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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 3/12/2026 has been entered.
Claim Status
Applicant’s reply filed on 03/12/2026 is acknowledged. Claims 1, 12, 14, 22, 30, 32, 36, 41, 45, and 46 have been amended. Claims 5 and 28 are cancelled.
In the reply filed 05/19/2025, applicant has elected examination of A multivalent binding agent comprising a VH CDR1 comprising the amino acid sequence of SEQ ID NO: 18, a VH CDR2 comprising the amino acid sequence of SEQ ID NO: 19, a VH CDR3 comprising the amino acid sequence of SEQ ID NO: 20, a VL CDR1 comprising the amino acid sequence of SEQ ID NO: 22, a VL CDR2 comprising the amino acid sequence of SEQ ID NO: 23, and a VL CDR3 comprising the amino acid sequence of SEQ ID NO: 24; optionally wherein the binding region comprises a heavy chain variable domain comprising the amino acid sequence of SEQ ID NO: 17 and a light chain variable domain comprising the amino acid sequence of SEQ ID NO: 21.
Claims 1, 8, 10, 12, 14, 22-23, 25-26, 30, 32, 34, 36-38, 41, and 45-46 are pending and under consideration.
Rejections Withdrawn
The following rejections are withdrawn:
The rejection of claim 45 under 35 U.S.C. 102(a)(1) as being anticipated by Huijbers (Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20783-8., IDS filed 03/29/2022).
The rejection of claims 1, 5, 8, 10, 22-23, 25-26, 28, 30, 32, 37-38, 41, and 45-46 under 35 U.S.C. 103 as being unpatentable over Huijbers (Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20783-8., IDS filed 03/29/2022) as applied to claim 45, and further in view of Burden (US20150050289A1, published 02/19/2015, IDS filed 03/29/2022).
The rejection of claims 1, 5, 8, 10, 12, 14, 22-23, 25-26, 28, 30, 32, 34, 36-38, 41, and 45-46 under 35 U.S.C. 103 as being unpatentable over Huijbers (Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):20783-8, IDS filed 03/29/2022) and Burden (US20150050289A1, published 02/19/2015, IDS filed 03/29/2022) as applied to claims 1, 5, 8, 10, 22-23, 25-26, 28, 30, 32, 37-38, 41, and 45-46 and further in view of Labrijn (J Immunol. 2011 Sep 15;187(6):3238-46).
Rejections Maintained
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 8, 10, 45 remain rejected under 35 U.S.C. 101 because the claimed invention is directed to natural phenomena without significantly more.
Claims 1, , 8, 10, and are directed to natural phenomena because they recite a product of nature (Step 2A, prong one), the judicial exception is integrated into a practical application as part of a pharmaceutical composition (Step 2A, prong two), but the claims do not recite additional elements that amount to significantly more than the judicial exception (Step 2B; MPEP 2106.05). The natural phenomena are anti-MuSK antibodies naturally occurring in myasthenia gravis patients. The antibodies as claimed are not modified in any way from their natural state and providing them within a pharmaceutical composition is not sufficient to amount to significantly more than the judicial exception.
Claims 45 is directed to natural phenomena because it recites a product of nature (Step 2A, prong one) and the judicial exception is not integrated into a practical application (Step 2A, prong two). The natural phenomena are anti-MuSK antibodies naturally occurring in MuSK myasthenia gravis patients. The antibodies as claimed are not modified in any way from their natural state and therefore the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception.
The specification teaches the disclosed antibodies were obtained by the following method: B cells were isolated from patients with MuSK myasthenia gravis. MuSK-specific cells were selected using recombinant MuSK-based binding assay. Isolated MuSK autoantibody producing cells were sequenced (Materials & Methods, Pg. 98). The variable region amino acid sequences for seven isolated clones are set forth in claim 19 (a)-(g), corresponding to clones 11- 3D9, 11-3F6, 11-8G4, 13-3B5, 13-3D10, 13-4D3 and 14-2E9, respectively (Specification Pgs. 88-93).
