DETAILED ACTION
Final Rejection
Notice of Pre-AIA or AIA Status
1. 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
2. Applicant’s election without traverse of Group I claims 1-6 and 11-16 and a species “a multimer” in the reply filed on 01/16/2026 is acknowledged.
Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement the applicant’s election without traverse is made final.
Status of Claims
3. Claims 2-8 and 17 filed as per amended claim listing on 06/26/2026 are pending.
4. Non-elected claims 7-8 and 17 are withdrawn from consideration due to restriction/election.
5. Claims 2-6 are under examination in this office action.
Priority
6. This application is a U.S. National Phase of International PCT Application No. PCT/CN2021/120518 filed on September 26, 2021, which claims priority to Chinese Patent Application Serial No. 202011351390.9 filed on November 26, 2020.
Information Disclosure Statement
7. Two information disclosure statements (IDSs) submitted on 05/25/2023 and 10/02/2023 is filed in time and the submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Withdrawn Objections to Sequence Disclosures
8. Withdrawn Objections to Nucleotide and/or Amino Acid Sequence disclosures in view of applicant’s response and corrections.
Withdrawn Objections to Specification
9. Withdrawn Objections to Specification in view of applicant’s response and corrections.
10. Withdrawn Objections to the specification in view of applicant’s response and English translation of foreign references.
11. Withdrawn Objections to the specification applicant’s response and deletion of NCBI sequence accession number.
Withdrawn Claim Rejections - 35 USC § 112
12. Withdrawn rejection of claim 11 under 35 U.S.C. 112(b) in view of applicant’s claim cancellation.
Claim Interpretation
13. The claims in this application are given their broadest reasonable interpretation using the plain meaning of the claim language in light of the specification as it would be understood by one of ordinary skill in the art.
The claims 2-6 are interpreted to be directed to a modified HPV52L1 protein with modifications (deletion, insertion, substitution) in the amino acid sequences at the N-terminal and or the C-terminal end of L1 protein of HPV52 to improve expression, solubility and purification yield of the expressed truncated L1 protein of HPV52 to obtain multimeric (pentamers) protein or VLPs for diagnostics antigen and immunogen applications. As deemed necessary, the modified HPV52L1 protein encoding polynucleotide is codon optimized to express for higher yield in insect cells sf9 or yeast cells or prokaryotic E. coli, and expression vector plasmid, baculovirus vector is used to express the protein in a compatible cell culture system.
Claim Rejections - 35 USC § 102 (modified)
14. 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 2, and 5-6 are rejected under 35 U.S.C. 102(a)(1)/(a)(2) as being anticipated by Li et al 2016 (US9499591B2, 11/22/2016).
Li et al 2016 (US9499591B2) is in the art and anticipated instant claim 2 directed to a modified HPV52 L1 protein, which is as shown in the sequence SEQ ID No: 2 (Qy). The prior art SEQ ID NO: 1 (Db) has 100% amino acid sequence identity with a single amino residue that has a conservative substitution E447D as shown below. Conservative amino acid substitutions retain the essential characteristics of the truncated protein. As used in the invention, the term “conservative substitution” refers to amino acid substitutions which would not negatively affect or change the biological activity of a protein/polypeptide comprising the amino acid sequence e.g. amino acids having acidic side chains (for example, aspartic acid and glutamic acid) (See, column 7, lines 11-45). Thus, Li et al 2016 anticipated instant SEQ ID NO:2. Li et al 2016 disclosed that in another preferred embodiment, the truncated HPV52 L1 protein has an amino acid sequence as set forth in SEQ ID NO: 1 (See, US9499591B2, column 3 lines 53-68, claim 1, abstract). Lee et al 2016 disclosed that although the specific embodiments of the present invention have been described in details, those skilled in the art would understand that, according to the teachings disclosed in the specification, various modifications and changes can be made without departing from the sprit or scope of the present invention as generally described, and that such modifications and changes are within the scope of the present invention. The scope of the present invention is given by the appended claims and any equivalents thereof (See, US9499591B2, column 46, lines 31-39). Thus, it is within the scope of Lee et al 2016 prior art and has taught the claimed modified HPV52L1 protein.
