.
The requirement for restriction between Groups I-III is still deemed proper and is therefore made FINAL.
Therefore, claims 1-3, 7, 8, 10-13, 15, 16, 19-26, and 28-30, are subject to examination to which the following grounds of rejection are applicable.
Priority
The instant application is a 371 of PCT/GB2020/052774 filed 11/02/2020, which claims foreign priority to UNITED KINGDOM 1915905.2 filed 11/01/2019.
Thus, the earliest possible priority for the instant application is 11/01/2019.
Specification
The disclosure is objected to because of the following informalities: The figure legend on Pg. 23 of the specification is titled as Figure 4 {A-C), however the drawings and the legend contents reference Figure 4D. Appropriate correction is required.
Drawings
The drawings filed 04/29/2022 are objected to as failing to comply with 37 CFR 1.84(p)(5) because they do not include the following reference sign(s) mentioned in the description: The drawings are missing several labels, for example, in Figure 6 the drawings do not have labels for A-B and D-E. Figure 11 is only partially scanned and is missing labeling for A-B. Figure 14 is missing the labeling for A.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 04/29/2022, 12/30/2022, 08/30/2024, 10/22/2024, and 05/22/2025 were filed before the mailing date of the non-final office action. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
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 1-3, 7, 8, 10-13, 15, 16, 19-26, and 28-30 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.
Claim 1 and by dependence, claims 2-3, 7, 8, 10-13, 15, 16, 19-26, and 28-30 are vague and indefinite in the recitation of “…capable of…” , since this phrase refers to a latent ability, and it is unknown whether the ability is expressed or observed in the invention.
Note, it has been held that the recitation that an element is “capable of” performing a function is not a positive limitation, but only requires the ability to so perform. It does not constitute a limitation in any patentable sense. In re Hutchinson, 69 USPQ 138. For the sake of compact prosecution, the examiner will consider the meaning of the claim to require the inclusion of the bound second peptide partner. Claim 1 is also rejected due to the recitation of the phrase “an adenoviral vector including an adenovirus”. The practitioner in the art would readily understand that an adenoviral -based vector is an adenovirus. It is unclear what applicants intended mean is for “…including an adenovirus”. Is the intended meaning a nucleic acid molecule encoding a capsid protein? Therefore, the claim is rendered indefinite. Applicant must plainly state what they intend to claim.
Claims 2-3,7, 8, 10-13, 15, 16, 19-26, and 28-30 are dependent upon and inherit the deficiencies of claim 1. Claim 3 recites the term “and/or” in line5. It is unclear what the metes and bounds of this term, as “and” could be interpreted to include only a modification of a hexon protein, a modification of piX protein, an insertion of the first peptide partner, a fusion of the first peptide partner, any number of modifications for each recited protein, any number of modifications for all recited proteins thereof, or “or” would imply that every component of the recited claim are in the alternative. Appropriate correction is required.
Claim 15 recites, “…wherein the second peptide partner is attached to the antigen and the antigen includes a structure specifically expressed on a tumour, a cancer cell, or a virus.” It is unclear what the applicant intends to claim within the phrase “includes a structure specifically expressed on a tumour, cancel cell, or a virus”. Are these inclusions a separate entity from “the antigen”? Did the applicant intend for these inclusions TO BE the antigen to which the claim references? For the sake of compact prosecution, the claim will be examined to require the antigen referenced IS a structure known to be expressed from one of the recited tumour, cancer cell, or a virus”. Claims 16 is dependent upon and inherits the deficiencies of claim 15.
Claim Interpretation
Claim 19 recites, “A kit comprising the adenoviral vector of claim 1”. The claim as written is interpreted as the only requirement for the kit being the vector of claim 1. Furthermore, the description related to a kit as provided by the specification on Pg. 21, Lines 6-27 does describe requirements other than the vector. Therefore, any prior art teaching the vector of claim 1 will read on the kit of claim 19.
