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 .
2. Claims 1-21 are pending and under consideration for their full scope.
3. Applicant’s IDS documents filed on 11/05/2024, 05/30/2025, 11/06/2025 and 02/18/2026 have been considered.
4. The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
5. Claims 1-21 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 14, 16, 18-19, 21, 23, 25-28, 39-42, 70-71 and 75-82 of copending Application No. 18/714,765 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because claims are directed to an ungulate-derived polyclonal human immunoglobulin composition, comprising: a population of ungulate-derived polyclonal human immunoglobulins, wherein the population of ungulate-derived polyclonal human immunoglobulins specifically binds an influenza hemagglutinin (HA) protein, and wherein the influenza HA protein is one or more of an HA protein of Influenza A and an HA protein of Influenza B; comprising glycans covalently linked to the population of ungulate-derived polyclonal human immunoglobulins, wherein the glycans are at least about 70% N-Glycolylneuraminic acid (NGNA) glycans; comprising glycans covalently linked to the population of ungulate-derived polyclonal human immunoglobulins, wherein the population of human immunoglobulins comprises less than about 50% N-Acetylneuraminic acid (NANA) glycans; wherein the population of ungulate- derived polyclonal human immunoglobulins comprises less than 5% chimeric IgG immunoglobulins; wherein the population of ungulate- derived polyclonal human immunoglobulins comprises less than 5% chimeric IgM immunoglobulins; the population of ungulate- derived polyclonal human immunoglobulins comprises at least about 70% of IgG1; wherein the population of ungulate- derived polyclonal human immunoglobulins comprises less than about 30% IgG2; wherein the population of ungulate-derived polyclonal human immunoglobulins comprises less than 4% of one or more of IgG3 and IgG4; a method of making an ungulate-derived polyclonal human immunoglobulin composition specific for influenza hemagglutinin (HA) protein, comprising; administering an effective amount of at least one influenza HA protein, or a polynucleotide encoding at least one influenza HA protein, to a transgenic ungulate, wherein the transgenic ungulate comprises a genome comprising a human immunoglobulin locus, or an artificial chromosome comprising a human immunoglobulin locus; and purifying a population of ungulate-derived polyclonal human immunoglobulins from serum or plasma of the transgenic ungulate, wherein the ungulate-derived polyclonal human immunoglobulin composition is made; comprising administering the influenza HA protein 3, 4, 5, or more times; wherein the influenza HA protein comprises one or more of a full-length influenza HA1 protein and a full-length influenza HA2 protein; comprising administering about 0.1 to 10 mg of the influenza HA protein to the transgenic ungulate; wherein an excipient is administered with the influenza HA protein; wherein the excipient is sodium chloride, monobasic sodium phosphate, dibasic sodium phosphate and/or polysorbate; an ungulate-derived polyclonal human immunoglobulin composition specific for influenza HA protein, prepared by the process of administering an effective amount of at least one influenza HA protein, or a polynucleotide encoding at least one influenza HA protein, to a transgenic ungulate, wherein the transgenic ungulate comprises a genome comprising a human immunoglobulin locus or an artificial chromosome comprising a human immunoglobulin locus; and purifying a population of ungulate-derived polyclonal human immunoglobulins from serum or plasma of the transgenic ungulate, wherein the ungulate-derived polyclonal human immunoglobulin composition is made; a pharmaceutical composition, comprising the composition of claim 1 and optionally one or more pharmaceutically acceptable excipients; a pharmaceutical composition, comprising the composition of claim 42 and optionally one or more pharmaceutically acceptable excipients; a method of treating influenza virus infection in a subject in need thereof, comprising administering an effective amount of the composition of claim to the subject; comprising glycans covalently linked to the population of ungulate-derived polyclonal human immunoglobulins, wherein the glycans are at least about 70% N-Glycolylneuraminic acid (NGNA) glycans; comprising glycans covalently linked to the population of ungulate-derived polyclonal human immunoglobulins, wherein the population of human immunoglobulins comprises less than about 50% N-Acetylneuraminic acid (NANA) glycans; wherein the population of ungulate-derived polyclonal human immunoglobulins comprises less than 5% chimeric IgG immunoglobulins; wherein the population of ungulate-derived polyclonal human immunoglobulins comprises less than 5% chimeric IgM immunoglobulins; wherein the population of ungulate-derived polyclonal human immunoglobulins comprises at least about 70% of IgG1; wherein the population of ungulate-derived polyclonal human immunoglobulins comprises less than about 30% IgG2; and wherein the population of ungulate-derived polyclonal immunoglobulins comprises less than 4% of one or more of IgG3 and IgG4.