Query Match 99.9%; Score 2615; Length 503;
Best Local Similarity 99.8%;
Matches 483; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSVWRPSEATVYLPPVPVSKVVSTDEYVSRTSIYYYAGSSRLLTVGHPYFSIKNTSSGNG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MSVWRPSEATVYLPPVPVSKVVSTDEYVSRTSIYYYAGSSRLLTVGHPYFSIKNTSSGNG 60
Qy 61 KKVLVPKVSGLQYRVFRIKLPDPNKFGFPDTSFYNPETQRLVWACTGLEIGRGQPLGVGI 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 KKVLVPKVSGLQYRVFRIKLPDPNKFGFPDTSFYNPETQRLVWACTGLEIGRGQPLGVGI 120
Qy 121 SGHPLLNKFDDTETSNKYAGKPGIDNRECLSMDYKQTQLCILGCKPPIGEHWGKGTPCNN 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SGHPLLNKFDDTETSNKYAGKPGIDNRECLSMDYKQTQLCILGCKPPIGEHWGKGTPCNN 180
Qy 181 NSGNPGDCPPLQLINSVIQDGDMVDTGFGCMDFNTLQASKSDVPIDICSSVCKYPDYLQM 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 NSGNPGDCPPLQLINSVIQDGDMVDTGFGCMDFNTLQASKSDVPIDICSSVCKYPDYLQM 240
Qy 241 ASEPYGDSLFFFLRREQMFVRHFFNRAGTLGDPVPGDLYIQGSNSGNTATVQSSAFFPTP 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 ASEPYGDSLFFFLRREQMFVRHFFNRAGTLGDPVPGDLYIQGSNSGNTATVQSSAFFPTP 300
Qy 301 SGSMVTSESQLFNKPYWLQRAQGHNNGICWGNQLFVTVVDTTRSTNMTLCAEVKKESTYK 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SGSMVTSESQLFNKPYWLQRAQGHNNGICWGNQLFVTVVDTTRSTNMTLCAEVKKESTYK 360
Qy 361 NENFKEYLRHGEEFDLQFIFQLCKITLTADVMTYIHKMDATILEDWQFGLTPPPSASLED 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 NENFKEYLRHGEEFDLQFIFQLCKITLTADVMTYIHKMDATILEDWQFGLTPPPSASLED 420
Qy 421 TYRFVTSTAITCQKNTPPKGKEDPLKEYMFWEVDLKEKFSADLDQFPLGRKFLLQAGLQA 480
||||||||||||||||||||||||||:|||||||||||||||||||||||||||||||||
Db 421 TYRFVTSTAITCQKNTPPKGKEDPLKDYMFWEVDLKEKFSADLDQFPLGRKFLLQAGLQA 480
Qy 481 RPKL 484
||||
Db 481 RPKL 484
Claim 3: Li et al 2016 (US9499591B2) taught added limitation a polynucleotide encoding the modified HPV52 L1 protein according to claim 2, wherein the sequence of the polynucleotide is whole-gene optimized using insect cell codons. Li et al 2016 disclosed insect baculovirus expression systems. A host cell comprising the polynucleotide or vector as recited above. The host cell includes, but is not limited to prokaryotic cells such as E. coli cells, and eukaryotic cells such as yeast cells, insect cells. The expression plasmid for expressing HPV structural proteins was codon-optimized to express HPV L1 and L2 gene efficiently in mammalian cells, thereby facilitating high efficient assembly of pseudovirion. Li et al 2016 comprise insect cells and bacilovirus and therefore it is inherent that a polynucleotide encoding the modified HPV52 L1 protein is codon-optimized to express HPV L1 and L2 gene efficiently in insect cells. (See, column 2, lines 48-62, column 4 lines 11-18, Example 7 lines 48-56).
Claim 5. Li et al 2016 (US9499591B2) taught added limitation, A vector comprising the polynucleotide according to claim 3, wherein the vector is selected from the group consisting of plasmid, recombinant Bacmid, and recombinant baculovirus (See, column 2, lines 48-62).
