DETAILED ACTION
Non-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 with traverse of Group I, Claims 1-12, 15, and 16 in the reply filed on 01/09/2026 is acknowledged.
Applicant elected species of the VLP binding agent (antibody) sequences comprising SEQ ID NO: 27 and SEQ ID NO: 31.
Response to traversal: The lack of unity is shown when the “common technical subject matter” encompasses subject matter that does not constitute a “special technical feature”.
The lack of unity is justified since a reference has been supplied to demonstrate lack of a “special technical feature” regarding the common subject matter. Narrower claim embodiments (e.g. dependent claims) are not relevant regarding if the common technical subject matter is broader.
Demonstrating a lack of a special technical feature demonstrates lack of unity that is needed as a basis for both restriction and a species requirement.
Accordingly, a showing of undue burden (search and/or examination burden) is not necessary in PCT lack of unity practice.
In any event, the restriction provides evidence of an undue burden of search and/or examination.
The requirement is still deemed proper and is therefore made FINAL.
Withdrawn Election of Species “VLP Binding Agent Sequences”
Withdrawn election of species for the VLP binding agent for the amino acid sequence recited by SEQ ID NOs in claims 7-11 for compact prosecution. All claimed SEQ ID NO as recited in claims 7-11 are being examined in this office action.
Status of Claims
3. The claims 1-18, 23, 27, 39, 51, 73 and 91 filed on 12/08/2022 are pending.
4. Claims 13-14, 17-18, 23, 27, 39, 51, 73 and 91 are withdrawn due to restriction/election.
5. Claims 1-12, 15, and 16 (elected Group I) is under examination in this office action.
Priority
6. This application is a National Stage Entry of International Application
No. PCT/US2020/067394 filed December 30, 2020, and claims the benefit of U.S. Provisional Application No. 62/954,7 16, filed December 30, 2019.
Information Disclosure Statement
7. The two information disclosure statements (IDSs) submitted on 12/08/2022 are 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
8. 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 1-2, 5, 7 and 9 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: It is not clear whether “A VLP binding agent” encompass agent or structure other than derived from an antibody. The instant specification para [0004] provide an example “Accordingly, some embodiments of the present invention include virus-like particle (VLP) binding agents (e.g., antibodies and monoclonal antibodies) that have many uses including but not limited to detecting VLPs, parvovirus, erythrovirus, and parvovirus B 19, diagnosing parvovirus, erythrovirus, and parvovirus B19, and treating parvovirus, erythrovirus, and
parvovirus B19. The example provided does not exclude comprising additional “VLP binding agent”. Accordingly, the metes and bounds of the claim as encompassing antibodies or additional “agents” that are different from antibodies.
Claim 2: It is not clear at what amino acid position and what is the reference amino acid sequence of wild type VP2. What type of amino acid modification the claim 2 encompass. The specification does not appear to clarify this ambiguity.
Claim 5: It is not clear what is the sequence or structure of the claimed construct A, construct B, construct D, or construct F. The specification does not necessarily incorporate missing structure that may be meant to correspond to these recited constructs.
The claim 7 (dependent on claim 1) recites the added limitation, wherein the VLP binding agent comprises an amino acid sequence with (a) SEQ ID NOS:2-4 and 14-16, each with up to four conservative amino acid substitutions, (b) SEQ ID NOS:5-7 and 17-19, each with up to four conservative amino acid substitutions, (c) SEQ ID NOS:8-10 and 20-22, each with up to four conservative amino acid substitutions, or (d) SEQ ID NOS:11-13 and 23-25, each with up to four conservative amino acid substitutions.
The claimed SEQ ID NO recites the six CDR sequences in (a), (b), (c), and (d). It is not clear if the claimed each CDR SEQ ID NO: comprise “each with up to four conservative amino acid substitutions” or whether all the six CDR sequences combined comprise “each with up to four conservative amino acid substitutions”
The term “conservative amino acid” must be interpreted under BRI (broadest reasonable interperation) as to the “plain meaning” to one of ordinary skill in light of the specification. Applicant can be their own lexicographer, if they clearly indicate as such providing a “special definition” (e.g. define differently that the plain meaning). See e.g. MPEP 2111 et seq.
Under “plain meaning” “conservative amino acid” substitutions normally encompass "the replacement in a protein of one amino acid by another, chemically similar, amino acid... [which] is generally expected to lead to either no change or only a small change in the properties of the protein." Dictionary of Biochemistry and Molecular Biology 97 (John Wiley & Sons, 2d ed. 1989)). See MPEP 2144.08 section II A. 4(a)( c).
However, the specification provides a “different” definition that would constitute a “special definition”; but does not “clearly” do so.
This would lead to an ambiguity of scope. For example, the specification recited, “Other such conservative substitutions include, for example, substitutions of entire regions having similar hydrophobicity characteristics” (See, instant specification para [0081]). It is possible that the “similar hydrophobicity characteristics” would be met by the non-conservative amino acids. The limitation is not clear or is ambiguous to the ordinary skills. Additionally, the specification “definition” is relative regarding the determination of “similar hydrophobicity characteristics” by not indicate what characteristics are encompassed and by not providing a clear test for evaluation what degree of “hydrophobicity” is encompassed by the claim. See e.g. MPEP 2173.05 (b) “Relative Terminology”.