The reference teachings anticipate the claimed invention.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
6. 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.
7. Claim 12 is 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 12 recites the limitation "the population of ungulate derived polyclonal immunoglobulins” in lines 1-2. There is insufficient antecedent basis for this limitation in the claim. The claim should recite "the population of ungulate derived human polyclonal immunoglobulins.
Correction is required.
Claim Rejections - 35 USC § 112
8. 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.
9. Claims 1-21 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 compositions comprising polyclonal human immunoglobulins of claims 1-21 derived from a transchromosomic goat and methods of production and use thereof, does not reasonably provide enablement for: the compositions comprising polyclonal human immunoglobulins of claims 1-21 derived from an ungulate and methods of production and use thereof.
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 or use the invention commensurate in scope with the claims. The specification disclosure does not enable one skilled in the art to practice the invention without an undue amount of experimentation.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to practice the claimed invention.
The specification has only disclosed polyclonal human immunoglobulins and a method of production thereof using a transchromosomic goat. The specification has no disclosure of any other “ungulate” from which polyclonal human immunoglobulins specific for influenza hemagglutinin are derived.
Reasonable correlation must exist between the scope of the claims and scope of the enablement set forth. In view on the quantity of experimentation necessary the limited working examples, the nature of the invention, the state of the prior art, the unpredictability of the art and the breadth of the claims, it would take undue trials and errors to practice the claimed invention.
10. 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.
11. 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.
12. Claims 1-21 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by U.S. Patent Application Publication 2017/0233459 (IDS filed on 11/05/2024).
U.S. Patent Application Publication 2017/0233459 teaches the following in paragraphs [00251]-[00252], [00255]-[0256], [00275] and Table 4.
“As set forth in Table 4 below, inactivated influenza virus Two Tc bovines (#2186 and #635) were immunized with a licensed 2012-2013 tri-valent seasonal influenza vaccine (Fluzone TIV - Sanofi-Pasteur containing A/California/07/2009 (H1N1), A/Victoria/361/2011 (H3N2), and B/Texas/6/2011 [B/Wisconsin/1/2010-like]) at total 1 mg of HA/dose formulated with SAB-adj-2. The Tc bovines were vaccinated 4 times (V1 - V4) at 3 week intervals.”
“Plasma collection and human immunoglobulin production. Prior to the first immunization (V1), plasma was collected from each Tc bovine as the negative control. Hyperimmune plasma (up to 2.1% of the body weight of each cow) was collected from immunized Tc bovines 10 days after each vaccination starting from the second immunization (V2) to the fifth immunization (V5). Plasma was collected using an automated plasmapheresis system (Baxter Healthcare, Autopheresis C Model 200). Plasma samples were stored frozen at - 80°C until purifications were performed. The frozen Tc plasma bags were thawed at room temperature (RT) overnight and equal volumes of plasma from each Tc bovine within a group at the selected time point were pooled. Samples were then pH adjusted to 4.80 with dropwise addition of 20% acetic acid, fractionated by caprylic acid at a caprylic acid/total protein ratio of 1.0 for 30 minutes at RT, and then clarified by centrifugation at 10,000 x g for 20 minutes at RT. The supernatant containing IgG was then neutralized to pH 7.50, filtered by a 0.22 pm filter, and affinity purified by an anti-human IgG light chain specific column, KappaSelect (GE Healthcare Life Sciences). Residual bovine IgG in the KappaSelect-purified IgG sample was then removed by passing through an anti-bovine IgG heavy chain specific affinity column, Capto HC15 (GE Healthcare Life Sciences). The Capto HC15 column flow thru that contains fully human IgG was then formulated by a Millipore Labscale tangential flow filtration (TFF) System. The final purified fully human IgG was in a buffer at a pH of 5.5 consisting of 10 mM of glutamic acid monosodium salt, 262 mM of d-sorbitol, and 0.05 mg/mL of Tween 80. The purified hIgG was sterile-filtered with 0.22 pm filter. Analysis of purified IgG product by HPLC size exclusion chromatography indicated that there were no IgG aggregates or IgG dimers (not shown).”