Claim 6. Li et al 2016 (US9499591B2) taught added limitation, A host cell comprising the vector according to claim 5, wherein the host cell is selected from the group consisting of E. coli, yeast cell, and insect cell. (See, column 2, lines 48-62, column 4 lines 11-18, claims 5-6).
Thus, based on the disclosures of Lee et al 2016 as recited above the instant claims 2-6 are anticipated.
Claim Rejections - 35 USC § 103 (modified)
15. 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.
16. Claims 2-6 are rejected under 35 U.S.C. 103 as being unpatentable over Li et al 2016 (US9499591B2, 11/22/2016), and further in view of Godi et al 2018 (J Gen Virol. 2019 Feb;100(2):237-245), Sun et al 2016 (Appl Microbiol Biotechnol (2016) 100:1231–1240), Wei et al 2018 (Emerg Microbes Infect. 2018 Sep 26;7(1):160), Ma et al 2008 (CN101245099A, 08/20/2008), Bhat et al 2018 (Glob J Biotechnol Biomater Sci. 2017; 4(1): 001-007), and The Protein Man’s Blog 2018 (PDF printout, G-Biosciences, Geno Technology Inc, Online publication, info.gbiosciences.com/blog/tips-for-preventing-protein-aggregation-loss-of-protein-solubility).
Claims 2-6: Li et al 2016 (US9499591B2) anticipated by instant claims 2-6 as recited supra and the disclosures are incorporated here in its entirety to render the claims obvious.
Li et al 2016 (US9499591B2) is in the art and teaches a truncated L1 protein of Human Papillomavirus Type 52, its coding sequence and preparation method, and a virus-like particle (VLP) comprising the protein, wherein the protein and the VLPs are useful for preventing HPV (particularly HPV52) infection, and a disease caused by HPV (particularly HPV52) infection, such as cervical cancer. The invention also relates to the use of the protein and the VLPs in the preparation of a pharmaceutical composition or a vaccine for preventing HPV (particularly HPV52) infection, and a disease caused by HPV (particularly HPV52) infection, such as cervical cancer. A truncated HPV52 L1 protein, wherein the truncated HPV52 L1 protein is different from wild type HPV52 L1 protein by a deletion of amino acid positions 2-35, 2-40, or 2-42 at an N-terminal of the wild type HPV52 L1 protein, wherein said truncated HPV52 L1 protein (See, abstract, claim 1). Li et al 2016 disclosed a truncated L1 protein of Human Papillomavirus Type 52 SEQ ID NO: 12 that has 99.9% amino acid identity with instant SEQ ID NO: 29 as recited below. A single amino acid difference in identity is due to a single conservative amino acid substitution in the reference database D434E of instant claimed SEQ ID NO: 29 (See, above 35 USC 102 anticipation rejection for claim 2 truncated HPV52L1 amino acid sequence, and claim 12 wild type HPV52L1 amino acid sequence).
Li et al 2016 does not teach (i) an alternative limitation of instant claim 1, D447E substitution, (ii) is not expressive regarding polynucleotide codon optimization for insect cell expression of HPVL52L1 the protein.
Godi et al 2018 is in the art of HPV52 L1 VLP and teaches an HPV 52 lineage D L1 protein containing D447E, VLPs (VLPs reads on multimer or pentamer), and codon-optimized gene, vectors, cells, and L1 and L2 pseudoviruses thereof. Homology models of the HPV52 L1 pentamer were generated which permitted mapping these residues to a small cluster on the outer rim of the surface exposed pentameric L1 protein. (See, Godi et al 2018, J Gen Virol. 2019 Feb;100(2):237-245, full article, pages 240 and 243, and figures 1-2, abstract, as recited in PCT written opinion on file (05/25/2023).
