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 .
Status of Claims
Claims 1-13 are pending.
Sequence Requirements
This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 C.F.R. § 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 C.F.R. § § 1.821-1.825 for the reason(s) set forth below. In the instant case, Figure 1 describes sequences that are not followed by a specific sequence identifier either in the text or the Figure. Additionally, the specification sets forth multiple sequences that are not followed by a specific sequence identifier. Full compliance with the sequence rules is required in response to this office action.
Priority
Acknowledgment is made of applicant's claim for foreign priority based on an application filed in the Republic of Korea on 12-21-2021 as 10-2021-0184203. It is noted, however, that the priority document is not in English. The priority date assigned for search and examination purposes is the instant filing date of 11-14-2022.
Election/Restrictions
Applicant’s election of Group I and species of antibody in the reply filed on 12-9-2025 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)). Claims 4 and 8-13 are withdrawn from consideration as drawn to a non-elected invention.
Information Disclosure Statement
The information disclosure statement has been considered. An initialed copy is enclosed.
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.
Claims 5 and 6 are rejected under 35 U.S.C. 112(b), as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
As to claim 5, the term “the exogenous protein” lacks clear unambiguous antecedent basis in the independent claim. Claim 6 as depending on claim 5 is likewise rejected as it does not resolve the ambiguity. This issue may be resolved by amending the claims to state that “the exogenous protein in the exogenous recombinant protein is an_____”.
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 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.
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.
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 set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied 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.
Claims 1-3 and 5-7 are rejected under 35 U.S.C. 103 as being unpatentable over Kim et al (Applied Microbiology and Biotechnology, 106:2043-2052, 2022, published on-line March 1, 2022) in view of Lakshmann et al (US2018/0028693).
Kim et al teach “next generation” strategy for displaying target-specific monoclonal antibodies on the surface of GVNPs prepared from Halobacterium sp. NRC-1. Kim et al teach the isolation and preparation of gas vesicles at page 2045, column 1-2. Kim et al teach the preparation of recombinant DNA for bioengineering GVNPs using GvpCGB fusions produced in E. coli at paragraph bridging pages 2045-46 and Figure 2. Kim et al teach the combination of the isolated GVNPs with recombinantly produced exogenous GvpCGB fusions to produce a display vehicle for antibodies (see paragraph bridging page 2048-49 and last paragraph in column 1 of page 2050 and first paragraph on column2). Kim et al differ by not stripping the wt GvpC using urea and dialysis from the isolated gas vesicle before contacting with the exogenously produced recombinant fusion protein.
Lakshmann et al teach engineered gas vesicles where the process is isolating native GV (gas vesicles), stripping gvpC in 6M urea and the re-addition of recombinant engineered GvpC produced in E. coli (see Figure 2, panel d). Lakshmann et al exemplify using Ana GVs (see pages 2-3, paragraphs [0023-0024]). Figure 10 demonstrates engineering of GV surface properties and cellular targeting. Representatives of endogenously express GVs are Anabaena floc-aquae (ANA GVs) and Halobaceterium salinarum (Halo GVs) (see paragraph [0149]). Lakshmann et al teach that the fvpC proteins of the native GVs are removed by treating the GVvs with urea as shown in example 1 leaving the fvpA-based shell intact. The gvpC protein may be replaced by a wild-gvpC or a genetically modified gvpC variant see paragraphs [0199-0208]. GvpC can be engineered to attach a tag fuse to or insertion into a N-terminal, C-terminal region of a gvpC or variant gvpC. In some embodiments, the tag comprises a moiety that can be used for targeting a GV to a cell, such as a receptor-targeting peptide RGD, a tag to increase or decrease uptake of GVs by macrophages such as CD47 or RS. A tag can also comprise a functionalized moiety that can be sued for modular approaches in which the GV surface can be specifically covalent conjugated to other recombinant proteins, such as a SpyTag-SpyCatcher (see paragraph [0211]). Examples include AvaGVs and HaloGVs see Example 1, 3 and 5 at pages 22-23. Example 10 at page 26 teaches stripping of native gvpCs from AnaGVs by mixing in urea and the stripped GVs can be stored in PTB after dialysis against PBS to completely remove the urea. Lakshmann et al teach the stripping of GVs and re-addition of engineered gvpC variants at example 16 page 30 and fusion at Examples 17, 18 and 19 at page 31. Lakshmann et al teach that it is expected that gvpC in other species can be engineered to produce variants in a similar manner to Ana (see Example 32, paragraphs [0332]). GV production microorganisms are listed in Figure 22.
