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. DETAILED ACTION Status of Claims 2. Applicant 's preliminary amendment of the instant application, which was originally submitted on FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 12/18/2023 and later amended on FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" the same day , is acknowledged by the Examiner . Claims 1 – 8 are pending and under review . Priority 3. The instant application is a FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" National Stage Entry of International Patent Application No. PCT/ FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" JP2022/020944 filed on FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 05/20/2022 , and also claims priority to Japanese Patent Application No. FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 2021-084985 filed on FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 05/20/2021 . It is noted, however, that Applicant has not filed a certified copy of these applications that complies with 37 CFR 1.55. Applicant has not provided a certified copy or English translation of Japanese Patent Application No. FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 2021-084985 . An English language translation of a ny non-English language foreign application is required ( i ) when the application is involved in an interference or derivation proceeding; (ii) when necessary to overcome the date of a reference relied upon by the examiner ; or (iii) when specifically required by the examiner. Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C. 119(a)-(d) prior to declaration of an interference, a certified English translation of the foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and 41.202(e). Failure to provide a certified translation may result in no benefit being accorded for the non-English application. Thus, the current U.S. effective filing date of claims 1 – 8 is the international filing date, i.e., 05/20/2022 . Information Disclosure Statement 4. The information disclosure statement (IDS) submitted on FILLIN "Identify the term that is a trade name or mark used in commerce." \d "[ 1 ]" 09/24/2024 has been considered by the Examiner . Notably, the listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Thus, unless the references have been cited by the Examiner on form PTO-892, they have not been considered. Specification 5. The use of the terms Tween™ on page 11; Perfect-Block™ on pages 11 and 13; Nunc- Immuno ™ Module F8 Maxisorp Surface™ on page s 11 and 13; and possibly others in the specification, which are trade names or a marks used in commerce, have been noted in this application. The terms should be accompanied by the generic terminology; furthermore, the terms should be capitalized wherever they appear or, where appropriate, include a proper symbol indicating use in commerce such as ™, ℠ , or ® following the terms. Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Applicant is required to properly annotate all trade names and/or marks that are present in the specification. 6 . The lengthy specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant ’s cooperation is requested in correcting any errors of which Applicant may become aware in the specification. 7 . No drawings were present at the time of this Office Action. Claim Objections 8 . Claim s 1 and 2 are objected to because of the following informalities: There is a typographical error in claim FILLIN "Enter claim indentification information" \* MERGEFORMAT 1 , line FILLIN "Enter claim indentification information" \* MERGEFORMAT 1 . There is a missing comma after “[A]n anti-norovirus antibody”; Claim 1 , line 1 and claim 2, lines 2 recite the phrase “ undergoes antigen-antibody reaction ” . This is grammatically incorrect. It is recommended that the phrase read “ undergoes an antigen-antibody reaction ”. Recommended amendments are underlined. Appropriate correction is required. Claim Rejections - 35 USC § 112 35 USC § 112(b) 9 . 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. 1 0 . Claim s 1 – 8 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. 1 1 . Claim s 1 and 2 are vague and unclear, which renders the claim indefinite. This rejection affects all claims that are dependent on claims 1 and 2, i.e., claims 3 and 6, respectively. Claim 1 recite s “ composed of the amino acid sequences of SEQ ID NO: 1 and SEQ ID NO: 2 , respectively ” , whereas claim 2 recites “composed of the amino acid sequences of SEQ ID NO: 3 and SEQ ID NO: 4 , respectively ”. The usage of the adverb “respectively” implies that the two different peptides are reacting with two different things in a parallel list. However, no such parallel list is recited. It is not clear if the two different peptides are both reacting with the anti-norovirus antibody mentioned in the preamble of the claims or only one is reacting with the disclosed antibody and the other is reacting with something else. The presence of multiple