Claim Rejections - 35 USC § 102
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 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 1, 3, 19 and 22-26 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Kreppel et al. (KREPPEL, F. et al., Molecular Therapy, (2005), IDS filed 04/29/2022) as evidenced by Farson et al. (Farson D et al., Mol Ther. 2006) and as evidenced by Donnelly et al. (Donnelly OG et al., Curr Pharm Biotechnol. 2012).
Regarding Claim 1 and 19, Kreppel teaches generation of an adenoviral vector with genetic and chemical modification of the adenovirus capsid. Kreppel teaches introduction of peptides comprising cysteine residues (first peptide partner), “We generated three Ad5-based, E1-deleted adenovirus vectors that had been genetically modified to present in the solvent-exposed fiber HI-loop the short cysteine containing motifs LIGGGCGGGID (Ad1Cys), LIGCGCGCGID (Ad3Cys), and LICCCCCID (Ad5Cys).” (Pg. 108, 1st Paragraph of Results). The introduced thiol groups are shown to covalent bind to transferrin (attached to second peptide partner) via an NHS-PEG3400-Mal linker (Pg. 110, Section: Maleimide-Based Chemical Coupling of the High-Affinity Ligand Transferrin Efficiently Targets Vector Particles to the Transferrin Receptor). As discussed in the claim interpretation above, the teachings of Kreppel provided in the 102 rejection anticipate the kit of instant claim 19. Regarding Claim 3, the modification of the capsid protein taught by Kreppel includes insertion of a cysteine residues in the solvent-exposed fiber HI-loop the short cysteine containing motifs LIGGGCGGGID (Ad1Cys), LIGCGCGCGID (Ad3Cys), and LICCCCCID (Ad5Cys).” (Pg. 108, 1st Paragraph of Results) in the adenovirus capsid.
Regarding Claim 22, Kreppel teaches the vector as described above in the rejection of instant claim 1. The contains a second peptide partner attached to a transferrin (targeting moiety). Adenovirus was known in the art to be an oncolytic virus as evidenced by Donnelly et al., who teaches “…six oncolytic viruses (adenovirus, reovirus, measles, herpes simplex, Newcastle disease virus and vaccinia)” (Abstract of Donnelly et al.). Although exemplary preparations are provided in the instant specification, as recited in the claim the requirement for this preparation is only vector as taught by Kreppel. Therefore, the teachings of Kreppel anticipate the instant claim.
Regarding Claims 23-25, Kreppel teaches their adenovirus vectors are Ad5 (human adenovirus)-based, E1-deleted (replication-incompetent) (Pg, 108, Results, 1st Paragraph). These vectors require E1-complementing cells (such as 293) to allow for replication. Therefore, replication is only possible in “selected cells” . This is evidenced by the teachings of Farson et al. Farson discloses, “Recombinant adenoviruses have predominantly been rendered replication defective or conditionally replicating via modifications to the E1 region, such as deletions, mutations, or replacement of the endogenous transcriptional control elements” (Abstract, 1st Paragraph) and “In 293 cells, a continuous adenovirus type 5 (Ad5) DNA fragment containing both E1A and E1B genes (nucleotides 1 to 4344) was integrated into chromosome 19 at 19q13.2. Since many first-generation adenoviral vectors are deleted from nucleotide (nt) 400 to nt 3500, the viral genome may have significant homology to the integrated viral DNA fragment in the host cell DNA. This homology between cellular DNA and viral genome can mediate double crossover recombination [9]. Therefore, 293-cell-derived viral E1 DNA may rescue the E1 deletion in the viral products and generate replication-competent adenovirus (RCA).” (Abstract, 2nd Paragraph).
Regarding Claim 26, Kreppel teaches the adenovirus comprises GFP (transgene) (Fig. 4).
