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 .
DETAILED ACTION
Election/Restrictions
Applicant’s election without traverse of species in the reply filed on 05/22/2026 is acknowledged.
Applicant elects the following:
Claim 1: Applicant elects to prosecute (a) from claim 1. Applicant elects to prosecute an antibody from Table 2, i.e., antibody Beta-27 comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 having the amino acid sequences set forth in SEQ ID NOs: 485-490, respectively. Claims 1-3, 8, 11-14, 17-19, 22-24, 29, and 31-34 read on this species.
Claim 2: Applicant elects to prosecute (a) from claim 2. Applicant elects to prosecute antibody Beta-27 comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 having the amino acid sequences set forth in SEQ ID NOs: 485-490, respectively. Claims 1-3, 8, 11-14, 17-19, 22-24, 29, and 31-34 read on this species.
Claim 3: Applicant elects to prosecute (a) in claim 3. Claims 1-3, 8, 11-14, 17-19, 22-24, 29, and 31-34 read on this species.
Claim 8: Applicant elects to prosecute antibody Beta-27 comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 having the amino acid sequences set forth in SEQ ID NOs: 485-490, respectively. Claims 1-3, 8, 11-14, 17-19, 22-24, 29, and 31-34 read on this species.
Claim 14: Applicant elects to prosecute Antibody 269 from Table 1 comprising a CDRH1, CDRH2, CDRH3, CDRL1, CDRL2, and CDRL3 having the amino acid sequences set forth in SEQ ID NOs: 275-280, respectively. Claims 1-3, 8, 11-14, 17-19, 22-24, 29, and 31-34 read on this species.
Claim 29: Applicant elects to prosecute the substitute position 417. Claims 1-3, 8, 11-14, 17-19, 22- 24, 29, and 31-34 read on this species.
Examiner Notes with respect to claims that read on the elected species:
Claims 13, 33, and 34 withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 05/22/2026.
Claim 13 recites “A combination of antibodies comprising two or more antibodies according to claim 1”. However, the election was only for one antibody, e.g. Beta-27. As a result, this claim is withdrawn from consideration.
Claim 33 recites a method of generating an antibody capable of binding to the spike protein of SARS-CoV-2, comprising raising an antibody against a modified spike protein. This claim reads on an unelected embodiment from claim 1 (c). Claim 34 is dependent on claim 33.
Additionally, based on the specification, claims 33 and 34 appear to read on the unelected antibodies, Beta-49 and Beta-50 and there does not appear to be overlap in with Beta-27.
The specification discloses, “the inventors identified that the potent cross-lineage neutralizing antibodies Beta-49 and Beta-50 bind to a conformation of the spike protein that has not been previously observed, and this conformation is referred to herein as the "down and out" conformation. The "down and out conformation" is similar to the conventional down (receptor inaccessible) conformation except that there are no direct contacts between the receptor binding domains (RBDs) in the spike protein trimer, except for contact with the N-glycosylation site at amino acid position 343 relative to the spike protein of the hCoV- 19/Wuhan/WIV04/2019 strain. The epitope bound by Beta-49 and Beta-50 extends across two subunits of the spike protein trimer and enables the antibodies to lock the trimer in the 'down and out conformation', which is receptor inaccessible. The epitope bound by Beta- 49 and Beta-50 is well conserved across the various lineages of SARS-CoV-2. Although mutations have been observed in the epitope bound by antibodies Beta-49 and Beta-50 in particular SARS-CoV-2 variants, these mutations surprisingly do not affect the neutralizing properties of antibodies Beta-49 and Beta-50. Accordingly, antibodies that bind to the same epitope as Beta-49 and Beta-50 are expected to have broad cross-lineage neutralizing properties (p. 4)…“The antibodies of the IgVH1-69 class, Beta-49 and Beta-50, bind to a previously unidentified conformation of the spike protein (see Example 18), in which the RBDs are in a down configuration (Figure 15), with the heavy chain making interactions with two
RBDs (Figure 16C), causing the RBD of the spike protein to be translated/rotated towards
the periphery of a spike trimer (an 'out' configuration)(Figure 16D)”(p. 53)…. Antibodies Beta-49 and Beta-50 are thought to 'lock' the spike protein into a 'down and out' conformation, a new type of receptor inaccessible state. Surprisingly, the antibodies that bind to the down and out conformation of the spike protein strongly neutralise all of the SARS-CoV-2 variants tested to date. Antibodies that bind to the down and out conformation of the spike protein may therefore be useful as cross-lineage potently neutralising antibodies of SARS-CoV-2 variants (p. 53)… A spike protein locked into the down and out conformation may be used to generate
antibodies targeting the same epitope as antibodies Beta-49 and Beta-50 (p. 55).