interpretations of the same claim language renders the claim indefinite. It is recommended that the phrase “respectively” be removed. In the interest of compact prosecution, it will be inferred that “respectively” means that the disclosed antibody must bind to both of the defined epitopes. Additionally, both claims recite “ composed of the amino acid sequences of SEQ ID NO: X”, wherein X is the different sequence number. It is unclear if this transitional phrase is open-ended or close-ended. In other words, it is unclear if any additional, unrecited elements not specified in the claim are included or excluded. The presence of multiple very different interpretations of the same claim language renders the claim indefinite. It is recommended that the “composed of” limitation be amended to a proper transitional phrase, i.e., “comprising”, “consisting of”, or “consisting essentially of”. In the interest of compact prosecution, the transitional phrase “composed of” has been interpreted in the same manner as “consisting of”. See AFG Industries, Inc. v. Cardinal IG Company, 239 F.3d 1239, 1245, 57 USPQ2d 1776, 1780-81 (Fed. Cir. 2001) ; In re Bertsch, 132 F.2d 1014, 1019-20, 56 USPQ 379, 384 (CCPA 1942) ; and MPEP § 2111.03. 12. Claims 4 and 7 recite “ utilizing the antigen-antibody reaction” in line 1 of the claims. The claims recite a use without any active steps delineating how the use is actually practiced. Attempts to claim a process without setting forth any steps involved in the process generally raises an issue of indefiniteness under 35 U.S.C. 112(b) or pre-AIA 35 U.S.C. 112, second paragraph. For example, a claim which read: "[a] process for using monoclonal antibodies of claim 4 to isolate and purify human fibroblast interferon" was held to be indefinite because it merely recites a use without any active, positive steps delimiting how this use is actually practiced. See Ex parte Erlich , 3 USPQ2d 1011 (Bd. Pat. App. & Inter. 1986) and MPEP § 2173.05(q) . Therefore, it is unclear if the claims are intended to be drawn to a product, i.e., the immunoassay as a kit , or drawn to a method of using the immunoassay. The presence of multiple very different interpretations of the same claim language renders the claim indefinite. 13. Claims 4 and 7 recite “an immunoassay” in the preamble of the claims. An assay can be a product or a method. The instant specification teaches that the instant specification is not limited to a specific method and any well-known immunoassay can be employed (page 9, paragraph 0033). However, i t is still unclear if the claims are intended to be drawn to a product, i.e., an immunoassay as part of a kit, or a method, i.e., using the immunoassay to detect something. The presence of multiple very different interpretations of the same claim language renders the claim indefinite. 1 4 . It is noted that any interpretation of the claims set forth above does not relieve Applicant of the responsibility of responding to this Office Action. In the interest of compact prosecution, all of the suggested amendments and/or set forth interpretations will be employed for other rejections. If the actual interpretation of the claims is different than that posited by the Examiner, additional rejection(s) and art may be applied in a subsequent Office Action. 35 USC § 112(a) 1 5 . 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. 16. Claim s 1 – 8 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 purpose of [the written description requirement] is to ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification"); LizardTech Inc. v. Earth Resource Mapping Inc., 424 F.3d 1336, 1345, 76 USPQ2d 1724, 1732 (Fed. Cir. 2005) . This requirement is separate and distinct from the enablement requirement. To satisfy the written description requirement for a claimed genus, the 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 at the time of filing. See In re Reiffin v. Microsoft Corp., 214 F.3d 1342, 1345, 54 USPQ2d 1915, 1917 (Fed. Cir. 2000) . “ Even if a claim is supported by the specification, the language of the specification, to the extent possible, must describe the claimed invention so that one skilled in the art can recognize what is claimed . The appearance of mere indistinct words in a specification or a claim, even an original claim, does not necessarily satisfy that requirement. ” See In re Enzo Biochem , Inc. v. Gen – Probe, Inc., 323 F.3d 956, 968, 63 USPQ2d 1609, 1616 (Fed. Cir. 2002). See also MPEP § 2163. The written description requirement may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, 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 applicant was in possession of the claimed genus. See In re University of California v. Eli Lilly & Co., 1 1 9 F.3d 1559, 1566, 43 USPQ2d 1398 , 1404 (Fed. Cir. 1997) ; and Juno Therapeutics, Inc. v. Kite Pharma, Inc. , 10 F.4th 1330, 1337, 2021 USPQ2d 893 (Fed. Cir. 2021) . A “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, the applicant must describe a sufficient variety of species to reflect the variation within the genus. See In re AbbVie Deutschland GMBH v. Janssen Biotech , 759 F.3d 1285, 1300, 111 USPQ2d 1780 , 1790 (Fed. Cir. 2014). The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure "indicates that the patentee has invented species sufficient to constitute the gen[us]." See In re Enzo Biochem , 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) . "A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed." See In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004) . The Federal Circuit has clarified the application of the written description requirement to inventions in the field of biotechnology. 