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) 2, 7-8, 10-13, 15, 20 and 28-29 are rejected under 35 U.S.C. 103 as being unpatentable over Kreppel et al. (KREPPEL, F. et al., Molecular Therapy, (2005), IDS filed 04/29/2022)) as applied to claim 1 above in view of Sabin et al. (WO 2019/006046 A2, IDS filed 04/29/2022) as evidenced by Zakeri et al. (ZAKERI, B. et al., PNAS, (March 2012), IDS filed 12/30/2022), and as evidenced by Schoene et al. (Schoene C et al., Chem Int Ed Engl. 2014).
Kreppel anticipates claim 1, as iterated above in the 102 rejection, the content of which is incorporated herein, in its entirety. Regarding Claims 2, 7-8, and 10-11, 13, Kreppel teaches that adenoviral capsid proteins can be genetically modified to include peptide motifs that enable covalent attachment of peptide binding partner (such as a ligand, transferrin) using a cysteine based covalent coupling.
However, Kreppel does not teach specifically teach an isopeptide bond as the covalent bond formed between the first and second peptide partner. Kreppel does not teach an antigen bound (elected species) to the second partner via fusion or chemical attachment or that the first and second partner are bound via isopeptide bond. The size of the second peptide partner is not explicitly disclosed by Kreppel as required in instant claim 12. Kreppel does not teach a tag/catcher system as the first and second partner. Kreppel teaches their targeting approach is appropriate for rational development of vaccines (Pg. 107, final paragraph), but does not specifically teach the use of their vector within a vaccine as recited in claim 15.
Sabin cures the deficiencies of Kreppel as Sabin teaches the targeting ligands are fused to the second peptide (paragraph [0029]), the targeting ligands can be bound to antigens (Pg. 19, continuation of paragraph [0032]), and the targeting ligand bound to a second peptide partner may bind a tumor-associated antigen (paragraphs [0029] - [0030], [0032]), as recited in instant claim 11. This reads on the peptide attached to the second binding partner in instant claim 2, the binding via fusion in instant claim 10, and the antigen being a tumor-associated antigen in instant claim11.
Moreover, Sabin teaches “compositions and methods for redirecting recombinant viral capsid particles via a specific protein:protein binding pair that forms a covalent, e.g., isopeptide (for instant claim 7), bond to display a targeting ligand on the capsid protein, wherein the targeting ligand specifically binds a cell surface marker expressed on the cell of interest.” (Abstract). Specifically, Sabin teaches recombinant viral vectors (claims 37-44 of Sabin) which comprise a capsid protein modified to comprise a protein:protein binding pair bound by an isopeptide bond (claims 3, 14-22 of Sabin) wherein the second member of the binding pair is linked to a targeting ligand (claim 4 of Sabin). Sabin teaches the virus may be an adenovirus of various serotypes (paragraphs [0020], [0043], [0093]), that one member of the binding pair may be inserted into the HI loop of the adenovirus fiber knob domain (paragraphs [0022], [0093], [0095]). Sabin also teaches various tag/catcher pairs for the protein:protein binding pair linked by an isopeptide bond (paragraphs [0027], [0078], [0080] - [0082], [0092]), including spytag/spycatcher and snooptag/snoopcatcher as recited in instant claim 8. Further, the use of tag/catcher systems such as spytag/spycatcher to enable rapidly forming isopeptide bonding was established in the art at the time of the instant application and has been shown to provide an known alterative with predictable advantages to previous systems, as evidenced by Zakeri et al. Zakeri teaches a spytag/catcher system (Figure 1), and discloses multiple positive characteristics: a high tolerance to a range of environmental pressures (pH and temperatures), requiring no artificial amino acids or added cofactors, high specificity to peptide partner, and rapid formation of isopeptide bonding (Zakeri, Author Summary). Spycatcher is also a 15kda protein as evidenced by Schoene et al. who states, “We engineered SpyTag, a 13 amino acid peptide, to rapidly form an irreversible amide bond to the 15 kDa protein SpyCatcher.” (Pg. 6101, 2nd Column, 1st full paragraph) which reads on the molecular weight requirement of claim 12.