Claim 9: The limitation, wherein the VLP binding agent comprise amino acid sequence with at least about 90% sequence identity to the elected SEQ ID NOs: 27 and 31. It is not clear whether the amino acid substitutions are in the antigen-binding domains (e.g. CDR) or the supporting frame-work amino acid sequence of the VLP binding agent. Additionally, applicant has not defined quantitively the term “about”. In context to how much variation is allowed by “about”. e.g. claim 9 recites at least about 90% sequence identity to any of SEQ ID NOs:26-29. The term “about” is not clearly defined. In the art, it is generally “about” quantitively is generally defined to comprise +/- 10% (as is generally known to be defined in the art) in addition to the 90% sequence identity to any of SEQ ID NOs:26-29. Additionally, the specification fails to provide a means or examples for determining the metes and bounds of the term “about” in this context. See e.g. MPEP 2173.05 (b) “Relative Terminology”.
Claim Rejections - 35 USC § 112
9. 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 1-12, 15 and 16 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.
The instant claims 1-12, 15 and 16 are directed to a VLP binding agent that specifically binds to a VLP a parvovirus, an erythrovirus, or a parvovirus B 19. According to the instant specification, a VLP binding agent is an antibody or antibodies, a monoclonal antibody or monoclonal antibodies, antigen binding fragments, or antibody fragment (See, specification para [0005]-[0006]), and elsewhere in the specification. The term "antibody" means an immunoglobulin molecule, …….., as used herein, the term "antibody" encompasses intact polyclonal antibodies, intact monoclonal antibodies (See, specification para [0026]. In some embodiments, an antibody is recombinantly produced. In some embodiments, an antibody is produced by a hybridoma (See, specification para [0027]).
The instant claim 1: It is not clear whether “A VLP binding agent” encompass agent or structure other than derived from an antibody. The instant specification para [0004] provide an example “Accordingly, some embodiments of the present invention include virus-like particle (VLP) binding agents (e.g., antibodies and monoclonal antibodies) that have many uses including but not limited to detecting VLPs, parvovirus, erythrovirus, and parvovirus B 19, diagnosing parvovirus, erythrovirus, and parvovirus B19, and treating parvovirus, erythrovirus, and parvovirus B19. The example provided does not exclude comprising additional “VLP binding agent”.
The scope of claim 1 is generic (very broad) because of a generic “a VLP binding agent (e.g. antibody) without reciting a structure and by only reciting the function of binding to a VLP, a parvovirus, an erythrovirus, or a parvovirus B 19.
Thus, the instant claims 1-12, 15 and 16 are directed to a genus of “a VLP binding agent” (e.g. an antibody or antibodies, a monoclonal antibody or monoclonal antibodies, polyclonal antibody, recombinant antibody).
To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116. 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 (see i)(A) above), reduction to drawings (see i)(B) above), or 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 inventor was in possession of the claimed genus (see i)(C) above). See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. See Juno Therapeutics, Inc. v. Kite Pharma, Inc., 10 F.4th 1330, 1337, 2021 USPQ2d 893 (Fed. Cir. 2021). See MPEP 2163 “Written Description Guidelines”.
The Federal Circuit has clarified the application of the written description requirement to inventions in the field of biotechnology. See University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568,43 USPQ2d l398, 1406 (Fed. Cir. 1997). The Court stated that a written description of an invention requires a precise definition, one that defines the structural features of the chemical genus that distinguishes it from other chemical structures. A definition by function does not suffice to define the genus because it is only an indication of what the genus does, rather than what it is. Further, the Court held that to adequately describe a claimed genus, an applicant must describe a representative number of species of the claimed genus, and that one of skill in the art should be able to “visualize or recognize the identity of the members of the genus.”
Amgen Inc. vs Sanofi (2017-1480, Fed Cir, 2017) states that "an adequate written description must contain enough information about the actual makeup of the claim products - a precise definition such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other material," which may be present in "function "terminology "when the art has established a correlation between structure and function" (page 17,1st paragraph).
The instant claims 7-8 recites the VLP binding agent comprise an amino acid sequence with each amino acid sequence comprise up to four conservative amino acid substitutions in SEQ ID NOs: 5-7 and SEQ ID NOs: 17-19. The four conservative amino acid substitutions introduce variant species of “a VLP binding agent” and variations. (See, instant specification, para [0081]). Additionally, the specification recited, “Other such conservative substitutions include, for example, substitutions of entire regions having similar hydrophobicity characteristics” (See, instant specification para [0081]). It is possible that the “similar hydrophobicity characteristics” would be met by the non-conservative amino acids. The limitation is not clear or is ambiguous to the ordinary skills.
The instant claim 9 recites the VLP binding agent comprise an amino acid sequence with at least about 90% sequence identity to the elected species SEQ ID NO: 29 and 31. Therefore, the claim 9 allows up to 10% amino acid substitutions introducing variant species of “the VLP binding agent”. (See, instant specification, page 4, para [0006]) and elsewhere in the specification. Additionally, applicant has not defined quantitively the term “about”. In context to how much variation is allowed by “about”. e.g. claim 9 recites at least about 90% sequence identity to any of SEQ ID NOs:26-29. The term “about” clearly needs to define whether “about” meaning +/- 10% (as is generally known to be defined in the art) in addition to the 90% sequence identity to any of SEQ ID NOs:26-29. The term “about” introduces additional variant species of a VLP binding agent due to the permissible % variation that is inherent to “about”.
See also discussion of the metes and bounds of these terms under 35 USC 112b rejections supra.