As a result, claims 33 and 34 (dependent on claim 33) are withdrawn from consideration.
Claims 1-3, 8, 11-12, 14, 17-19, 22-24, 29, 31-32 are under consideration.
Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/20/2023, 05/22/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawings
The drawings are objected to because the drawings are indicated by “Figure” rather than “FIG.” as required by 37 C.F.R § 1.84 (u)(1) (see also MPEP § 608.02 (V)). The different views must be numbered in consecutive Arabic numerals, starting with 1, independent of the numbering of the sheets and, if possible, in the order in which they appear on the drawing sheet(s). Partial views intended to form one complete view, on one or several sheets, must be identified by the same number followed by a capital letter. View numbers must be preceded by the abbreviation “FIG.” Where only a single view is used in an application to illustrate the claimed invention, it must not be numbered and the abbreviation “FIG.” must not appear.
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.
Based on text in the specification, “Brief Description of the figures”, it appears that color drawings were submitted. For example, in the description for Figures 4-7, 10, 14-16, 19-21, 23 (p. 7), the “colouring scheme” (Figure 4 description) or different color distinctions are mentioned (p. 7-11).
Color photographs and color drawings are not accepted in utility applications unless a petition filed under 37 CFR 1.84(a)(2) is granted. Any such petition must be accompanied by the appropriate fee set forth in 37 CFR 1.17(h), one set of color drawings or color photographs, as appropriate, if submitted via the USPTO patent electronic filing system or three sets of color drawings or color photographs, as appropriate, if not submitted via the via USPTO patent electronic filing system, and, unless already present, an amendment to include the following language as the first paragraph of the brief description of the drawings section of the specification:
The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.
Color photographs will be accepted if the conditions for accepting color drawings and black and white photographs have been satisfied. See 37 CFR 1.84(b)(2).
Specification
The disclosure is objected to because of the following informalities:
The drawings are indicated by “Figure” rather than “FIG.” See objection to the drawings, above.
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code on pages 77, 99, and 101. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Appropriate correction is required.
Claim Objections
Claims 11, 22-23, 29, 31-32 are objected to because of the following informalities:
Claim 11: Change “a IgG1 constant region” to “an IgG1 constant region”.
Claim 22: Remove the comma after according to claim 1. For example, “antibody according to claim 1 to said subject”.
Claims 29, 31, 32: For increased clarity, change “spike protein relative to the spike protein of the hCoV-19/Wuhan/WIV04/2019 strain” to “spike protein relative to the spike protein (SEQ ID NO: 681)”.
Claim 23: For increased clarity, change “therewith” to “ with a SARS-CoV-2 infection”. For example, “or a disease or complication associated with a SARS-CoV-2 infection”.
Claim 31: Change “substitution” to “substitutions”.
Claim 32: Change “substitution” to “substitutions”.
Appropriate correction is required.
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, 8, 11-12, 14, 17-19, 22-24, 29, 31-32 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.
See claims 1-3, 8, 11-12, 14, 17-19, 22-24, 29, 31-32 as submitted 05/22/2026.
Claim 1 recites an antibody capable of binding to the spike protein of coronavirus SARS-CoV-2, wherein [as elected] (a) the antibody comprises at least three CDRs of antibody Beta-27.
Claim 2 recites the antibody of claim 1, comprising [as elected] (a) at least four, five or all six CDRs of antibody Beta-27.
Claim 3 recites the antibody of claim 1, wherein the antibody is selected from the group consisting of (a), which also reads on the election of Beta-27.
Claim 8 recites the antibody of claim 1, wherein the antibody is [as elected] Beta-27.
Claims 11-12, 14, 17-19, 22-24, 29, 31-32 are dependent on claim 1.