Sabin also describes vaccine utility of their invention “the utilization of a specific binding pair (SpyCatcher: SpyTag) to generate virus like particles (VLP) from a modified bacteriophage AP205 displaying immunogenic antigens at a high density on a the AP205 capsid for the purposes of vaccination [Pg. 38, Paragraph [0060]). The antigen within their vaccine being a structure expressed from a cancer [Pg. Paragraph 0104, last line) as in instant claims 15 and 20. It would have been obvious to a person of ordinary skill in the art at the time of the instant application to modify the adenoviral vector containing a cysteine-based covalent coupling system taught by Kreppel to incorporate the isopeptide-bond forming tag/catcher system (including the antigen-linked second peptide) taught by Sabin to enhance the vector by providing a well characterized system (as evidenced by Zakeri) enabling a modular, covalent, display of targeting ligands of interest, such as antigens for use in a vaccine development.
Regarding the rationale for combining prior art elements according to known methods to yield predictable results, all of the claimed elements were known in the prior art and one skilled in the art could have combined the element as claimed by known methods with no change in their respective functions, and the combination would have yielded predictable results to one of ordinary skill in the art at the time of the invention.
The skilled artisan would have had a reasonable expectation of success in combining the teachings of Kreppel and Sabin because the molecular biology required to produce an adenovirus vector comprising a modified capsid protein containing a first peptide partner of a tag/catcher system had been practiced prior to the filing of the instant application.
Therefore, the adenoviral vector containing a peptide binding pair as taught by Kreppel in view of Sabin would have been prima facie obvious over the adenoviral vector of the instant application.
With respect to instant claim 13, the recitation of “wherein the second peptide partner attached to the antigen, targeting moiety, or shielding entity shields the adenovirus from antibody binding to the capsid.” would be an inherent effect of the vector taught by Sabin and Kreppel. Therefore, the effect of the vector, as recited in instant claim 13, is taught by Sabin and Kreppel, absent evidence to the contrary.
The discovery of a new use for an old structure based on unknown properties of the structure might be patentable to the discoverer as a process of using. In re Hack, 245 F.2d 246, 248, 114 USPQ 161, 163 (CCPA 1957). However, when the claim recites using an old composition or structure and the "use" is directed to a result or property of that composition or structure, then the claim is anticipated. In re May, 574 F.2d 1082, 1090, 197 USPQ 601, 607 (CCPA 1978) and In re Tomlinson, 363 F.2d 928, 150 USPQ 623 (CCPA 1966). See M.P.E.P. § 2112.02.
Regarding Claim 28, Sabin teaches the targeting ligand of the second peptide partner may be bound to CD markers associated with immune response, (Pg. 60, Paragraph [0107]) and the invention may be used as a therapeutic to enhance immune response (Pg. 68, Paragraph [0143]).
Regarding Claim 29, Sabin teaches the targeting ligand of the second peptide partner may be bound to viral antigens, including from HPV (HPV E2, HPV E6, HPV E7)(Pg. 19, Paragraph [32]).
Claim 30 is rejected under 35 U.S.C. 103 as being unpatentable over Kreppel et al. (KREPPEL, F. et al., Molecular Therapy, (2005), IDS filed 04/29/2022)) as applied to claim 1, 2, 10-11 and 29 above in view of Sabin et al. (WO 2019/006046 A2, IDS filed 04/29/2022) as evidenced by Zakeri et al. (ZAKERI, B. et al., PNAS, (March 2012), IDS filed 12/30/2022), and as evidenced by Schoene et al. (Schoene C et al., Chem Int Ed Engl. 2014) and further in view of Du et al. (Du L et al., Nat Rev Microbiol., 2009) Kreppel and Sabin as evidenced by Zakeri and Schoene together teach the adenovirus vector as described above. Sabin teaches antigens from known viruses within the vector. However, they do not teach an antigen from the SARS-CoV-2 virus used as an antigen.