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. This is because functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support, especially in technology fields that are highly unpredictable, where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus. 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.” The description needed to satisfy the written description varies depending on the nature and scope of the claims and on the complexity and predictability of the relevant technology. See In re University of California v. Eli Lilly and Co., 119 F.3d 1559, 1568, 43 USPQ2d 1398, 1406 (Fed. Cir. 1997); In re AbbVie Deutschland GMBH v. Janssen Biotech , 759 F.3d 1285, 1300, 111 USPQ2d 1780 , 1790 (Fed. Cir. 2014) ; In re Ariad Pharms., Inc. v. Eli Lilly & Co. , 598 F.3d 1336, 94 USPQ2d 1161 (Fed. Cir. 2010) ; and In re Capon v. Eshhar , 418 F.3d at 1357, 76 USPQ2d at 1084 . Claims 1 – 8 are drawn to an antibody , which encompasses a monoclonal antibody , that binds to a norovirus antigen. At a minimum, at least six of the parent al CDRs that could define an antibody genus with this function must be defined . However, no such CDRs are taught by the claims, leading one to turn to the instant disclosure. Paragraph 0017 of the instant disclosure teaches that the anti-norovirus antibody undergoes an antigen-antibody reaction with the peptides composed of SEQ ID NOs: 1 and 2 and binds to an epitope in the shell domain of the norovirus capsid protein (VP1) considered in SEQ ID NOs: 3 and 4, which are found within SEQ ID NOs: 1 and 2, respectively. There is no recitation for the sequence of even one parental CDR in the instant disclosure. The closest teaching of the antibody occurs in paragraph 0030, wherein hybridoma cells are cultured according to conventional methods to obtain a monoclonal antibody that is, in turn, propagated in a mammal. It is further taught by the instant disclosure that noroviruses are rich in genetic diversity and classified into five groups based on sequence similarity of capsid genes (paragraph 0003). In general, this creates an enormous breadth of potential antibody sequences with the six parental CDRs for a single norovirus that becomes innumerable when coupled with the massive genera of sequences for the five different groups of noroviruses . When there is substantial variation within the genus, as here, one must describe a sufficient variety of species to reflect the variation within the genus to provide a “representative number” of species. The claims are drawn to several genera, i.e., norovirus groups , which are each comprised of innumerable sequences, yet, the specification has only adequately described, and successfully reduced to practice, two generic anti-norovirus shell domain antibodies that bind to the desired epitope without disclosing any structural or functional limitations of the antibodies themselves (paragraphs 0045 – 0050). This is not representative of the extremely large genus of sequences claimed. One of ordinary skill in the art cannot conclude that Applicant was in possession of the innumerable antibodies encompassed by the disclosed genera. Absent the disclosed antigen sequences, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, each individual sequence utilized for the antibody . Thus, it is clear that the breadth of the recited genera in the claims far overreaches the Applicant’s contribution. In the absence of a representative number of examples, the specification must at least describe the structural features that are required for the claim function. In the instant case, the specification should explain the structure of the antibody that is required to bind to the defined epitopes, namely the CDRs . However, the specification fails to describe any substantive structural limitations as to establish the criteria necessary to design an antibody against norovirus that binds to the epitopes and has all six parental CDRs . At best, the specification contemplates the use of BLAST to identify functional homologs based on sequence homology. However, this is not sufficient to describe members of the claimed genus because such methods access online databases that are continually being updated as sequencing technology improves. As a result, they are not a static source of