Claims 3-6: Li et al 2016 (US9499591B2) as recited supra teaches the modified HPV52 L1 protein according to claim 1. Li et al 2016 also teaches (instant claim 2 above) a coding sequence (reads on polynucleotide) of the truncated HPV52 L1 protein, a virus-like particle (VLP) comprising the protein, and a method of preparing the protein and the VLP. Li et al 2016 further disclosed SEQ ID NO: 12 that has 100% amino acid identity with instant SEQ ID NO: 29 as recited supra (with a single a single conservative amino acid substitution as compared to the prior art reference sequence “Aspartate” D434E “Glutamate” of instant claimed SEQ ID NO: 29. Li et al 2016 further teaches (the instant claim 12) the wild-type HPV52 L1 protein amino acid sequence (the prior art SEQ ID NO: 1) that has 100% amino acid identity with instant SEQ ID NO: 1 that is a wild type HPV52 L1 protein. Li et al 2016 teaches eukaryotic expression systems insect baculovirus vector system for HPV L1 protein expression, HPV52 virus-like particle, comprising or consisting of or formed from the truncated protein, and VLP production.
Li et al 2016 teaches a host cell comprising a polynucleotide or vector. The host cell includes but is not limited to prokaryotic cells such as E. coli cells, and eukaryotic cells such as yeast cells, insect cells. The host cell according to the invention may also be a cell line, such as 293T cell. Li et al 2016 teaches plasmid p52L1h, the pAAV vector carrying the nucleotide sequence encoding HPV52 L1 protein. Li et al 2016 teaches the expression plasmid for expressing HPV structural proteins was codon-optimized to express HPV L1 gene efficiently in mammalian cells, thereby facilitating highly efficient assembly of pseudo-virion (reads on VLPs).
Li et al 2016 (US9499591B2) disclosed SEQ ID NO: 14 that has 64.7% nucleotide sequence identity (78% best local similarity) with instant SEQ ID NO: 31 of instant claim 4 (instant claim 4).
Li et al 2016 teaches the polynucleotide sequence to express the claimed HPV52L1, insect cells for expression, and baculovirus vector. However, does not teach codon optimized polynucleotide whole-gene HPV52L1 optimized using insect cell codons.
Sun et al 2016 is in the HPVL1 VLP art and teaches a 21 amino acid NLS lacking C-terminally truncated HPV6 L1 polynucleotide sequence gene that is optimized for insect cell codons expression (codon optimized for insect cells) and production of the VLPs (See, abstract, page 1238 col 1 last para, page 1232 col 2 para 1, Fig. 6 a, b).
Wei et al 2018 is in the art and teaches N-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitro. We et al 2018 teaches up to 15 amino acid truncations at the N-terminal of HPV 52 L1 protein achieved increased expression and solubility for truncated protein constructs N5C, N10C, N15C and N19C. The nucleotide sequences, vectors, host cells, virus-like particles, vaccines and the like thereof, wherein N-terminal truncations can promote the expression of the L1 proteins are taught. In our previous work, we found that truncation of several N-terminal residues could improve proteins the solubility of HPV L1 (See, abstract, result, page 9, and figure 1 and legends). It would have been obvious to try for one of the ordinary skills to truncate the HPV52L1 N-terminal protein based on the teachings of Wei et al 2018 and attempt to obtain increased expression and solubility in eukaryotic expression system (e.g. insect cells, mammalian cells). It would have been "Obvious to try" to the ordinary skills by choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success by deleting 2, 4, 5, 8, 10, 13, 14, 15, 18, or 20 successive or non-successive amino acids at the N-terminus.
Ma et al 2008 (CN101245099A, 08/20/2008) discloses a recombinant HPV L1 capsid protein, being capable of being dissolved in water and expressed to obtain an Ll pentamer having the same immunogenicity and antigenicity as a wild type protein. Compared with the wild type protein, the N-terminal is substituted and the C-terminal is truncated. The amino acid sequence of the HPV52 L1 protein is shown in SEQ ID NO: 13 (see, claims 1-12, description).
Bhat et al 2018 is in the protein expression and purification art. Bhat et al 2018 teaches the protein solubility is achieved by the site-directed mutagenesis that generates the hydrophobic to hydrophilic mutations, a hydrophobic composition of protein adversely affects solubility, delete or mutate the hydrophobic residues which increase the protein expression and solubility. Alpha helices are stabilized by predominantly hydrogen bonds, while hydrogen bonding and hydrophobic interactions are the stabilizing forces for beta sheets. Exposed hydrophobic residues in a protein molecule in the cell due to misfolding or mutation tend to stick together and lead to the formation of insoluble aggregates called inclusion bodies in recombinant proteins (See, abstract, entire article).