Claim 14 also recites (b) an antibody comprising at least three CDRs of antibody 269.
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 requirement 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.
According to the specification, Beta-27 was found to neutralize the Omicron variant of SARS-CoV-2 (Table 15, Figure 22)(p. 14). The sequences of the CDRs for Beta-27, while not included in the claims, are provided in the Specification as CDRH1, CDRH2 and
CDRH3 having the amino acid sequences specified in SEQ ID NOs: 485, 486 and 487,
respectively, and a CDRL1, CDRL2 and CDRL3 having the amino acid sequences specified in SEQ ID NOs: 488, 489 and 490, respectively.
The state of the prior art is such that it is well established in the art that the formation of an intact antigen-binding site of antibodies generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs or hypervariable regions, which provide the majority of the contact residues for the binding of the antibody to its target epitope (Paul et al.)(Paul)(See PTO-892 Notice of References Cited). 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. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (Paul, p. 293).
Additionally, Bendig et al. (Bendig)(See PTO-892 Notice of References Cited) teaches that the general strategy for “humanizing” antibodies involves the substitution of all six CDRs from a rodent antibody that binds an antigen of interest, and that all six CDRs are involved in antigen binding (see entire document, but especially Figures 1-3). It is noted that Bendig used Kabat CDRs in their humanization process (p. 86). Similarly, the skilled artisan recognizes a “chimeric” antibody to be an antibody in which both the heavy chain variable region (which comprises the three heavy chain CDRs) and the light chain variable region (which comprises the three light chain CDRs) of a rodent antibody are recombined with constant region sequences from a human antibody of a desired isotype (see entire document, but especially Figures 1-3.
Thus, the state of the art recognized that it would be highly unpredictable that a specific antibody comprising less than all six parental CDRs would have antigen binding function. The minimal structure which the skilled artisan would consider predictive of the function of binding the antigen of a murine or humanized antibody includes six CDRs (three from the heavy chain variable region and three from the light chain variable region) in the context of framework sequences which maintain their correct spatial orientation and have the requisite binding function. One of skill in the art would neither expect nor predict the appropriate functioning of the antibody fragments and mutated antibodies of the instant claims as broadly as claimed.
Instant claims 1 and 14 recite only three CDRs for Beta-27 and also in the case of claim 14’s antibody 269. Instant claim 2 recites “at least four, five or six CDRs of antibody Beta 27”. Four or five CDRs would be insufficient. Six CDRs, however, is more likely to suggest binding function.
In the case of antibodies, it is especially important to disclose which residues are permissive to mutation. Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al. (Rudikoff)(See PTO-892 Notice of References Cited). Rudikoff teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function.
For the reasons above, the application has not provided sufficient written description support for an antibody capable of binding to the spike protein of coronavirus SARS-CoV-2 with only 3, 4, or 5 CDRs.
Claim 22 is 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 treating infection or a disease or complication from SARS-COV-2 and some of its variants, does not reasonably provide enablement for preventing any coronavirus infection, or a disease or complication associated with coronavirus infection, in a subject, comprising administering a therapeutically effective amount of the antibody, as elected Beta-27, to said subject.
The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
There are many factors to be considered when determining whether there is sufficient evidence to support a determination that a disclosure does not satisfy the enablement requirement and whether any necessary experimentation is “undue.” These factors 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;
(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.
In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
Here, the instant claims are broadly drawn to a method of treating or preventing a coronavirus infection, or a disease or complication associated with a coronavirus infection in a subject, comprising administering a therapeutically effective amount of the antibody, e.g. Beta-27, to said subject. The specification defines subject as human (p.72-73) and non-human animals such as rats, rabbits, sheep, pigs, cows, cats, or dogs (p. 73).
“Preventing” reads upon complete prevention or prophylaxis.
The level of skill in the art is high and would include, e.g., Ph.D. level scientists and physicians.