information. Therefore, one having ordinary skill in the art would readily appreciate that relying on a non–patent source that is continuously subject to change as a means to identify members of the claimed genus does not sufficiently meet the written description requirement. The d isclosure of an antigen fully characterized by its structure, formula, chemical name, physical properties, or deposit in a public depository does not, without more, provide an adequate written description of an antibody claimed by its binding affinity to that antigen, even when preparation of such an antibody is routine and conventional. See Amgen Inc. v. Sanofi, 872 F.3d 1367, 1378, 124 USPQ2d 1354, 1361 (Fed. Cir. 2017)("knowledge of the chemical structure of an antigen [does not give] the required kind of structure-identifying information about the corresponding antibodies"); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1351-52, 97 USPQ2d 1870, 1877 (Fed. Cir. 2011) (patent disclosed the antigen the claimed antibody was supposed to bind, but did not disclose any antibodies with the specific claimed properties) . D escribing a composition by its function alone typically will not suffice to sufficiently describe the composition. See Eli Lilly, 119 F.3 at 1568, 43 USPQ2d at 1406 (Holding that description of a gene’s function will not enable claims to the gene "because it is only an indication of what the gene does, rather than what it is."); see also Fiers , 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen Inc. v. Chugai Pharm. Co., 927 F.2d 1200, 18 USPQ2d 1016 (Fed. Cir. 1991)). An adequate written description of a chemical invention also requires a precise definition, such as by structure, formula, chemical name, or physical properties, and not merely a wish or plan for obtaining the chemical invention claimed. See Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 927, 69 USPQ2d 1886, 1894-95 (Fed. Cir. 2004) . See MPEP 216 Thus, while Applicant has generically described the antigen the claimed antibody is supposed to bind, no specific properties of the claimed antibody have been adequately described. The claims encompass millions of antibody structures that cannot be visualized from the prior art or instant disclosure. One having ordinary skill in the art cannot determine the structures encompassed by the claimed genera. The described species is too generic and cannot be considered representative of the entire recited genus. No parental CDRs have been described in the claims or instant disclosure. Overall, the claims as currently written are not adequately described and one of ordinary skill in that art would readily appreciate that Applicant was not in possession of the claimed genera , i.e., an anti-norovirus antibody that binds to the disclosed epitopes of SEQ ID NOs: 1 – 4 , at the time of filing. Due to the variation among antibodies with respect to their CDRs, the structure of which is what correlates with their function, it is very difficult to provide adequate representation, i.e., written description, of a functionally defined antibody genus. For example, it is highly unlikely that any CDR structure will be shared by an entire genus. Additionally, the disclosure of one set of antibody CDRs does not guide one of skill in the art to the next set of CDRs. That is to say that all CDRs are unique and none are obvious. This is because it is well known in the art that the mutation of even a single CDR residue can dramatically impact antibody function, and even lead to the loss of antigen binding. For example, it is taught by Rudikoff , S., et. al. , ( Single amino acid substitution altering antigen-binding specificity. Proceedings of the National Academy of Sciences of the United States of America , 79 (6), 1979–1983 ; Published 03/1982) that the mutation of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding specificity (page 1979, title and abstract). Thus, while Applicant has described one or more species within each of the genera recited, and the art may provide more, each genus is very large and would encompass antibody structures, i.e., CDR sets, that cannot be visualized from the prior art or instant disclosure. One with skill in the art cannot determine the antibody structures encompassed by the claimed genera as they are only defined by their function. Any future antibody structure may or may not be encompassed, and if it is, it would not have been represented in Applicant’s disclosed species. Therefore, the described species of the prior art and specification cannot be considered representative of the recited genera of antibodies. E.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). 