Therefore, the claims 7, and claim 9 comprise the VLP binding agent that encompass many amino acid variations, and thus comprise variants of the VLP binding agent. It has been well known in the art that minor structural differences even among structurally related compounds or compositions can result in substantially different biological or pharmacological activities. It is known in the art that the substitution of amino acids within the protein sequence may cause the loss of function of the protein. Thus, the large number of sequences (“variant” antibody or fragments) encompassed by the instant claims 7 and 9 may or may not be effective in achieving the binding affinities of the claims. Specifically in relation to antibody CDRs, it should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity which is characteristic of the parent immunoglobulin (Janeway et al 2001, Immunobiology: The Immune System in Health and Disease. 5th edition. New York: Garland Science; 2001. The structure of a typical antibody molecule. Available from: ncbi.nlm.nih.gov/books/NBK27144/. See entire article). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al 1982, Single amino acid substitution altering antigen-binding specificity. Proc Natl Acad Sci U S A. 1982;79(6):1979-1983, see entire article, particularly the abstract and the middle of the left column of page 1982). Thus, based upon the prior art, skilled artisan would reasonably understand that it is the structure of the claimed VLP binding agent (CDRs within an antibody) which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves. The instant specification does not have written description support by example to demonstrate that that the applicant possess variants (amino acid variation) of the VLP binding agents that is required to be satisfied through sufficient description of a representative number of species by actual reduction to practice (with an affinity to bind to the claimed parvovirus VLP or a dissociation equilibrium constant (KD value) similar to that of a VLP binding agent without amino acid variations). In claim 9, at least about 90% sequence identity can be 80% because in the art “about” is defined as + 10% or - 10%. One of the ordinary skills in the art is not reasonably convinced how the claimed variant VLP binding agent will retain binding ability to the VLP. Many different variants of VLP binding agent are possible and can be envisioned by the ordinary skills. The ordinary skill is not convinced that variant VLP binding agents would have a function of binding to a claimed VLP at the same affinity (kD value) as that of the binding of a VLP binding agent comprising the amino acid sequences without variation or substitution and retain a therapeutic efficacy or binding affinity (As recited supra, see references, Rudikoff et al 1982, and Janeway et al 2001).
Therefore, the ordinary skill in the art is not reasonably convinced that the applicant and inventors at the time the application was filed, had possession of the full scope of claimed invention as claimed in claims 1-12, 15 and 16 since there is insufficient representative species and/or identifying characteristics to place applicant in possession of the generic scope of the claimed invention.
Claim Interpretation
10. 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.
Claim 1: The instant claim 1 is interpreted to be directed to a VLP binding agent that specifically binds to a VLP, a parvovirus, an erythrovirus, or a parvovirus B 19.
According to the instant specification (para [0004] – [0006]) “A VLP binding agent” is antibody and monoclonal antibody that specifically bind to a parvovirus wt or mutant VP2 protein comprised in the VLP or a parovirus B19. The VLP binding agent has many uses including but not limited to detecting VLPs, parvovirus, erythrovirus, and parvovirus B 19, diagnosing parvovirus, erythrovirus, and parvovirus B19, and treating parvovirus, erythrovirus, and parvovirus B19. An antibody is interpreted to be a polyclonal antibody, rabbit polyclobal antibody that binds to wt VLP or mutant mVLP (See, instant specification para [0017], [0190]). The term "antibody" encompasses intact polyclonal antibodies, intact monoclonal antibodies, different classes and subtypes of antibody, antibody fragments (e.g. Fab, Fab', F(ab')2, and Fv fragments), single chain Fv (scFv) mutants, multispecific antibodies such as bispecific antibodies, chimeric antibodies, humanized antibodies, human antibodies (See, instant specification, para [0026], [0190]). The instant claim 1: It is not clear whether “A VLP binding agent” encompass agent or structure other than derived from an antibody. The instant specification para [0004] provide an example “Accordingly, some embodiments of the present invention include virus-like particle (VLP) binding agents (e.g., antibodies and monoclonal antibodies) that have many uses including but not limited to detecting VLPs, parvovirus, erythrovirus, and parvovirus B 19, diagnosing parvovirus, erythrovirus, and parvovirus B19, and treating parvovirus, erythrovirus, and parvovirus B19. The example provided does not exclude comprising additional “VLP binding agent”.
Claim 7: The instant claim 7 recited a limitation e.g. (a) SEQ ID NOS:2-4 and 14-16, each with up to four conservative amino acid substitutions which can interpreted under BRI as
Each claimed CDR and thus all six CDR sequence (a) SEQ ID NOS:2-4 and 14-16, each with up to four conservative amino acid substitutions. Additionally, the specification recited, “Other such conservative substitutions include, for example, substitutions of entire regions having similar hydrophobicity characteristics” (See, instant specification para [0081]). It is possible that the “similar hydrophobicity characteristics” would be met by the non-conservative amino acids.
Claim 9: The claim 9 is interpreted to be directed to a VLP binding agent that comprise about 10% mismatched amino sequence (at least about 90% sequence identity) to the SEQ ID NO: 27 and 31. It is interpreted that the mismatch amino acid variation can be in the CDR or non-CDR comprising heavy and light chain backbone framework amino acids.
Claim Rejections - 35 USC § 102
11. 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 1-6 are rejected under 35 U.S.C. 102(a)(1)/(a)(2) as being anticipated by Ghim et al 2017 (US20170015712A1, 01/19/2017; patent granted Publication of US10214565B2 on 02/26/2019).
Claims 1-2: Ghim et al 2017 (US20170015712A1) anticipated instant claims 1-2 by teaching a VLP binding agent (an antibody) that specifically binds to a VLP, wtVLP and mutant mVLP of a parvovirus, an erythrovirus, or a parvovirus B 19, the VLP comprise VP2 protein of a parvovirus B19. A VLP binding agent is interpreted as an antibody or polyclonal antibody. Ghim et al 2017 is directed to a parvovirus B19 VLP, wt VLP, mutant VLP (see, para [0005]-[0006], claim 5). Polyclonal antibody (parvovirus B19 wt VLP or mVLP anti-serum raised in rabbit) showed binding or reactivity of the antibodies to the VLPs as measured by ELISA antigen (VLP) binding assay (See, para [0101]-[0102]). Mouse polyclonal antibodies induced against parvovirus B19 wt VLP or mVLP showed hemagglutination-inhibition (HI) activity (binding) to the wt VLP or mVLP (See, para [0103]). A mutant VLP or “mVLP” is a virus-like particle formed from inventive polypeptides, where the inventive polypeptide has at least one amino acid modification relative to wild type VP2 (See, para [0053]). An example of the wild type and mutant VLPs are shown in FIG. 1C (wild type: QQT401YDQ) and FIG. 1D (Constrict A: QQF401TDQ) (See, para [0087]- [0088]).
