DETAILED ACTION Notice of Pre-AIA or AIA Status The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Election/Restrictions Applicant's election with traverse of invention I in the reply filed on 10/27/2025 is acknowledged. The traversal is on the ground(s) that the claimed inventions are drawn to product and process of use and therefore share unity of invention . This is not found persuasive because the claimed inventions do not provide a contribution over the prior art (see 35 USC 102a1 rejection below) . The requirement is still deemed proper and is therefore made FINAL. Claim 61 is withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention , there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 10/27/2025 . Claims 1, 3, 5, 7-9, 13, 17, 18, 22, 32, 33, 35-39, 43-45, 49, 53-55, 59 and 60 are examined on the merits. Information Disclosure Statement The information disclosure statement (IDS) submitted on 9/30/2022 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Objections Specification This application contains sequence disclosures that are encompassed by the definitions for nucleotide and/or amino acid sequences set forth in 37 CFR 1.821(a)(1) and (a)(2). However, this application fails to comply with the requirements of 37 CFR 1.821 through 1.825 for the reason(s) set forth below. The specification is objected to because figures descriptions for drawings 2 and 3 present amino acid sequences but no SEQ ID NO: are mentioned in these descriptions. Applicants must comply with sequence rules in order to be considered a complete response to this Office Action. Drawings The drawings are objected to because figures 3 and 7 possess unclear text (figure 3 displays a sequence, but the sequence is not legible and figure 7 presents line graphs with unclear text throughout. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Claim Rejections - 35 USC § 112 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, 3, 5, 7-9, 13, 17, 18, 22, 32, 33, 35-39, 43-45, 49, 53-55, 59 and 60 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 following quotation from section 2163 of the Manual of Patent Examination Procedure is a brief discussion of what is required in a specification to satisfy the 35 U.S.C. 112 written description requirements for a generic claim covering several distinct inventions: 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 .... 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 Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406. 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, one must describe a sufficient variety of species to reflect the variation within the genus. Thus, when a claim covers a genus of inventions, the specification must provide written description support for the entire scope of the genus. Support for a genus is generally found where the applicant has provided a number of examples sufficient so that one in the art would recognize from the specification the scope of what is being claimed. Claims 1, 3, 5, 7-9, 13, 17, 18, 22, 32, 33, 35-39, 43-45, 49, 53-55, 59 and 60 are rejected as lacking adequate descriptive support for possessing an isolate peptide: comprising a haemagglutinin subtype 5 (H5) globular head domain, and optionally a haemagglutinin stem domain, with the following amino acid residues at positions 156, 157, 171, 172, and 205 of the head domain: i ) 156: R, 157: P, 171: D, 172: T, and 205: K; ii) 156: R, 157: P, 171: N, 172: T, and 205: K; or iii) 156: R, 157: S, 171: N, 172: A, and 205: R. In addition, the isolated polypeptide is at least 70% identical to SEQ ID NO:s 1, 3, 7, 8, 10 or 11. The claimed invention alternatively requires an isolated polypeptide having at least 70% sequence identity to SEQ ID NO: 5, 9, or 12 with an F amino acid at positions 148 and 166 or a polypeptide having at least 70% identity to SEQ ID NO: 13 with amino acids: 1: R. 2: P, 16: D, 17: T, and 50: K; 1: R, 2: R, 16: N, 17: T, and 50: K; or 1: R, 2: S, 16:N, 17: A, and 50: R The polypeptides are within an influenza hemagglutinin protein or represent the full-length sequence of such a hemagglutinin protein. These hemagglutinin proteins possess at least one function (binding sialic acid on cell surfaces ), however, the claims recite that 30% of the claimed amino acid sequences can be varied. This degree of variation ranges from 15 to 170 amino acids based on the amino acid length of SEQ ID NO:s 1, 3, 5, 7, 8, 9, 10, 11 and 13. In support of the claimed genus ( polypeptides with 70% identity to the claimed sequences ), the application discloses 9 specific amino acid sequences (SEQ ID N0:s 1, 7 and 10) which are full-length H5 HA proteins . Thu s, the application fails to provide examples of any species within the claimed genus. Thus, in view of the above, there would have been significant uncertainty as to which portions of the 30% variation of the claimed HA proteins can vary and still retain the functions of a