35 USC § 112(a) – Scope of Enablement 1 7 . Claim s 1 – 8 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA), first paragraph, because the specification, while being enabling for the tested antibodies and fragments thereof that have a full set of parental CDRs , does not reasonably provide enablement for merely any antigen-binding fragment, which reads on having as little as one CDR . The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims. 1 8 . In order to determine compliance with the enablement requirement of 35 U.S.C. 112(a), the Federal Circuit has developed a framework of factors in In re Wands , 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988), referred to as the Wands factors, to assess whether any necessary experimentation required by the specification is "reasonable" or is "undue." The factors considered include , but are not limited to: (A) the breadth of the claims; (B) the nature of the invention; (C) the state of the prior art; (D) the level of one of ordinary skill in the art; (E) the level of predictability in the art; (F) the amount of direction provided by the inventor; (G) the existence of working examples; and (H) the quantity of experimentation needed to make or use the invention based on the content of the disclosure. Breadth of the claims and nature of the invention: Claim s 1 and 2 of the claimed invention are drawn to an anti-norovirus antibody , or an antigen-binding fragment thereof , that binds to an antigen with SEQ ID NOs: 1 and 2, which has the epitopes disclosed in SEQ ID NOs: 3 and 4. Further limitations include that the antibody be a monoclonal antibody, as disclosed in claims 3 and 6. Those with relevant skill in the art: The level of skill in the art is that of Ph.D.-level scientists and medical doctors (D.O. and/or M.D.). Amount of direction and existence of working examples: The instant application teaches a single working example with two generic antibodies, which does not represent an example for any antigen-bind fragment, which could be numerous CDRs or as little as one CDR. The closest working example is in paragraphs 0039 – 0050. It is taught that mice are immunized with norovirus virus-like particles (VLPs), then cells were fused with mouse myeloma cells to yield hybridomas. The hybridoma cells are cultured according to conventional methods to obtain a monoclonal antibody that is, in turn, propagated in mice. This resulted in cell lines that produce anti-norovirus monoclonal antibodies, wherein two antibodies directed to the shell domain of norovirus , i.e., SMoAb1 and SMoAb2, were found to recognize SEQ ID NOs: 3 and 4. Aside from the two antibodies disclosed, there is no guidance as to what CDRs are required to bind to the defined epitopes. The instant disclosure offers no reasonable guidance or direction to use any antigen-binding fragments. State of the prior art and unpredictability in the art: It is taught by Paul, W. E., ( Fv structure and diversity in three dimensions, Fundamental Immunology , 3 , 292-295; Published 1993), hereby Paul, that an intact antigen-binding site of antibodies generally requires the association of the complete heavy and light chain variable regions of a given antibody (page 293, left column, lines 3 – 8; right column, lines 1 – 9 and 27 – 30). It is further taught that both the heavy and light chain variable regions are comprised of three CDRs or hypervariable regions, for a total of six CDRs per antibody, which provide the majority of the contact residues for the binding of the antibody to its target epitope (page 293, left column lines 3 – 8 and 19 – 22) . 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 immunoglobulin (page 293, left column, lines 8 – 22). It is expected that all of the heavy and light chain CDRs are required in their proper order in the context of framework sequences which maintain their required conformation in order to produce a protein having antigen-binding function. Moreover, the proper association of the CDRs for both the heavy and light chain variable regions is required in order to form functional antigen-binding sites. It is further taught by Bendig M. M., (Methods: A Companion to Methods in Enzymology, 8 , 83-93; Published 1995), hereby Bendig , teaches that the general strategy for “humanizing” antibodies involves the substitution of all six CDRs from a rodent antibody and grafting these regions into human regions (page 83, abstract and right column, second paragraph; page 84). It is noted that Bendig used Kabat CDRs in their humanization process (page 86, right column, second paragraph). Bendig goes on to teach that the six CDRs of the antibody’s light and heavy chain variable regions form loop-like structures that make direct contact with the antigen, holding it in place (page 84, figure 3 ) . Quantity of experimentation needed: At a minimum, the art teaches that a skilled artisan would consider the predictive function of an antibody if the six CDRs are defined, wherein there are three each for the heavy and light chain variable regions, in the context of the framework sequences with the correct spatial orientation . Thus, one of skill in the art would neither expect nor predict the appropriate function of an y antigen-binding fragment of the instant claims for a n anti-norovirus antibody