“All mice were housed under specific pathogen-free conditions and all
experiments were conducted at ABSL-3 in accordance with AAALAC-approved institutional guidelines for animal care and used approved by the University of Pittsburgh IACUC committee.”
“Protection conferred by transchromosomic polyclonal antibody (TcpAb). Six- week-old Balb/c mice (Charles River Laboratories) received 100 pg TcpAbs intraperitoneally or 100 pg intraperitoneally and 100 pg intranasally either prophylactically or therapeutically as described in figure legends. Mice were challenged either subcutaneously with 1000 PFU of V3000-derived virus in the rear footpad or via aerosol with either 50-100 LD50 or >100 LD50 of V3000 nluc TAV virus. For the co-infection aerosol exposure, six week old DBA2 (Charles River) mice were exposed to a lethal dose of V3000 and A/California/07/2009 (H1N1) and treated intraperitoneally with the combined anti-VEEV/anti-Flu TcpAb preparation either prophylactically or therapeutically as described in the figure legend. All mice were weighed daily and monitored for clinical signs of disease, which was increased to twice daily upon onset of clinical signs of disease.”
“A significant advantage in protection from a bioweapons/bioterrorism attack
would be the ability to treat infections with multiple pathogens, either before the time that an infecting organism is identified or in the case of a multi-organism release. Therefore, development of a multi-agent specific antiviral therapeutic is of high priority. To test the potential use of the TcpAb preparations in this context, DBA2 influenza-sensitive mice were treated either prophylactically or therapeutically with an equal mixture of VEEV TcpAbs (V3000 nt3A AMT TcpAbs) and influenza TcpAbs or given negative control TcpAbs then exposed to a lethal aerosol dose of VEEV and H1N1 influenza combination. As a baseline measure of disease manifestation, negative control-treated mice were also exposed to each virus individually. In control TcpAb- treated animals, the combination of the two viruses significantly (p<0.001) lowered the AST versus individual infections (Fig 21) suggesting an increase in disease severity with co-infection. As an additional control, co-infected mice were treated with the individual TcpAbs (VEEV TcpAb or influenza TcpAb) and all succumbed to infection (DNS), further demonstrating that the co-infected mice received a lethal dose of both viruses. In contrast,( co- infected mice treated either prophylactically 67% survival; p=0.0013) or( therapeutically 78% survival; p=0.0004) with the two TcpAbs exhibited significantly higher survival compared to mice who were given the( negative control TcpAbs 0%) (Fig 21). These data suggest the TcpAb platform can be useful in the treatment of infections with multiple co-infecting pathogens.”
Claims 3 and 15 are included in this rejection because Fluzone TIV comprises full length HA1 and HA2 proteins in the inactivated viruses in the vaccine.
Claims 4-7, 10-12 and 16-17 are included in this rejection because the antibodies were produced using the same methods of the instant specification. Since the office does not have a laboratory to test the reference antibodies, it is applicant's burden to show that the reference antibodies do not have the characteristics recited in claims 4-7, 10-12 and 16-17. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
Claims 8-9 are included in this rejection because the claims produced in U.S. Patent Application Publication 2017/0233459 do not produce any chimeric antibodies.
The reference teachings anticipate the claimed invention.
13. Claims 1-2, 4-12 and 20-21 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by the SAB BIO reference (Reference 1 on the IDS filed on 02/18/2026).
SAB BIO teaches the AB-176 multivalent, broadly neutralizing fully-human polyclonal antibody therapeutic candidate in development for the treatment, or prevention, of severe influenza. The novel, specifically-targeted therapeutic leverages the natural human biological immune response to specifically bind to Type A and Type B influenza viruses. It can also be modified to address annual strain changes when needed. Preclinical data suggests that SAB-176 offers broad protection against diverse influenza strains. (In particular, page 2, first paragraph, whole document).
Since the office does not have a laboratory to test the reference antibodies, it is applicant's burden to show that the reference antibodies do not have the characteristics recited in claims 4-7 and 10-12. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
Claims 8-9 are included in this rejection because the reference teaches that AB-176 antibodies are fully-human
The reference teachings anticipate the claimed invention.
14. Claims 1-21 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by the SAB BIO reference (Reference 11 on the IDS filed on 11/05/2024).