Thus, Ghim et al 2017 anticipated instant claims 1-2 with disclosure as recited supra.
Claims 3-6: Ghim et al 2017 anticipated instant claims 3-6 by disclosures of the prior art as follow:
Claims 3-6: The VLP binding agent, wherein the wild type VP2 has the amino acid sequence of SEQ ID NO: 1, and the at least one amino acid modification comprises a substitution at Y401 (instant claim 3 limitation); Y401F (instant claim 4 limitation), SEQ ID NO: 85 taught by Ghim et al 2017 that has 99.9% identity with instant SEQ ID NO: 1 with Y401F substitution; wherein VP2 polypeptide is construct A, construct B, construct D, or construct F (instant claim 5 limitation), wherein the VLP binding agent is an antibody (instant claim 6 limitation) is taught by polyclonal antibody (parvovirus B19 wt VLP or mVLP anti-serum raised in rabbit) showed binding or reactivity of the antibodies to the VLPs as measured by ELISA antigen (VLP) binding assay (See, para [0101]-[0102]). Mouse polyclonal antibodies induced against parvovirus B19 wt VLP or mVLP showed hemagglutination-inhibition (HI) activity (binding) to the wt VLP or mVLP (See, para [0103]), (See, para [0005], claim 8, para [0101]- [0103]).
Ghim et al 2017 SEQ ID NO 85
LENGTH: 554
Query Match 99.9%; Score 2993; Length 554;
Best Local Similarity 99.8%;
Matches 553; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MTSVNSAEASTGAGGGGSNPVKSMWSEGATFSANSVTCTFSRQFLIPYDPEHHYKVFSPA 60
Qy 61 ASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ASSCHNASGKEAKVCTISPIMGYSTPWRYLDFNALNLFFSPLEFQHLIENYGSIAPDALT 120
Qy 121 VTISEIAVKDVTDKTGGGVQVTDSTTGRLCMLVDHEYKYPYVLGQGQDTLAPELPIWVYF 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 VTISEIAVKDVTDKTGGGVQVTDSTTGRLCMLVDHEYKYPYVLGQGQDTLAPELPIWVYF 180
Qy 181 PPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPE 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 PPQYAYLTVGDVNTQGISGDSKKLASEESAFYVLEHSSFQLLGTGGTATMSYKFPPVPPE 240
Qy 241 NLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTK 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 NLEGCSQHFYEMYNPLYGSRLGVPDTLGGDPKFRSLTHEDHAIQPQNFMPGPLVNSVSTK 300
Qy 301 EGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVTGINAISHGQTTYG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 EGDSSNTGAGKALTGLSTGTSQNTRISLRPGPVSQPYHHWDTDKYVTGINAISHGQTTYG 360
Qy 361 NAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTYFPNKGTQQYTDQIERPLMVGSVWNRRAL 420
|||||||||||||||||||||||||||||||:||||||||||||||||||||||||||||
Db 361 NAEDKEYQQGVGRFPNEKEQLKQLQGLNMHTFFPNKGTQQYTDQIERPLMVGSVWNRRAL 420
Qy 421 HYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQ 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 HYESQLWSKIPNLDDSFKTQFAALGGWGLHQPPPQIFLKILPQSGPIGGIKSMGITTLVQ 480
Qy 481 YAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEK 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 YAVGIMTVTMTFKLGPRKATGRWNPQPGVYPPHAAGHLPYVLYDPTATDAKQHHRHGYEK 540
Qy 541 PEELWTAKSRVHPL 554
||||||||||||||
Db 541 PEELWTAKSRVHPL 554
Thus, Ghim et al 2017 anticipated instant claims 3-6 with disclosure as recited supra.
12. Claims 1-2 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Chandramouli et al 2013 (Vaccine 31, (2013), p. 3872– 3878).
Chandramouli et al 2013 is directed to a parovirus B19 wtVP2 VLPs, and anticipated instant claim 1 by disclosing a monoclonal antibody mAb 5E408 (a VLP binding agent reads on or is interpreted as a monoclonal antibody) that recognized or bound to both VP1 and VP2 of a parvovirus B19 VLPs as the binding of the monoclonal antibody mAb 5E408 is demonstrated in a wester-blot of the VLPs. The VLP of parvovirus B19 were produced by co-expressing VP2 (read on a wild type VP2 and thus wtVLP comprising wtVP2) and either a wild-type VP1 or phospholipase-negative VP1 (See, abstract, p. 3873 Fig 1 and associated legends, page 3875 Fig 3-C).
Claim Rejections - 35 USC § 103
13. 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 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.
14. Claims 1-6, 12 and 15-16 are rejected under 35 U.S.C. 103 as being unpatentable over Ghim et al 2017 (US20170015712A1, 01/19/2017; patent granted Publication of US10214565B2 on 02/26/2019) as applied to claims 1-6 above, and further in view of Chandramouli et al 2013 (Vaccine 31, (2013), p. 3872– 3878), Huille et al 2012 (CA2805685A1, 02/09/2012, Google machine translated English PDF printout), Arakelov et al 1993 (J Infect Dis., 1993;168(3):580-5), and Bredl et al 2013 (AU2012222888A1, 09/26/2013).