as broadly as claimed , as such a fragment could have as little as one CDR antibody and, thus, would not provide the framework required to bind to the disclosed antigen. Any and all enablement of the claimed fragments must therefore come from the instant disclosure. However, the instant disclosure only teaches the production and usage of two generic anti-norovirus shell domain antibodies that bind to the desired epitope . The claims are clearly not enabled to their full scope. Moreover, claims not containing elements critical or essential to the practice of the invention, such as antibodies or antibody fragments not having all of the relevant functional CDRs in the proper site on an appropriate antibody heavy or light chain framework, are not enabled by the disclosure. Claims that contain materials demonstrated not to bind to the critical element of the invention are also not enabled by the disclosure. See In re Mayhew , 527 F.2d 1229, 188 USPQ 356 (CCPA 1976). For the reasons discussed above, undue experimentation would be required to practice the claimed invention commensurate with the scope of the claims. Reasonable correlation must exist between the scope of the claims and scope of enablement set forth. It would take undue trials and errors to practice the claimed invention in view of the quantity of experimentation necessary, the limited working examples, the unpredictability of the art, the lack of sufficient guidance in the specification, and the breadth of the claims. Conclusion : The instant disclosure is not enabling for any antigen-binding fragment as presently written, but rather FILLIN "Identify claimed subject matter for which the specification is enabling" \* MERGEFORMAT the tested antibodies and fragments thereof that have a full set of parental CDRs that binds to the disclosed antigen sequences . Thus, any claim that does not further limit the “ an antigen-binding fragment ” as presently written to an antibody is not enabled. This includes claims 1 – 8, i.e., all claims . It i s recommended that all iterations of “an antigen-binding fragment thereof ” be re moved. Claim Rejections - 35 USC § 102 16. 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. 17. Claim s 1 and 2 are rejected under 35 U.S.C. 102 FILLIN "Insert either \“(a)(1)\” or \“(a)(2)\” or both. If paragraph (a)(2) of 35 U.S.C. 102 is applicable, use form paragraph 7.15.01.aia, 7.15.02.aia or 7.15.03.aia where applicable." \d "[ 2 ]" (a)(1) as being FILLIN "Insert either—clearly anticipated—or—anticipated—with an explanation at the end of the paragraph." \d "[ 3 ]" anticipated by Hansman , G. S., et. al. , ( Genetic and antigenic diversity among noroviruses. The Journal of general virology , 87 (Pt 4), 909–919 ; Published 04/01/2006; Cited in Applicant’s IDS on 09/24/2024 as Non-Patent Literature (NPL) Document Doc. No. AF), hereby Hansman . Hansman teaches cross-reactivity using polyclonal antisera raised against among 26 different norovirus virus-like particles (VLPs; page 910 , right column). VLPs belonging to six genogroup I (GI) and 12 genogroup II (GII) genotypes were constructed (pages 910 and 911, expression of VLPs; page 917, left column, last paragraph). It is taught that hyperimmune sera to these norovirus VLPs were prepared in rabbits, then an antibody ELISA was used to compare cross-reactivities among the VLPs (page 91 1 , right column, second paragraph). A number of cross-reactive polyclonal antiserum were reported, including one several that cross-reacted strongly with genotypes from both GI and GII (page 912, right column, second and third paragraphs; page 914, right column, first and second paragraph; page 917, right column, second paragraph). Within these polyclonal antisera that are cross-reactive with the capsid protein from both GI and GII, there will be an antibody molecule that binds each antigenic sequence therein. In fact, Hansman teaches that the broad cross-reactivities were due to conserved residues in the shell and/or P1 domains of the norovirus capsid protein, wherein each VLP has unique epitopes that it binds (page 017, right column, second paragraph). This reads on instant claims 1 and 2 , wherein SEQ ID NO: 1 is drawn to the sequence of a GI capsid protein and SEQ ID NO: 2 is drawn to the sequence of a GII capsid protein. Thus, claims 1 and 2 are anticipated by Hansman . Claim Rejections - 35 USC § 103 1 8 . 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. 1 9 . The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: Determining the scope and contents of the prior art. Ascertaining the differences between the prior art and the claims at issue. Resolving the level of ordinary skill in the pertinent art. Considering objective evidence present in the application indicating obviousness or nonobviousness . 