Protein Man’s Blog 2018 is in the protein art and teaches adding a mixture of arginine and glutamate to your buffer increases protein solubility by directly binding to charged and hydrophobic regions (See, PDF printout).
Therefore, it would have been "Obvious to try" to the ordinary skills by combining the prior art teachings Wei et al 2018, Bhat et al 2018, and Protein Man’s Blog 2018 by choosing from a finite number of identified, predictable solutions, with a reasonable expectation of success by deleting 13 amino acids at the N-terminus and substituting N-terminal hydrophobic (non-polar) amino acids with hydrophilic (polar) amino acids and balance the hydrophobic and hydrophilic properties of the N-terminal domain of HPV52L1 protein with the alternative claimed limitations: any one selected from the group consisting of serine, serine-glutamate, serine-glutamate-arginine, and proline-serine-glutamate-alanine-threonine. (See, MPEP § 2143, example of rationales, A-G).
It would have been obvious to one of the ordinary skills in the art before the effective filing date of the claimed invention to modify the prior art teachings of Li et al 2016 as applied to claim 2 and relevant dependent claims with additional teachings of Godi et al 2018 on D447E mutation, and Sun et al 2016 on codon optimization and baculovirus expression for the HPV52 L1 polynucleotide sequence to produce the HPV52 L1 multimer protein or the HPV52 L1 VLPs taught by the prior arts Li et al 2016, HPV52L1 protein N-terminal 15 amino acid deletions by both Wei et al 2018, and Ma et al 2008, hydrophobic amino acid substitutions or deletion approach taught by Bhat et al 2018, and the insight provided by Protein Man’s Blog 2018 on hydrophobic protein property neutralization by addition of hydrophilic amino acid (e.g. mixture of arginine and glutamate) addition to increase solubility of protein to arrive at the inventions of claims 2-6. One of the ordinary skills in the art would have been motivated to develop a codon optimized baculovirus expression vector for expression of the claimed HPV52L1 in the insect cells (e.g. Sf9) for producing soluble protein for purification, HPV52 L1 VLPs for production of immunogens, vaccines and diagnostic antigens for commercial success. There would be a reasonable expectation of success given the applied prior art teachings in the art as recited supra. This is analogous to some teaching, suggestions, or motivation in the prior art that would have led one of ordinary skill to modify the prior art reference or to combine prior art reference teachings to arrive at the invention as claimed in claims 2-6. See KSR Int'l Co. v. Teleflex Inc., 550 U.S. 398, 415-421, 82 USPQ2d 1385, 1395-97 (2007) (see MPEP § 2143, example of rationales, A-G).
Response to Arguments
17. Applicant’s arguments with respect to claim(s) filed in response to non-final rejection office action mailed on 03/30/2026 have been considered but are moot because the new ground of rejection does not rely only on teachings of reference applied in the prior rejection of record for any teaching or matter specifically challenged in the argument. Additional teachings from prior art were applied.
18. Relevant Prior Arts:
Merck Sharp and Dohme BV. (CN 1934131 A, 21 March 2007). Optimal Expression of HPV52 L1 in Yeast.
Arifah et al 2025. Truncation on N-Terminal Hydrophobic Domain of L1 Major Capsid Protein of Human Papillomavirus Type 52 Enhances Its Expression in Hansenula polymorpha. HAYATI Journal of Biosciences 32(4):1062-1072 (Year: 2025).
Conclusion
19. No claim is allowed.
20. 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).
21. 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 SAMADHAN J JADHAO whose telephone number is (703)756-1223. The examiner can normally be reached M-F 8:00-5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Thomas J Visone can be reached at 571-270-0684. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/SAMADHAN JAISING JADHAO/Examiner, Art Unit 1672
/BENNETT M CELSA/Primary Examiner, Art Unit 1600
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