The state of the art before the effective filing date is exemplified by the following references. Marovich et al. (Marovich)(July 2020)(See PTO-892 Notice of References Cited) teaches “SARS-CoV-2 monoclonal antibodies have the potential to be used for both prevention and treatment of infection. Benefits have been demonstrated in animal models for both SARS-CoV and MERS-CoV monoclonal antibodies. Most people recovering from SARS-CoV-2 infection will generate a cellular and humoral immune response against SARS-CoV-2. Given the lack of effective therapies for patients with advanced COVID-19, several groups have collected convalescent plasma and measured SARS-CoV-2 neutralization titers. In the largest study to date, Joyner et al…administered 1 to 2 units of convalescent plasma to 5000 patients with severe or life-threatening SARS-CoV-2 infection. The investigators reported an incidence of less than 1% for severe adverse events and a 7-day mortality rate of 14.9%, which is consistent with the natural history of severe infection” (p. 131). Marovich also teaches the “limitations of convalescent plasma include the difficulty in collection, variability of binding and neutralizing antibody titers, potential contamination with infectious agents, risk of transfusion reactions, and circulatory overload associated with administration. However, success in convalescent plasma research serves to inspire development and deployment of monoclonal antibodies”(p. 131). With respect to monoclonal antibodies, Marovich teaches “Even though more than 75 monoclonal antibodies have been licensed for use by the US Food and Drug Administration, only 3 are used to treat or prevent infectious diseases—respiratory syncytial virus, anthrax, and Clostridioides difficile” (p. 131). Marovich further teaches “[s]everal SARS-CoV-2 monoclonal antibodies are poised to enter clinical trials during the summer of 2020. Therapeutic trials will include treatment of patients with SARS-CoV-2 infection, with varying degrees of illness, to block disease progression. Given the long half-life of most monoclonal antibodies (approximately 3 weeks for IgG1), a single infusion should be sufficient…A potential limitation of monoclonal antibodies for treatment of COVID-19 is the unknown bioavailability of passively infused IgG in tissues affected by the disease, especially the lungs, which serve as a key target of SARS-CoV-2 infection. Another consideration is the effect of viral diversity, so it will be important to monitor for the emergence of resistant viral mutations under selective pressure of monoclonal antibody treatment. Accordingly, monoclonal antibodies have been chosen to target conserved regions of the viral spike and some products will include of a combination of 2 monoclonal antibodies targeting different sites on the spike protein” (p. 131-132). With respect to monoclonals as vaccines, Marovich teaches “Monoclonal antibodies provide an alternative avenue for the prevention of COVID-19. Passive infusion of monoclonal antibodies as preexposure or postexposure prophylaxis might offer immediate protection from infection that could last weeks or months. Newer technologies that modify the Fc region of the antibody to extend the half-life of monoclonal antibodies can provide potentially protective levels for months, depending on the monoclonal antibody concentrations required” (p. 132). Finally, Marovich teaches “There are substantial challenges to demonstrating the benefits of monoclonal antibodies in clinical trials. Because most people with early infection recover, the clinical end points needed to demonstrate a benefit relative to placebo are not easily achieved. Likewise, it may be difficult to demonstrate benefit in patients with more severe disease, in whom inflammation and coagulopathy may be more important than viral replication. For monoclonal antibody prevention trials, the difficulty is finding individuals at sufficient risk (i.e, a high enough attack rate) to demonstrate prevention of symptomatic infection. As the COVID-19 pandemic evolves across the US and the world, the clinical research infrastructure will require the flexibility to provide monoclonal antibodies on short order to populations or facilities at high risk of infection. Another potential challenge is the ability to produce enough monoclonal antibody product. Although this will be influenced by the dose required and may differ for prevention and treatment, current commercial manufacturing capacity can likely produce millions of doses annually. There is also some concern for immune enhancement of COVID-19 because vaccine-associated enhanced disease has been observed in animal models of SARS-CoV and for other animal coronaviruses. Categories of possible disease enhancement include antibody-mediated enhancement of viral entry and replication in target cells (Fc-bearing monocytes or macrophages) and virus-antibody immune complexes and the associated cytokine release. For the former, antibody-mediated enhancement is classically defined as Fcγ-receptor–mediated enhanced disease in the presence of subneutralizing concentrations of antibodies or nonneutralizing antibodies” (p. 132).