Du et al. teaches SARS-CoV vaccines containing antigens such as the S protein were well established in the prior art at the time of the instant application (Pg. 229, Section: Vaccines SARS-CoV protein; Table 1.). It would have been prima facie obvious to one of ordinary skill in the art at the time of the instant application to modified the vector as taught by Kreppel and Sabin to include a SAR-COV protein, such as the S protein, as taught by Du et al. Further, through rational vaccine development, would having skill in the art would optimize the vector to include an antigen of the most prevalent variant of SARS-CoV, which at the time would have been SARS-CoV-2. One would have been motivated to combine these teachings as it would allow for the production of a vector that could be rationally used and optimized for production and testing of a vaccine to be used as a therapeutic for SARS-CoV-2. The skilled artisan would have had a reasonable expectation of success in combining the teachings of Kreppel and Sabin with those of Du because the molecular biology required to isolate an S protein for SAR-CoV and produce a vaccine using the vector as taught by Kreppel and Sabin, with the inclusion of the S protein to act as an antigen as taught by Du as these techniques had been practiced prior to the filing of the instant application.
Therefore, the adenoviral vector containing a peptide binding pair as taught by Kreppel in view of Sabin modified to contain an antigen from the SAR-CoV virus would have been prima facie obvious over the adenoviral vector of the instant application.
Nonstatutory 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 1-3, 7, 8, 10-13, 15, 16, 19-26, and 28-30 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-12, 15-19 of US Application 18558898. Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are obvious over the cited claims of US Application 18558898.
Claim 1 of US Application 18558898 is directed to:
An adenoviral vector encoding a heterologous transgene encoding an antigen and wherein the vector has at least one modified capsid protein, said modification comprises the inclusion of a first peptide partner covalently bonded to a second peptide partner, wherein the second peptide partner is attached to an antigen, characterized in that the antigen encoded by the transgene has at least one T cell epitope and the antigen attached to the second peptide partner has at least one B cell epitope.
Claim 1 of the invention is directed to:
An adenoviral vector including an adenovirus, comprising at least one modification in a capsid protein, wherein the at least one modification comprises inclusion of a first peptide partner in a capsid protein, and the first peptide partner is capable of forming a covalent bond with a second peptide partner.
This is an obviousness-type double patenting rejection is, which is appropriate where the conflicting claims are not identical, but an examined application claim not is patentably distinct from the reference claim(s) because the examined claim is anticipated by the reference claim(s). This type of obviousness-type double patenting situation arises when the claim being examined is, for example, generic to a species or sub-genus claimed in a potentially conflicting patent or application. The species of an adenoviral vector encoding a heterologous transgene encoding an antigen and wherein the vector has at least one modified capsid protein, said modification comprises the inclusion of a first peptide partner covalently bonded to a second peptide partner, wherein the second peptide partner is attached to an antigen, characterized in that the antigen encoded by the transgene has at least one T cell epitope and the antigen attached to the second peptide partner has at least one B cell epitope are species of the instant claims and render the instant claims obvious. In such a situation, a patent to a genus would, necessarily, extend the rights of a species or sub-genus should the genus issue as a patent after the species or sub-genus. It is well established that a species of a claimed invention renders the genus obvious. In re Schaumann , 572 F.2d 312, 197 USPQ 5 (CCPA 1978). This is a provisional obviousness-type double patenting rejection because the conflicting claims have not in fact been patented.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KODYE LEE ABBOTT whose telephone number is (703)756-1111. The examiner can normally be reached M-F 8-5.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Maria G. Leavitt can be reached at (571) 272-1085. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/KODYE LEE ABBOTT/Examiner, Art Unit 1634
/MARIA G LEAVITT/Supervisory Patent Examiner, Art Unit 1634