SAB BIO teaches SAB-176 is a multivalent, broadly neutralizing fully-human polyclonal antibody therapeutic candidate in development for the treatment or prevention of severe influenza. The novel, specifically-targeted therapeutic leverages the natural human biological immune response to specifically bind 10 Type A and Type B influenza viruses. Like vaccines, it can be modified to address annual strain changes, when needed, to SAB's novel DiversitAb™ immunotherapy platform enables the production of large amounts of targeted, highly potent human polyclonal antibodies. The platform leverages transchromosomic cattle (Tc Bovine that have been genetically designed to generate fully human antibodies (immunoglobulin G) rather than bovine antibodies, in response to inoculation with an Immunogen. To develop and produce SAB-176. To Bovine were hyperimmunized with a quadrivalent antigen, including a number of influenza strains. Within a brief period of time, the Tc Bovine generated significant amounts of fully-human antibodies to combat the virus, driving titers beyond the levels known to be protective. Plasma was collected (in a similar manner as from human plasma donors), then purified to isolate the antibodies that comprise the therapeutic treatment (In particular, pages 3-4, whole document).
The Phase 2a challenge study, initiated in June 2021, was a randomized, double-blind, placebo-controlled study evaluating the safety and treatment efficacy of SAB-176 in 60 healthy adults challenged with a pandemic influenza virus strain (pH1N1). Participants were randomized to receive either SAB-176 (25 mg/kg dose) or placebo and were intranasally inoculated with pandemic H1N1 (2009/California) virus, and nasopharyngeal swabs were taken 8 days after inoculation timepoint as measured by qRT-PCR. SAB-176 met the primary endpoint of significantly reducing patient pH1N1 influenza viral load in the treated subjects (p = 0.026, one sided). A secondary endpoint of the challenge study was reduction of clinical flu signs and symptoms in the subjects receiving active treatment (n=8) compared to placebo controls (n=12) for those who had signs and symptoms. SAB-176 achieved statistical significance in meeting the secondary endpoint at Day 4 (p = 0.013, one sided) in symptomatic patients. Additional analyses of secondary endpoint data are underway. In this study SAB-176 also appeared to be safe and well tolerated. No SAB-176-related serious adverse events (SAEs) were observed, and most adverse events were mild to moderate. Based on these positive efficacy and safety results, SAB plans to further evaluate SAB-176 in advanced clinical trials. "One remarkable aspect of these results is that SAB's To Bovine TM were not immunized to the specific influenza virus strain that was used in the challenge study," added Christoph Bausch, PhD, Chief Scientific Officer of SAB Biotherapeutics. "Nonetheless, the statistically significant reduction in virus load and symptoms that were achieved confirm that SAB-176 demonstrated high cross reactivity to this pandemic strain. This reinforces a unique and timely feature of our DiversitAb TM platform-the diversity of the human antibodies it produces gives our therapeutics the potential to be broadly neutralizing to both known and unknown viral variants-a very valuable feature when addressing rapidly mutating pathogens." (In particular, pages 2-3, whole document).
Claims 3 and 15 are included in this rejection because the reference teaches inoculating with quadrivalent antigen, including a number of influenza strains.
Claims 4-7, 10-12 and 16-17 are included in this rejection because the antibodies were produced using the same methods of the instant specification. Since the office does not have a laboratory to test the reference antibodies, it is applicant's burden to show that the reference antibodies do not have the characteristics recited in claims 4-7, 10-12 and 16-17. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
Claims 8-9 are included in this rejection because the reference teaches that AB-176 antibodies are fully-human
The reference teachings anticipate the claimed invention.
15. No claim is allowed.
16. Any inquiry concerning this communication or earlier communications from the examiner should be directed to NORA MAUREEN ROONEY whose telephone number is (571)272-9937. The examiner can normally be reached on M-F from 8:00am to 4:30pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner' s supervisor, Misook Yu, can be reached at telephone number (571) 272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of an application may be obtained from Patent Center. Status information for published applications may be obtained from Patent Center. Status information for unpublished applications is available through Patent Center for authorized users only. Should you have questions about access to Patent Center, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
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) Form at https://www.uspto.gov/patents/uspto-automated- interview-request-air-form.
June 27, 2026
/Nora M Rooney/
Primary Examiner, Art Unit 1641
Prosecution Insights