Tuccori et al. (Tuccori)(December 2020)(See PTO-892 Notice of References Cited) teaches “numerous mAbs with potential neutralizing activity against SARS-CoV-2 have been discovered, but only a few of them are being currently tested in clinical trials (p. e1854149-2). Tuccori also teaches “Efficacy against mutant viral strains is also a relevant issue. The SARS-CoV-2 spike protein mutated after few months of viral circulation…with one mutation outside the receptor-binding motif (23403A >G single nucleotide polymorphism, corresponding to D614G amino acid change), currently defining a dominant clade…characterized by reduced S1 shedding and increased infectivity…Although particular mutation increases the susceptibility to neutralization…only a few of these candidate drugs have been tested for their capability of neutralizing different strains of SARS-CoV-2. Antibody cocktails theoretically reduce the ability of mutant viruses to escape treatment and protect against spike variants that have already arisen in the human population (p. e1854149-6). Tuccori further teaches “While numerous Phase 3 trials are still pending, mAb therapy has the requisites to make a difference in the management of COVID-19. Nevertheless, even if their efficacy will be proven and their safety will be acceptable, sufficient quantities may not be available to meet the expected large request, their price could make these drugs unaffordable for healthcare systems. Therefore, it will be a priority to identify those patients who could receive the highest benefit from these mAbs, thus maximizing the appropriate use of resources” (p. e1854149-6).
Jaworski et al. (Jaworski)(Feb 2021/online November 2020)(See PTO-892 Notice of References Cited) teaches “MAbs are currently established as targeted therapies for malignancies, transplant rejection, autoimmune and infectious diseases. Among the advantages of MAbs over conventional drugs are their high specificities, their long half-lives and their good risk benefit ratio; moreover, regulatory approval rates for MAbs are about 20% compared with 5% for new chemical entities....However, intravenous administration of MAbs carries the risk of immune reactions such as acute anaphylaxis, serum sickness and the generation of anti-drug anti bodies. In addition, there are numerous adverse effects of MAbs that are related to their specific targets, including the development of infections and cancer, autoimmune disease, and organ-specific adverse events such as cardiotoxicity…However, most of these adverse effects are related to the immunomodulatory effect of MAbs targeting different endogenous immune mediators (i.e., immune system check points, cytokine and cytokine receptors, etc.) and are expected to be absent for MAbs targeting exogenous viral epitopes. As mentioned earlier, recent technical advances have allowed the transition from mouse, via chimeric and humanized, to fully human MAbs, with a reduction in potentially immunogenic mouse components. In addition, molecular engineering has enabled the fine-tuning of MAb function to enhance their effects and to minimize immunogenicity and side effects”(p. 12). Jaworski also notes the challenges with increasing the scale of production as noted above by other researchers (p. 12). Jaworski concludes their article with “Although several vaccine candidates and repurposed drugs are currently being evaluated for safety and efficacy in record time, none of them have been approved for COVID-19 use” (p. 13).
The specification only exemplifies and reduces to practice the following examples. The examples relate to SARS-CoV-2 and its variants known in the art. The examples do not include other non-SARS-CoV-2 coronaviruses, like SARS or MERS.
In Figure 1G, Beta-27, while not the most “potent”, shows the ability, albeit low in comparison with other antibodies in the invention, to block ACE2 binding to the Beta variant spike protein.
In Figure 2, A. Beta-27 shows full cross-reactivity with other strains and 100% neutralization at higher concentrations.
In Figure 3, using a transgenic mouse model, mice were inoculated with 103 FFU of Beta and at 24 h post-inoculation, were administered a single 10mg/kg dose of Beta-27 mAb via i.p. injection and this prevented weight loss over the 6 days following inoculation and reduced viral loads in the lung and brain but not in nasal washes. These results demonstrate that Beta-27 can reduce the severity of infection and prevent systemic disease but do not prevent viral infection in the upper respiratory tract (Figure 3C-F, p. 82).
In view of the foregoing, an undue amount of experimentation, including extensive animal and human clinical trials, would be required to use the invention based on the content of the disclosure.
Taken together, the Specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with the claims.
Enablement – Deposit
Claims 1-3, 8, 11-12, 14, 17-19, 22-24, 29, 31, 32 are rejected under 35 U.S.C. § 112 (pre-AIA ), first paragraph or 35 U.S.C. 112(a), because the specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention, because the specification does not provide evidence that the claimed biological materials are (1) known and readily available to the public; (2) reproducible from the written description.