Claims 1-6: The prior art teachings of Ghim et al 2017 on polyclonal antibodies binding to the claimed parvovirus B19 VLPs (VP2 wtVLPs, VP2 mVLPs) as applied to claims 1-6, and the prior art teachings of Chandramouli et al 2013 on monoclonal antibody binding to the claimed parvovirus B19 VLPs (VP2 wtVLPs) as applied to claims 1-2, as recited supra, are incorporated here in its entirety to render obvious claims 1-6.
Both Ghim et al 2017 and Chandramouli et al 2013 does not teach a composition or a pharmaceutical composition comprising the VLP binding agent (polyclonal or monoclonal antibody binding to the VLP) of claim 1.
Claim 15-16: Huille et al 2012 is directed to a composition or a liquid pharmaceutical composition comprising of human immunoglobulins G characterized in that the concentration of human immunoglobulins G is at least 230 g / L, the pharmaceutical composition of the invention is thus useful as a medicament as drug, in particular to treat parvovirus B19 virus infection by administration via the subcutaneous route in human (See, CA2805685A1, Google machine translated English PDF printout page 7 para 8-9, page 2 claim 27). Arakelov et al 1993 renders obvious added limitations of instant claims 15-16 instant claims 15-16 by interpreting the VLP binding agent as a polyclonal antibody or antibody.
Huille et al 2012 does not teach monoclonal antibody-based composition or a pharmaceutical composition.
Arakelov et al 1993 teaches generation of neutralizing anti-B19 parvovirus human monoclonal antibodies, the MAbs were specific for conformational epitopes on the VP2 capsid protein of B19 parvovirus and both were capable of neutralizing 50% of the viral infectivity in a human erythroid colony-forming unit assay at < or = 1 micrograms of MAb/mL. These human MAbs are potentially useful in the treatment of acute B19 parvovirus infection (See, abstract). Arakelov et al 1993 renders obvious added limitations of instant claims 15-16 by interpreting the VLP binding agent as a monoclonal antibody.
Additionally, Chandramouli et al 2013 recited the monoclonal antibody mAb 5E408 that binds to parvovirus B19 VP1 and VP2 as recited supra and can be used to form a composition or pharmaceutical composition of the instant claims 15-16. Chandramouli et al 2013 renders obvious added limitations of instant claims 15-16 by interpreting the VLP binding agent as a monoclonal antibody.
Claim 12: Bredl et al 2013 is in the parvovirus B19 viral antigen diagnostic art and teaches instant claim 12 added limitation, the VLP binding agent of claim1 wherein the VLP binding agent is detectably labeled by disclosing an improved method for the detection of parvovirus B19 in a sample. The human Mab 860-55 that is parvovirus B19 VP2-specific is disclosed, and the Mab was purchased from Millipore. The labelling of the antibodies with AlexaFluor647* was made with the APEXTM Alexa Fluor 647 15 Labelling Kit (Invitrogen) according to the manufacturer's instructions (See, page 12 lines 10-15, claims 1, 11). Various immunoassay formats are available to the skilled person and these often involve the use of a labelled antibody e.g. with an enzymatic, fluorescent, chemiluminescent, radioactive, or dye label. Assays which amplify signals from immune complexes are also known e.g. those which utilize biotin and avidin, and enzyme-labelled and mediated immunoassays, such as ELISA. The antibody may be a polyclonal or monoclonal preparation. An antibody may include a non-protein substance e.g. via covalent conjugation. For example, an antibody may include a detectable label (See, page 4 lines 25-40). Although the claims of the prior art are directed to a method for detecting parvovirus B 19 in a sample, the improvement consisting of detecting a parvovirus B 19 non-structural protein, the prior art recited a commercially available human Mab 860-55 that specifically binds to parvovirus B19 VP2 and thus the antibody can be labelled and the assay can be reasonably modified to detect or quantify a parvovirus B19 wtVP2 protein in a sample (e.g. parvovirus B19 in a sample) or wtVLP (e.g. wtVLP immunogen derived from parvovirus B19).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art teaching of Ghim et al 2017 on polyclonal antibody binding to a parvovirus B19 wild type wt VP2 or wtVLPs or mutant VP2 mVLPs by incorporating additional teachings of Chandramouli et al 2013 on a monoclonal antibody mAb 5E408 binding to a parvovirus B19 wild type wtVP2 VLPs to arrive at the instant claims 1-6. Further, the invention rendered obvious by the combined teachings of Ghim et al 2017 and Chandramouli et al 2013 would have been obvious to modify by incorporating teachings of Huille et al 2012, and Arakelov et al 1993 to arrive at the invention of claims 15-16. Bredl et al 2013 teachings on antibody label results in arrival at instant claim 12. The motivation would have been to develop the claimed parvovirus B-19 VLP binding agent of claims 1-6 for developing approaches to develop immunodiagnostic assays to quantify parvovirus B19 VLPs for vaccine doses optimization, diagnostic assays targeting parvovirus B19 VP2 protein antigen (instant claims 1-6) or passive antibody immunoglobulin (anti-VP2 polyclonal or monoclonal antibody against parvovirus B19 as claimed in instant claims 15-16) therapy using the composition or pharmaceutical composition for treatment and therapeutics against parvovirus B19, Bredl et al 2013 teachings labeling the VLP binding agent (read as Mab or antibody or polyclonal antibody) to develop qualitative detection or quantification of wtVP2 or wtVLP of parvovirus B19. The polyclonal antibodies can also be labelled as per method disclosed by Bredl et al 2013 to develop broadly reactive quantification and detection diagnostics assay (instant claim 12) and for commercial success. There would have been a reasonable expectation of success given the applied prior arts teachings and required research skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, 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 1-6, 12 and 15-16. 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).
15. Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over combined teachings of Ghim et al 2017 (US20170015712A1, 01/19/2017; patent granted Publication of US10214565B2 on 02/26/2019), Chandramouli et al 2013 (Vaccine 31, (2013), p. 3872– 3878), Huille et al 2012 (CA2805685A1, 02/09/2012, Google machine translated English PDF printout), Arakelov et al 1993 (J Infect Dis., 1993;168(3):580-5), and Bredl et al 2013 (AU2012222888A1, 09/26/2013) as applied to claims 1-6 above, and further in view of Gip et al 2025 (US12215163B2, 02/04/2025 with earlier priority of 11/14/2018 to US 62/767,405), and Blein et al 2016 (US9493563B2,11/15/2016).
Claim 9. The VLP binding agent of claim 1, wherein the VLP binding agent comprises an amino acid sequence with (a) at least about 90% sequence identity to any of SEQ ID NOs:26-29; and/or (b) at least about 90% sequence identity to any of SEQ ID NOs:30-33.
The prior art teachings of Ghim et al 2017, Chandramouli et al 2013, Huille et al 2012, Arakelov et al 1993, and Bredl et al 2013 as applied to render obvious claim 1 as recited supra, however, does not teach the added limitation of the instant claim 9.
Instant claim 9 SEQ ID NO: 28 (Qy) is taught by prior art Gip et al 2025 (US12215163B2, 02/04/2025 with earlier priority of 11/14/2018 to US 62/767,405) by disclosing SEQ ID NO: 434 (Db).
Query Match 92.2%; Score 588; Length 119;
Best Local Similarity 93.3%;
Matches 111; Conservative 3; Mismatches 5; Indels 0; Gaps 0;
Qy 1 QVQLQQSGAELARPGASVKMSCKASGYTFTSYTMHWVKQRPGQGLEWIGYINPSSGYTNY 60
|:||||||||||||||||:||||||||||||||:||||||||||||||||||||||||||
Db 1 QIQLQQSGAELARPGASVRMSCKASGYTFTSYTIHWVKQRPGQGLEWIGYINPSSGYTNY 60
Qy 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCARPDGYYAWFAYWGQGTLVTVSA 119
|||||||||||||||||||||||||||||||||||||| ||||||||||||||||
Db 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCARSGLRQAWFAYWGQGTLVTVSA 119
Instant claim 9 SEQ ID NO: 32 (Qy) is taught by prior art Blein et al 2016 (US9493563B2,11/15/2016) teaches SEQ ID NO: 115 (Db).
Query Match 98.0%; Score 540; Length 106;
Best Local Similarity 97.2%;
Matches 103; Conservative 2; Mismatches 1; Indels 0; Gaps 0;
Qy 1 DIQMTQSSSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
||::||| ||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIELTQSPSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
Qy 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPTFGGGTKLEIK 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPTFGGGTKLEIK 106
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the prior art to modify the combined prior teaching of Ghim et al 2017, Chandramouli et al 2013, Huille et al 2012, and Arakelov et al 1993 with the additional teachings of Gip et al 2025, and Blein et al 2016 on the amino acid sequences of an antibody that has 90% or higher amino acid identity with the claimed amino acid sequences SEQ ID NO: 28 and SEQ ID NO:32 of the VLP binding agent and to arrive at the invention of claim 9. The motivation would have been to develop broadly reactive VLP binding agent, and to produce large amount of the VLP binding agent using transient transfection of cell culture with vectored DNA sequences or generate antibody secreting stable cell lines for high quantity and quality production for therapeutics against parvovirus B19 and commercial success. There would have been a reasonable expectation of success given the applied prior arts teachings and required research skills available with one of the ordinary skills in the art. Thus, the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention. This is analogous to some teaching, suggestion, 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 claim 9. 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).
16. Claims 7-8:
The instant Claim 7: The claimed SEQ ID NOs are free of prior art because one SEQ ID NO: from each (a), (b), (c), (d) is free of prior art as recited below:
Claim 7: The VLP binding agent of claim 1, wherein the VLP binding agent comprises an amino acid sequence with
(a) claimed is SEQ ID NOS:2-4 and 14-16, each with up to four conservative amino acid substitutions, however, as recited below SEQ ID NO: 4 is free of prior art because the closest prior art Wang et al 2022 (US11214615B2, 01/04/2022, priority to US16/633,262 filed on 07/26/2018) SEQ ID NO: 75 teach sequence identity of 69.2% with the claimed SEQ ID NO: 4 amino acid identity as shown below:
Query Match 69.2%; Score 63; Length 16;
Best Local Similarity 83.3%;
Matches 10; Conservative 1; Mismatches 1; Indels 0; Gaps 0;
Qy 2 GNYRYDGYYGMD 13
|:||||||| ||
Db 4 GHYRYDGYYAMD 15
(b) claimed is SEQ ID NOS:5-7 and 17-19, each with up to four conservative amino acid substitutions; however, SEQ ID NO: 7 is free of prior art because the closest prior art Poma et al 2021 (US11142584B2, 10/12/2021; priority of 09/17/2015 to US20150259428A1) teaches SEQ ID NO: 13 that has 74.7% Query match, and 83.3% Best local similarity sequence identity to the instant SEQ ID NO:7 as recited below:
Qy 2 YYGSNYVWHFDV 13
||||:||| |||
Db 3 YYGSSYVWFFDV 14
(c) claimed is SEQ ID NOS:8-10 and 20-22, each with up to four conservative amino acid substitutions, however, SEQ ID NO: 10 is free of prior art because the closest prior art Chen et al 2023 (US11773510B2, 10/03/2023, with earlier priority of 01/08/2019-08-01 to US20190233813A1) teaches SEQ ID NO: 178 that has 89.2% Query match, and 100% Best local similarity sequence identity to the instant SEQ ID NO:10 as recited below:
Query Match 89.2%; Score 58; Length 16;
Best Local Similarity 100.0%;
Matches 9; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 2 DGYYAWFAY 10
|||||||||
Db 8 DGYYAWFAY 16
or
(d) claimed is SEQ ID NOS:11-13 and 23-25, each with up to four conservative amino acid substitutions however, SEQ ID NO: 12 is free of prior art because the closest prior art Spellberg et al 2022 (US11306137B2, 04/19/2022 with earlier priority of 08/02/2018 to US20180215811A1) teaches SEQ ID NO: 3 that has 90.8% Query match, and 88.2% Best local similarity sequence identity to the instant SEQ ID NO:12 as recited below:
Query Match 90.8%; Score 89; Length 118;
Best Local Similarity 88.2%;
Matches 15; Conservative 1; Mismatches 1; Indels 0; Gaps 0;
Qy 1 RINPYNGDSFYNQNFRG 17
||||||||||||| |:|
Db 50 RINPYNGDSFYNQKFKG 66
Claim 8: The VLP binding agent of claim 1, wherein the VLP binding agent comprises an amino acid sequence with (a) SEQ ID NOS:2-4 and 14-16, (b) SEQ ID NOS:5-7 and 17-19, (c) SEQ ID NOS:8-10 and 20-22, or (d) SEQ ID NOS:11-13 and 23-25.