full-length HA . In view of this uncertainty and the lack of any examples of the claimed genus, the claims are rejected for lack of adequate written description support. Claims 17, 18, 22, 32, 33, 35 and 36 are rejected under 35 U.S.C. 112, first paragraph, as containing subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention. Applicant broadly claims a host cell or expression vector or nucleic acid containing the nucleic acids of claims 17, 18, 22, 32, 33, 35 and 36 . The claims read on a transgenic animal or a transgene therein given that the term "isolated" is not denoted in describing the nucleic acid, or expression vector. With respect to the transgenes as “nucleic acids” or “ expression vectors “of the instant claims discussed above, the state of the art at the time of filing was such that one of skill could not predict the phenotype of transgenics. The art of transgenic animals has for many years stated that the unpredictability lies, in part, with the site or sites of transgene integration into the target genome and that "the position effect" as well as unidentified control elements are recognized to cause aberrant expression of a transgene (Wall et Al., Theriogenology, Vol. 45, Pg. 57-68, 1996). The elements of the particular construct used to make transgenic animals are also held to be critical, and they must be designed case by case without general rules to obtain good expression of a transgene; e.g., specific promoters, presence or absence of introns, etc. ( Houdebine et Al., Journal of Biotechnology, Vol. 34, Pg. 269- 287, 1994). Furthermore, transgenic animals are regarded to have within their cells, cellular mechanisms that prevent expression of the transgene, such as methylation or deletion from the genome ( Kappell et Al., Current Opinions in Biotechnology, Vol. 3, Pg. 548-553, 1992). Houdebine (Comparative Immunology, Microbiology, and Infectious Diseases, Vol. 32, Pg. 107-121, 2009) teaches progress has been made in the field of transgenic animals for production of foreign proteins (Abstract); however, constructing an efficient expression vector to produce a therapeutic protein is not a standard operation (Pg. 116, Paragraph, second). Therefore, undue experimentation is required to make and use a transgene and transgenic animal to produce the antibody and antibody fragments of the instant claims. Examples in the literature aptly demonstrate that even closely related species carrying the same transgene construct can exhibit widely varying phenotypes. Mullins (1993, Hypertension, Vol. 22, No. 4, pp. 630-633) states that not all animals express a transgene sufficiently to provide a model for a disease as the integration of a transgene into different species of animal has been reported to give divergent phenotypes. For example, several animal models of human diseases have relied on transgenic rats when the development of mouse models was not feasible. Mullins (1990, Nature, Vol. 344, 541-544) produced outbred Sprague-Dawley x WKY rats with hypertension caused by expression of a mouse Ren-2 renin transgene. Hammer (1990, Cell, Vol. 63, 1099- 1112) describes spontaneous inflammatory disease in inbred Fischer and Lewis rats expressing human class I major histocompatibility allele HLA-B27 and human 02- microglobulin transgenes. Both investigations were preceded by the failure to develop human disease-like symptoms in transgenic mice expressing the same transgenes that successfully caused the desired symptoms in transgenic rats (Mullins, 1989, EMBO J., Vol. 8, pages 183-191 ). Thus, the use of nonmurine species for transgenesis will continue to reflect the suitability of a particular species for the specific questions being addressed, bearing in mind that a given construct may react very differently from one species to another. The examiner notes here, in addition to these issues, even assuming arguendo a person having ordinary skill in the art could make a host organism with functional transgene that encodes the instantly recite d SEQ ID NO: 1 , there is no predictability that the host will survive its expression. The transgene depends on the host for function and harm to the host, including death, renders the transgene nonfunctional and thus not enabled. The art is well-aware of side effects caused by expressing proteins, such as therapeutic antibodie s . In a transgenic cell or animal that expresses the same, the antibody will exert any possible side effect it can. It is not administered but chronically present and so such side effects are chronic and potentially more serious than any from an administered antibody. Hansel (Nature Reviews Drug Discovery, Vol. 9, Pg. 325-337, 2010) teaches in their table 1 on page 328 numerous exemplary side effects from licensed monoclonal antibodies to include: increased bleeding risk, infection, heart failure, cancer, thyroid disorder, autoimmune reactions, and cytokine release syndrome (CRS) to name only a few. One