It is unclear if a cell line which produces an antibody having the exact chemical identity of antibody Beta-27 is known and publicly available, or can be reproducibly isolated without undue experimentation. Therefore, a suitable deposit for patent purposes is suggested. Without a publicly available deposit of the above cell line, one of ordinary skill in the art could not be assured of the ability to practice the invention as claimed. Exact replication of: (1) the claimed cell line; (2) a cell line which produces the chemically and functionally distinct antibody claimed; and/or (3) the claimed antibody's amino acid or nucleic acid sequence is an unpredictable event.
If the deposit is made under the provisions of the Budapest Treaty, filing of an affidavit or declaration by applicant or assignees or a statement by an attorney of record who has authority and control over the conditions of deposit over his or her signature and registration number stating that the deposit has been accepted by an International Depository Authority under the provisions of the Budapest Treaty and that all restrictions upon public access to the deposited material will be irrevocably removed upon the grant of a patent on this application. This requirement is necessary when deposits are made under the provisions of the Budapest Treaty as the Treaty leaves this specific matter to the discretion of each State.
If the deposit is not made under the provisions of the Budapest Treaty, then in order to certify that the deposits comply with the criteria set forth in 37 CFR 1.801-1.809 regarding availability and permanency of deposits, assurance of compliance is required. Such assurance may be in the form of an affidavit or declaration by applicants or assignees or in the form of a statement by an attorney of record who has the authority and control over the conditions of deposit over his or her signature and registration number averring:
(a) during the pendency of this application, access to the deposits will be afforded to the Commissioner upon request:
(b) all restrictions upon the availability to the public of the deposited biological material will be irrevocably removed upon the granting of a patent on this application:
(c) the deposits will be maintained in a public depository for a period of at least thirty years from the date of deposit or for the enforceable life of the patent of or for a period of five years after the date of the most recent request for the furnishing of a sample of the deposited biological material, whichever is longest; and
(d) the deposits will be replaced if they should become nonviable or non-replicable.
In the instant case, the specification fails to state that a hybridoma that produces the antibody Beta-27 was deposited. Further, it is not clear that a deposit was made under the terms of the Budapest Treaty, nor is there available a viability statement, i.e. one certifying that the deposit was viable at the time of the deposit or a certificate verifying such from the depository.
Amendment of the specification to recite the date of deposit and the complete name and address of the depository is required. As an additional means for completing the record, applicant may submit a copy of the contract with the depository for deposit and maintenance of each deposit.
If a deposit is made after the effective filing date of the application for patent in the United States, a verified statement is required from a person in a position to corroborate that the biological material described in the specification as filed is the same as that deposited in the depository, stating that the deposited material is identical to the biological material described in the specification and was in the applicant's possession at the time the application was filed.
Applicant's attention is directed to In re Lundak, 773 F.2d. 1216, 227 USPQ 90 (CAFC 1985) and 37 CFR 1.801-1.809 for further information concerning deposit practice.
Claim Rejections - 35 USC § 101
Section 33(a) of the America Invents Act reads as follows:
Notwithstanding any other provision of law, no patent may issue on a claim directed to or encompassing a human organism.
Claim 17 is rejected under 35 U.S.C. 101 and section 33(a) of the America Invents Act as being directed to or encompassing a human organism. See also Animals - Patentability, 1077 Off. Gaz. Pat. Office 24 (April 21, 1987) (indicating that human organisms are excluded from the scope of patentable subject matter under 35 U.S.C. 101).
See claim 17 as submitted 05/22/2026.
Claim 17 recites “a host cell comprising said vectors”. The terminology “a host cell” reads on a cell that could be within a human organism in which the vector delivers genetic material into the cells by various means.
To overcome this rejection, change “a host cell” to an “isolated host cell”.
Conclusion
SEQ ID NO: 485, SEQ ID NO: 277, SEQ ID NO: 280 are free of the prior art of record.
No claims allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Claire Cornelius whose telephone number is (571) 272-0860. The examiner can normally be reached M-F, 0930-1700.
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/C.C./Examiner, Art Unit 1672
/M FRANCO G SALVOZA/Primary Examiner, Art Unit 1672
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