The instant Claim 8 sequence SEQ ID are free of prior art. The closest prior art that does not teach required 100% amino acid sequence identity match for the SEQ ID NOs: 4, 7, 10 and 12 are same as recited above for claim 7.
17. Claims 10-11:
Claim 10: The VLP binding agent of claim 1, wherein the VLP binding agent comprises an amino acid sequence with (a) at least one of SEQ ID NOs:26- 29; and/or (b) at least one of SEQ ID NOs:30-33.
The instant claim 10 claimed SEQ ID NOS: are free of prior art because claim limitation is interpreted to requires 100% amino acid sequence identity.
Claim 11: The VLP binding agent of claim 1, wherein the VLP binding agent comprises an amino acid sequence with (a) SEQ ID NOs:26 and 30, (b) SEQ ID NOs:27 and 31, (c) SEQ ID NOs:28 and 32, or (d) SEQ ID NOs:29 and 33.
The instant claim 11 claimed SEQ ID NO are free of prior art because claim limitation is interpreted to requires 100% amino acid sequence identity.
The closest prior arts are recited below:
Instant SEQ ID NO: 26: Prior art by Getts et al 2013 (US8524234B2, 09/03/2013) SEQ ID NO: 9 as recited below.
Query Match 87.5%; Score 580; Length 253;
Best Local Similarity 91.9%;
Matches 113; Conservative 3; Mismatches 3; Indels 4; Gaps 2;
Qy 1 QVQLQQSGAELARPGASVKMSCKASGYTFTSYTMYWVKQRPGQGLEWIGYVNPSSGYTNY 60
||||||||||||||||||||||||||||||||||:|||||||||||||||:|||||||||
Db 1 QVQLQQSGAELARPGASVKMSCKASGYTFTSYTMHWVKQRPGQGLEWIGYINPSSGYTNY 60
Qy 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCARHGNYRYDGYYGMDCWGQGTSVT 120
|||||||||||||||||||||||||||||||||||||| :| | || || ||||||||
Db 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCAR---WR-DAYYAMDYWGQGTSVT 116
Qy 121 VSS 123
|||
Db 117 VSS 119
Instant SEQ ID NO: 27: Prior art by Bernett et al 2021 (US11084863B2, 08/10/2021, with an earlier priority of 01/17/2019 to US20190016778A1) disclosed SEQ ID NO. 468 that has that has 83.1% query match identity and 84.9% best local similarity to the instant SEQ ID NO: 27 as recited below.
Query Match 83.1%; Score 554.5; Length 125;
Best Local Similarity 84.9%;
Matches 107; Conservative 7; Mismatches 7; Indels 5; Gaps 2;
Qy 1 QVQLQQPGAELVRPGASVKLSCKASGYTFTNYWMHWVKQRPEQGLEWIGRIDPYDSETHY 60
||||||||||||||||||||||||||||||:|||:||||||||||:||||||||||||||
Db 1 QVQLQQPGAELVRPGASVKLSCKASGYTFTSYWMNWVKQRPEQGLQWIGRIDPYDSETHY 60
Qy 61 NQKFKDKAILTVDTSSNTAYMQLSSLTSEDSAVYYCTSYYY----GSNYVWHFDVWGAGT 116
:|||||||||||| ||:||||:|||||||||||||| | |: | | ||||||||
Db 61 SQKFKDKAILTVDKSSSTAYMRLSSLTSEDSAVYYCARGGYDFDVGTLY-WFFDVWGAGT 119
Qy 117 TVTVSS 122
||||||
Db 120 TVTVSS 125
Instant SEQ ID NO: 28: Prior Art Gip et al 2025 (US12215163B2, 02/04/2025 with earlier priority of 11/14/2018 to US 62/767,405) SEQ ID NO: 434.