or more such effects, or similar, may occur with the therapeutic antibody instantly recited when administered and indeed be exacerbated by chronic exposure due to internal expression. The instantly encoded antibody binds a mammalian protein and so may very well target related or unrelated proteins in the transgenic host, leading to such side effects. For all these reasons, previously raised and new, transgenes are not enabled. At the time of filing, the phenotype of a transgene and transgenic cell contained within any animal was unpredictable. The claims as written, encompassing a transgene in a transgenic animal, is not adequately described in the specification as to prevent excessive experimentation by the public to generate and use the invention. Applicants can obviate the instant rejection by amending the claim to recite the term "isolated" before the vector and polynucleotide claims to specify they are not in a transgenic animal. Applicant may consider using purified in such claims if description is appropriate for such a term and it is not redefined away from standard meaning. Method claims using these products should also carry the appropriate adjectives above. In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to make and use transgenic animals possessing the claimed nucleic acid, or expression vector, with a reasonable expectation of success, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed nucleic acid, or expression vector, commensurate in scope with the claimed invention. The same can be said for the transgenes and transgenic animals encompassed by the instant claims. Thus, the claims are rejected here. 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 appl icant regards as his invention. Claim s 1 , 3, 5 , 7 , 17, 17, 22, 32, 33, 35-39, 43-45, 49, 53-55, 59 and 60 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 recites, “An isolated polypeptide comprising a haemagglutinin subtype 5 globular head domain …with the following amino acid residues at positions 156, 157, 171, 172 and 205 of the head domain: 156: R, 157: P, 171: D, 172: T, and 205: K; 156: R, 157: P, 171: N, 172: T, and 205: K; or 156: R, 157: S, 171: N, 172: A, and 205: R. ” However, it is unclear where these domains exactly are in the head domain amino acid sequence and as a result where exactly the amino acid positions are in the H5 hemagglutinin. Is the head domain full-length or a functional fragment thereof, is the head domain attached to a stem domain, is the HA protein that possesses the head domain full-length. It is suggested that applicants amend claim 1 to recite a corresponding SEQ ID NO: of an amino acid sequence that would clarify where these residues are located. Claim 3 (see lines 6 and 7) of the instant application possesses such a corresponding claim limitation as an example. Claims 3, 5, 7, 17, 17, 22, 32, 33, 35-39, 43-45, 49, 53-55, 59 and 60 are also rejected because they depend from claim 1, but do not remedy this deficiency. Claim 3 recites, “which has the following amino acid residues at positions corresponding to positions 156, 157, 171, 172 and 205 of SEQ ID NO: 7 or 8…”. However, SEQ ID NO: 7 is 568 amino acids long while SEQ ID NO: 8 is 268 amino acids long. Furthermore, while SEQ ID NO: 7 comprises SEQ ID NO: 8, the amino acids at positions 156, 157, 171, 172 and 205 of SEQ ID NO: 7 do not li ne up with the same positions of SEQ ID NO: 8. Therefore, it is unclear which SEQ ID NO: is properly functioning as the corresponding amino acid sequence of the claimed invention. Claim 5 recites, “which has the following amino acid residues at positions corresponding to positions 156, 157, 171, 172 and 205 of SEQ ID NO: 10 or 11 …”. However, SEQ ID NO: 10 is 568 amino acids long while SEQ ID NO: 11 is 268 amino acids long. Furthermore, while SEQ ID NO: 10 comprises SEQ ID NO: 11 , the amino acids at positions 156, 157, 171, 172 and 205 of SEQ ID NO: 10 do not li ne up with the same positions of SEQ ID NO: 11 . Therefore, it is unclear which SEQ ID NO: is properly functioning as the corresponding amino acid sequence of the claimed invention. Claim 7 recites, “which has the following amino acid residues at positions corresponding to positions 156, 157, 171, 172 and 205 of SEQ ID NO: 1 or 3 …”. However, SEQ ID NO: 1 is 568 amino acids long while SEQ ID NO: 3 is 268 amino acids long. Furthermore, while SEQ ID NO: 1 comprises SEQ ID NO: 3 , the amino acids at positions 156, 157, 171, 172 and 205 of SEQ ID NO: 1 do not light up with the same positions of SEQ ID NO: 3 . Therefore, it is unclear which SEQ ID NO: is properly functioning as the corresponding amino acid sequence of the claimed invention. Claim 13 recites, “comprises an amino acid sequence of any of SEQ ID NO:s 5, 9, or 12, or an amino acid sequence that has at least…”. However, it is unclear if the recitation of “an amino acid sequence” includes fragments thereof or only the sequence of the claimed SEQ ID NO:. Claim Rejections - 35 USC § 103 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. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claim (s) 1, 17, 39, 43-45, 49 and 53 are rejected under 35 U.S.C. 103 as being unpatentable over Vaughn et al. (US PGPub 20080193471 ) and Genbank Accession: AJC97681 (1/15/2015) and KP311300 (1/15/2015) The claimed composition is drawn to a pharmaceutical composition comprising a pharmaceutically acceptable carrier, excipient, or diluent and a n isolated polypeptide comprising a haemagglutinin subtype 5 (H5) globular head domain, and optionally a haemagglutinin stem domain, with the following amino acid residues at positions 156, 157, 171, 172, and 205 of the head domain: i ) 156: R, 157: P, 171: D, 172: T, and 205: K; ii) 156: R, 157: P, 171: N, 172: T, and 205: K; or iii) 156: R, 157: S, 171: N, 172: A, and 205: R. In addition, the isolated polypeptide is also drawn to a polypeptide which comprises an amino acid sequence of SEQ ID NO: 1, 3, 7 8 , 10 or 11 . Alternatively, the pharmaceutical composition a nucleic acid molecule encoding a polypeptide which comprises an amino acid sequence of SEQ ID NO:7 or 8. The recitation of “comprises an amino acid sequence of” is interpreted to include fragments of the claimed SEQ ID NO:s. *Applicants can overcome this rejection by amending claims 43-45 and 53 to recite, “comprises the amino acid sequence of…”. Vaughn et al. teach t hus according to a further embodiment, the present invention also relates to a pharmaceutical/vaccine composition comprising i . a therapeutically effective amount of any one of the H5 proteins of influenza virus as described herein wherein the H5 protein having the amino acid 223N and the modification 328K+, wherein numbering of the amino acid positions of the H5 protein refers to the amino acid position as exemplarily given in SEQ ID NO:1 and wherein the modification 328K+ means that at amino acid position 328 of H5 protein a second Lysine (K+) is inserted and ii. a pharmaceutically acceptable adjuvants as described above. [see paragraphs 159-161] Vaughn et al also teach t he H5 proteins as provided herewith, the nucleic acid molecules coding for any such H5 proteins, the vectors comprising any such nucleic acid molecules coding for any such H5 proteins as described herein, and any pharmaceutical/vaccine composition comprising any of such H5 protein, nucleic acid molecule or vector can be used as a medicine, preferably for the treatment and prophylaxis of infections, caused by influenza virus, most preferably by influenza A virus. The H5 proteins as provided herewith, the nucleic acid molecules encoding for any such H5 proteins, the vectors comprising any such nucleic acid molecules encoding for any such H5 proteins as described herein, and any pharmaceutical/vaccine composition comprising any of such H5 protein, nucleic acid molecule or vector, as described herein, can be used for the treatment or prophylaxis of human beings as well as in veterinary medicine. When used in veterinary medicine, the treatment of poultry, preferably bird, chicken, duck, turkey and the like as well as mammals, preferably pigs, cattle, horses, seals, camels, dogs, cats, hamsters, mice and the like, is preferred. [see paragraph 179] However, Vaughn et al do not teach an H5 HA protein or nucleic acid sequence with sequence identity with a fragment of SEQ ID NO:s 1, 3, 7, 8, 10 and 11. Genbank Accession: AJC97681 is an amino acid sequence that comprises an H5 hemagglutinin protein which 100% identity to portions (fragments) of SEQ ID NO:s 1, 3, 7, 8, 10 and 11 (see alignment below) . Genbank Accession KP311300 is a nucleic acid sequence that encodes the hemagglutinin protein of AJC97681. It would have been obvious to one of ordinary skill in the art to modify the compositions taught by Vaughn et al. in order to combine a H5 HA protein with identical amino acid sequences to fragments of SEQ ID NO:s 1, 3, 7, 8, 10 and 11 and nucleic acid sequences which encode such a protein . One would have been motivated to do so, given the suggestion Vaughn et al. that influenza H5 h emagglutinin proteins and nucleic acid sequences can be combined with pharmaceutical carriers . There would have been a reasonable expectation of success, given the knowledge that an influenza HA protein and nucleic acid sequence encoding the protein were previously known as evidenced by Genbank accession AJC97681 and KP311300 . Thus the invention as a whole was clearly prima facie obvious to one of ordinary skill in the art at the time the invention was made. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Examiner name" \* MERGEFORMAT BENJAMIN P BLUMEL whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-4960 . The examiner can normally be reached FILLIN "Work Schedule?" \* MERGEFORMAT M-F 8-5 EST . 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. /BENJAMIN P BLUMEL/ Primary Examiner, Art Unit 1671