It would have been prima facie obvious to one skilled in the art at the time the invention was filed to modify the method of producing target-specific monoclonal antibodies on the surface of GVNPs prepared from Halobacterium sp. NRC-1 of Kim et al by stripping the native gvpC by means of urea treatment followed by dialysis and then adding the exogenous GvpCGB fusion because it would allow for consistent loading of the stripped GV and Lakshmann et al teach that GV particles can be stripped of their native gvpC and reloaded with exogenously produced recombinant fusion proteins useful for targeting or loading proteins for targeting.
Applicant cannot rely upon the certified copy of the foreign priority application to overcome this rejection because a translation of said application has not been made of record in accordance with 37 CFR 1.55. When an English language translation of a non-English language foreign application is required, the translation must be that of the certified copy (of the foreign application as filed) submitted together with a statement that the translation of the certified copy is accurate. See MPEP §§ 215 and 216.
Claims 1, 3 and 7 are rejected under 35 U.S.C. 103 as being unpatentable over Lakshmann et al (US2018/0028693).
Lakshmann et al teach engineered gas vesicles where the process is isolating native GV (gas vesicles), stripping GvpC in 6M urea and the re-addition of recombinant engineered GvpC produced in E. coli (see Figure 2, panel d). Lakshmann et al exemplify using Ana GVs (see pages 2-3, paragraphs [0023-0024]). Figure 10 demonstrates engineering of GV surface properties and cellular targeting. Representatives of endogenously express GVs are Anabaena floc-aquae (ANA GVs) and Halobaceterium salinarum (Halo GVs) (see paragraph [0149]). Lakshmann et al teach that the gvpC proteins of the native GVs are removed by treating the GVs with urea as shown in example 1 leaving the gvpA-based shell intact. The gvpC protein may be replaced by a wild-gvpC or a genetically modified gvpC variant see paragraphs [0199-0208]. GvpC can be engineered to attach a tag fuse to or insertion into a N-terminal, C-terminal region of a gvpC or variant gvpC. In some embodiments, the tag comprises a moiety that can be used for targeting a GV to a cell, such as a receptor-targeting peptide RGD, a tag to increase or decrease uptake of GVs by macrophages such as CD47 or RS. A tag can also comprise a functionalized moiety that can be used for modular approaches in which the GV surface can be specifically covalent conjugated to other recombinant proteins, such as a SpyTag-SpyCatcher (see paragraph [0211]). Examples include AvaGVs and HaloGVs see Example 1, 3 and 5 at pages 22-23. Example 10 at page 26 teaches stripping of native gvpCs from AnaGVs by mixing in urea and the stripped GVs can be stored in PBS after dialysis against PBS to completely remove the urea. Lakshmann et al teach the stripping of GVs and re-addition of engineered gvpC variants at example 16 page 30 and fusion at Examples 17, 18 and 19 at page 31. Lakshmann et al teach that it is expected that gvpC in other species can be engineered to produce variants in a similar manner to Ana (see Example 32, paragraphs [0332]). GV production microorganisms are listed in Figure 22. Lakshmann et al differ by not exemplifying Halo GVs with a recombinant gvpC-tag on the surface produced by the claimed process.
However, It would have been obvious to one having ordinary skill in the art at the time of filing to culture Halobacterium spp and obtain Gas vesicles according to the method of Lakshamann et al, strip the native gvpC from the Halo GVs according to the method for Ava GVs, purify the stripped Halo GVs and perform a re-addition of a exogenously produced recombinant gvpC comprising a protein having a tag for targeting the GV to a cell or a protein moiety capable of binding to other proteins such as the SpyTag because Lakshamann et al teach that the GVs of the disclosure are not limited to a particular bacterial source. Lakshamann et al teach that it was known that native gvpC could be stripped from archebacterial GVs and reassociated with an exogenously produced recombination gvpC fusion protein having a protein tag.
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Lakshmann et al (US2018/0028693) as applied to claims 1, 3 and 7 above and further in view of Hill et al (Microbiology 166:501-509, April 2020).
The teachings of Lakshmann et al are set forth supra. The teachings differ by not specifying that the Holo GVs are from Halobacterium sp NRC-1.
Hill et al teach that gas vesicles have been purified from a number of species and their applications in biotechnology have been shown by the art. The species are Halobacterium sp NRC-1, Anabaena flos-aquae and Bacillus megaterium (see page 501 abstract). Halobacterium sp NRC-1 has been engineered to display antigens from eukaryotic, bacterial and viral pathogens and are able to generate an immune response that has been quantified both in vitro and in vivo (see pages 503-505).
It would have been prima facie obvious to use Halobacterium sp NRC-1 in the method for preparing a gas vesicle nanoparticle as combined supra because Hill et al teach that the species produces GVs that already have demonstrated utility as a display platform.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Patricia Duffy whose telephone number is (571)272-0855. The examiner can normally be reached 8:00 am - 4 pm.
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, Daniel Kolker can be reached at 571-272-3181. 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.
/Patricia Duffy/Primary Examiner, Art Unit 1645