20 . Claims 1 – 8 are rejected under 35 U.S.C. 103 as being unpatentable over FILLIN "Insert the prior art relied upon." \d "[ 4 ]" Motohiro Miki, G., (US 20140349277 A1; Published 11/27/2014; Cited in Applicant's IDS on 09/24/2024 as U.S. Patent Document Doc. No. AB), hereby Miki , and in further view of Brusic , V., et. al. , (US 9205144 B2; Published 12/08/2015), hereby Brusic , and Richardson, C., et. al., (US 8841120 B2; Published 09/23/2014), hereby Richardson, as evidenced by De Los Rios, M., et. al. , (WO 2010042742 A2; Published 04/15/2010), hereby Rios, Wang, C. Y. (US 20140271690; Published 09/18/2014), hereby Wang , and Crowe, J. E. and Estes, M. (WO 2020046857 A1; Published 03/05/2020; Cited in Applicant’s IDS on 09/24/2024 as Foreign Patent Doc. No. AD), hereby Crowe . Miki teaches an anti-human-norovirus GII that is either a polyclonal antibody or monoclonal antibody (page 3, paragraph 0059), as claimed in instant claims 1 – 3 and 6 . It is taught that an animal, particularly a mouse, is immunized with a sensitizing antigen, i.e., genogroup II (GII) norovirus-like particles (page 4, paragraphs 0062 and 0063; page 5, paragraph 0079). After immunization and confirmation of a rise in serum level of an antibody of interest, the blood is collected from the mouse and the serum is purified to produce a polyclonal antibody that binds to at least one epitope of GII (page 1, paragraphs 0011 and 0013; page 4, paragraph 0063 ). To produce a monoclonal antibody with high norovirus reactivity , immunocytes are removed and subject to cell fusion to form hybridomas (page 3, paragraphs 0059 and 0060; page 4, paragraphs 0060 – 0069; see also example 1 from paragraphs 0078 – 0090 on pages 5 and 6). Miki goes on to teach that th is anti-human-norovirus antibody can be applied to an immunological assay method to specifically detect and measure human norovirus GII present in a specimen (page 4, paragraph 0071), as defined in instant claims 4, 5, 7, and 8. Here, the detection of norovirus GII in a specimen is on the basis of a reaction between norovirus present in the specimen and an immobilized anti-norovirus GII antibody (pages 4 and 5, paragraph 0075), as required in instant claims 4, 5, 7, and 8. It is further taught that the immunoassay can also be a kit that contains an immobilized anti-human-norovirus GII antibody, a diluent for a specimen, a labeled anti-norovirus GII antibody, a reaction substrate, and other components (page 5, paragraph 0077), as broadly disclosed in instant claims 4 and 7 . Miki goes on to teach the production of an immunochromatographic method, wherein a solution containing the anti-human-norovirus antibody is applied to a sheet in a line patter to attain a coating and provide test lines (page 6, paragraph 0093). It is further taught that a sample pad, the membrane, the conjugate pad, and an absorption pad were stacked in this order on a plastic backing sheet , wherein the product was cut to provide test strips. i.e., an immunoassay device (page 6, paragraph 0095), as required in instant claims 5 and 8. While the antibody taught by Miki is a monoclonal antibody , its antigenic epitope is in the protruding (P) domain of the capsid protein found in GII noroviruses (page 1, paragraph 0011; page 6, paragraph 0086), not the stem domain of GII as instantly claimed in claims 1 – 8. However, Miki teaches that the norovirus GII has the sequence disclosed in SEQ ID NOs: 2 and 4 (see figure 1-1 as reproduced below, underline added to emphasize location of SEQ ID NO: 2). Brusic teaches a method of treating or preventing norovirus infection in a subject by administering a therapeutically effective amount of a composition comprised of 1 or more peptides of an amino acid sequence shown in figure 65 ( column 37, lines 33 – 39; see figure 65-4 as reproduced below on the left). One such sequence, i.e., SEQ ID NO: 266011, has a portion of the antigenic epitope disclosed in instant SEQ ID NO s : 2 and 4 , as demonstrated in the sequence alignment reproduced below on the right (see also SEQ ID NOs: 265917, 266034, and 266053). The Board of Patent Appeals and Interferences has taken the position that once an antigen has been isolated, the manufacture of monoclonal antibodies against it is prima facie obvious. See Ex parte Ehrlich, 3 USPQ 2d 1011 (PTO BPAI, 1987) and Ex parte Sugimoto , 14 USPQ 2d 1312 (PTO BPAI, 1990). In light of this case law and the teachings of Brusic , it would have been obvious for a person having ordinary skill in the art to design a monoclonal antibody directed to the antigenic center bottom epitope s of instant SEQ ID NOs: 2 and 4 , as required in instant claims 1 – 3 and 6. Miki and Brusic do not teach the design of an anti-norovirus antibody that binds to the stem (S) domain of GI , i.e., SEQ ID NOs: 1 and 3, and th e combination of that epitope with an epitope directed to GII, as required in instant claims 1 – 8. However, Richardson teaches a polypeptide comprising a composite capsid sequence from two or more circulating strains of a non-enveloped virus, wherein the two strains may be from GI or GII of norovirus, as a vaccine formulation (column 2, lines 55 – 65; column 6, lines 9 – 13), as required in instant claims 1 – 8. The composite sequence for each strain is derived from consensus sequences of VP1 proteins from different norovirus strains within GI and GII (column 6, lines 19 – 26). The consensus sequence itself is determined by aligning and comparing the nucleotide sequences of two or more viruses (column 6, lines 26 – 36). 