Query Match 92.2%; Score 588; Length 119;
Best Local Similarity 93.3%;
Matches 111; Conservative 3; Mismatches 5; Indels 0; Gaps 0;
Qy 1 QVQLQQSGAELARPGASVKMSCKASGYTFTSYTMHWVKQRPGQGLEWIGYINPSSGYTNY 60
|:||||||||||||||||:||||||||||||||:||||||||||||||||||||||||||
Db 1 QIQLQQSGAELARPGASVRMSCKASGYTFTSYTIHWVKQRPGQGLEWIGYINPSSGYTNY 60
Qy 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCARPDGYYAWFAYWGQGTLVTVSA 119
|||||||||||||||||||||||||||||||||||||| ||||||||||||||||
Db 61 NQKFKDKATLTADKSSSTAYMQLSSLTSEDSAVYYCARSGLRQAWFAYWGQGTLVTVSA 119
Instant SEQ ID NO: 29: Prior Art Touze et al 2025 (US12365721B2, 07/22/2025 with earlier priority of 06/03/2019 to FR 19/05881) SEQ ID NO: 18.
Query Match 86.3%; Score 551.5; Length 137;
Best Local Similarity 86.6%;
Matches 103; Conservative 5; Mismatches 10; Indels 1; Gaps 1;
Qy 1 EVQLQQSGPELVKPGASVKISCKASGYSFTDYFMNWVKQSHGKSLEWIGRINPYNGDSFY 60
|||||||||||||||||||||||||||||| ||||||||||||||||||||||||||:||
Db 20 EVQLQQSGPELVKPGASVKISCKASGYSFTGYFMNWVKQSHGKSLEWIGRINPYNGDTFY 79
Qy 61 NQNFRGSVTLTVDKSSGTAHMELLSLTSEDSTVYYCGAYRYDGYAMDYWGQGTSVTVSS 119
|| |:| |||||||| |||||||||||||| |||||:| | | |||||||::||||
Db 80 NQKFKGKATLTVDKSSSTAHMELLSLTSEDSAVYYCGSYYYGDY-FDYWGQGTTLTVSS 137
Instant SEQ ID NO: 30: Prior Art: Igawa et al 2022 (US11505605B2, 11/22/2022 with earlier priority US20170260271A1, 09/14/2017) teaches SEQ ID NO: 44.
Query Match 99.8%; Score 557; Length 107;
Best Local Similarity 99.1%;
Matches 106; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQMTQSSSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQMTQSSSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
Qy 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPYTFGGGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||:|
Db 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPYTFGGGTKLEVK 107
Instant SEQ ID NO: 31: Prior Art by Bernett et al 2020 (US10787518B2, 09/29/2020, with an earlier priority of 05/03/2018 to US20180118836A1) disclosed SEQ ID NO: 39181 that has 98.6% query match identity and 97.3% best local similarity to the instant SEQ ID NO: 31 as recited below.
Query Match 98.6%; Score 579; Length 112;
Best Local Similarity 97.3%;
Matches 109; Conservative 2; Mismatches 1; Indels 0; Gaps 0;
Qy 1 DVVMTQTPLTLSVTIGQPASISCKSSQSLLDSDGRTYLNWLLQRPGQSPKRLIYLVSKLD 60
||||||||||||||||||||||||||||||||||:|||||||||||||||||||||||||
Db 1 DVVMTQTPLTLSVTIGQPASISCKSSQSLLDSDGKTYLNWLLQRPGQSPKRLIYLVSKLD 60
Qy 61 SGVPDRFTGSGSGTDFTLKISRVEAEDLGIYYCWQGTHLPYTFGGGTKLEIK 112
|||||||||||||||||||||||||||||:|||||||| |||||||||||||
Db 61 SGVPDRFTGSGSGTDFTLKISRVEAEDLGVYYCWQGTHFPYTFGGGTKLEIK 112
Instant SEQ ID NO: 32: Prior Art Blein et al 2016 (US9493563B2,11/15/2016) teaches SEQ ID NO: 115.
Query Match 98.0%; Score 540; Length 106;
Best Local Similarity 97.2%;
Matches 103; Conservative 2; Mismatches 1; Indels 0; Gaps 0;
Qy 1 DIQMTQSSSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
||::||| ||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIELTQSPSSFSVSLGDRVTITCKASEDIYNRLAWYQQKPGNAPRLLISGATSLETGVPS 60
Qy 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPTFGGGTKLEIK 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGKDYTLSITSLQTEDVATYYCQQYWSTPTFGGGTKLEIK 106
Instant SEQ ID NO: 33: Yokoseki et al 2014 (US8858949B2, 10/14/2014) teaches SEQ ID NO: 2624.
Query Match 99.1%; Score 578; Length 112;
Best Local Similarity 99.1%;
Matches 111; Conservative 1; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSDGNTYLHWYLQKPGQSPKLLIYKVSNRF 60
||||||||||||||||||||||||||||||||:|||||||||||||||||||||||||||
Db 1 DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPKLLIYKVSNRF 60
Qy 61 SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIK 112
||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIK 112
18. Relevant Prior Art:
Ghim et al 2022. (EP3116540B1, 08/17/2022, with an earlier priority of 01/18/2017 to EP3116540A1). Compositions and methods for treating, including preventing, parvovirus infections and related diseases.
Sato et al 1991. Identification of the region including the epitope for a monoclonal antibody which can neutralize human parvovirus B19. J Virol. 1991 Apr;65(4):1667-72.
Gentilomi et al 1997. Dot immunoperoxidase assay for detection of parvovirus B19 antigens in serum samples. J Clin Microbiol. 1997 Jun;35(6):1575-8.
Brown et al 1992. Localization of an immunodominant domain on baculovirus-produced parvovirus B19 capsids: correlation to a major surface region on the native virus particle. J Virol. 1992 Dec;66(12):6989-96.
Conclusion
19. No claim is allowed.
20. 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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/SAMADHAN JAISING JADHAO/ Examiner, Art Unit 1672
/BENNETT M CELSA/Primary Examiner, Art Unit 1600