0 2583815 Richardson does not explicitly teach that the GI and GII antibodies are instant SEQ ID NOs: 1 – 4. However, Richardson does teach that the consensus sequence is SEQ ID NO: 12 for GI and SEQ ID NO: 7 for GII, wherein SEQ ID NO: 12 comprises a portion of instant SEQ ID NOs: 1 and 3 and SEQ ID NO: 7 comprises a portion of instant SEQ ID NOs: 2 and 4 (column 10, lines 48 – 58; column 26, lines 13 – 19; column 27, lines 22 – 28 ; see also figures 20 and 21 as reproduced below on the top and bottom, respectively, with emphasis added , i.e., boxed in, to indicate the portion of SEQ ID NOs: 2 and 4 and 1 and 3, correspondingly ). Rios teaches that the first 20 amino acids of the capsid protein of Norwalk Virus, i.e., Norovirus, is the N-terminus (page 17, paragraph 0078), wherein this includes instant SEQ ID NOs: 1 and 3 (see alignment results as reproduced below). It would have been prima facia obvious to a person having skill in the art to design an antibody against the terminal portions of a protein as is standard practice in the art. In support of this, Wang teaches that B cells from the blood of patients previously receiving a vaccine formulation are used for the preparation and selection of human monoclonal antibodies targeting the N-terminus of Aβ , i.e., a protein, for the prevention and treatment of Alzheimer’s Disease ( page 16, paragraph 0276 ). Thus, Wang evidences the standard practice in this art to raising antibodies against termini of protein targets, including the N-terminus, wherein Richardson and Rios teach that the N-terminus of GI and GII is that of instant SEQ ID NOs: 1 – 4, center 5076825 0 0 as required in instant claims 1 – 8 . Miki, Brusic , and Richardson are considered to be analogous to the claimed invention because all are drawn to therapeutics, i.e., antibodies or vaccines, to protect and/or treat norovirus infections . Based on the prior art teachings , it would have been obvious to a person having ordinary skill in the art to generate monoclonal antibod ies against the N-terminus of the G1 and GII peptides and/or using each short epitope taught by the art above , as taught by Brusic and Richardson and evidenced by Rios and Wang , for use as or in an immunoassay as taught by Miki. This obviousness is mainly owed to Miki teaching the production of a monoclonal antibody that binds epitopes in a norovirus GII capsid protein and can be used in an immunoassay device, wherein Brusic and Crowe make improvements on the antibodies thereof in an attempt to elicit a protective immune response against multiple norovirus genogroups . Therefore, it would have been obvious to a person having ordinary skill in the art to have combined the teachings of Miki, Brusic , and Richardson before the effective filing date of the claimed invention with a reasonable expectation of success to provide an anti-norovirus antibody that can comprehensively detect human noroviruses of different genotypes (Miki; abstract, page 1, paragraph 0006) . This could be accomplished by combining the two obvious monoclonal antibodies above to generate an oligoclonal antibody that binds to both the GI and GII epitopes . Numerous bispecific antibodies are known in the prior art. For example, Crowe teaches bi specific antibodies against norovirus that have binding specificities for at least two different epitopes, wherein a first antigen binding site is combined with a binding site for a second antigen (page 52, lines 11 – 16; claims 13 and 22). In turn, generating a recombinant bispecific antibody wherein one arm binds to an epitope of GI and the other arm binds to an epitope of GII would yield the predictable result of versatile detection and/or protection against multiple human norovirus subtypes (increased sensitivity) . Moreover, both the oligoclonal or bispecific antibody would have also been predictably useful in the immunoassay discussed above. Conclusion 21 . Claims 1 – 8 are rejected. No claims are allowed. 2 2 . Any inquiry concerning this communication or earlier communications from the Examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT Hallie N. Pennington, Ph.D. whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-6781 . The Examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-Th 7:30-5:30 ET . 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, FILLIN "SPE Name?" \* MERGEFORMAT Michael Allen can be reached at FILLIN "SPE Phone?" \* MERGEFORMAT (571)270-3497 . 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. /HALLIE N. PENNINGTON, PH.D./ Examiner, Art Unit 1671 /Michael Allen/ Supervisory Patent Examiner, Art Unit 1671