The additional element of the pharmaceutical composition comprising a therapeutically effective amount of the antibody is well-understood, routine and conventional limitation. Well-understood, routine and conventional limitations are not meaningful limitations and are not enough to qualify the claimed method as reciting something “significantly more” than the judicial exception(s) (see Part I.B.1 of the interim Guidance).
Response to Arguments
Applicant's arguments filed 03/12/2026 have been fully considered but they are not persuasive.
The applicant argues that a therapeutically effective amount of the claimed antibodies is not directed merely to a natural phenomenon, but instead to a human-engineered application that imposes meaningful limitations the claims are no longer directed to natural phenomenon.
In response, the incorporation of the naturally occurring antibodies into a pharmaceutical formulation is a well-understood, routine and conventional limitation. The additional limitation wherein the pharmaceutical composition comprises a therapeutically effective amount of the antibody does not provide any elements that make the claim as a whole amount to significantly more than the judicial exception because the antibodies retain the same structure as found in nature independent of the volume in which they are formulated. The specification teaches:
“Generally, the multivalent binding agents (e.g. binding proteins such as antibodies) are administered in a pharmaceutically effective amount. The amount of multivalent binding agent actually administered will typically be determined by a physician, in the light of the relevant circumstances, including the condition to be treated, the chosen route of administration, the actual compound administered, the age, weight, and response of the individual patient, the severity of the patient's symptoms, and the like.” (Pg. 76)
This limitation is therefore a well-understood, routine and conventional limitation as it relies on the knowledge of those practicing the method of administering the claimed pharmaceutical composition to determine what constitutes a “therapeutically effective amount” based on their knowledge of the art.
As an example of additional elements that amount to significantly more than the judicial exception, claim 14 introduces an IgG4 variant that transform the antibodies from the state they are found in nature.
Claim Rejections - 35 USC § 112(a)
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.
WRITTEN DESCRIPTION
Claims 12, 22-23, 25-26, 30, 32, 34, 36-38 remain 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.
MPEP § 2163 states that 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, 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. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention.
The teachings of the specification and the claimed invention
The invention of claims 22-23, 25-26, 28, 30, 32, 34, and 36-38 is directed to a method for inducing or increasing MuSK activity in a subject comprising administering to the subject a therapeutically effective amount of a bivalent, monospecific antibody comprising at least two binding regions that specifically bind to an Ig-1 like domain of a MuSK protein.
The claimed antibodies have the following required functional properties: (1) to bind specifically to an Ig-like 1 domain of a MuSK protein and (2) increase MuSk activity.
The specification discloses the inventors were in possession of 6 different clones isolated from human patients with VH and VL set forth in claims 1, 41, 45, 46. The specification provides evidence that the inventors have made recombinant anti-MuSK antibodies using the variable region sequences from isolated human autoantibodies 13-3B5 and 11-3F6 (see for example, Fig.1 and Fig. 7).
The state of the relevant art
Pertaining to IgG4 variants:
The disclosure of Labrijn teaches the mechanism of IgG Fab-arm exchange in human IgG4, the mechanism by which chains of IgG4 are exchanged to form bispecific antibodies (Abstract, Lines1-4). Labrijn identified the CH3 resides that mediate Fab-arm exchange (Pg. 3240, Results). Labrijn teaches particular mutations at amino acid positions 228, 409, and 405 disable Fab-arm exchange in IgG4 antibodies (see abstract; p. 3239 col. 1; and discussion); and rationale for implementing these mutations to prevent Fab-arm exchange in IgG4 antibody therapeutics (see bottom of col. 2 on p. 3238 to the top of col. 1 on p. 3239- “Thus, in time, bivalent IgG4 therapeutics convert into functionally monovalent IgG4 therapeutics, which could potentially affect both their initial binding strength and cross-linking behavior. This kind of unpredictability is an undesired trait for a therapeutic Ab, and eliminating the molecular features enabling Fab-arm exchange should be considered when designing therapeutic IgG4 Abs”).
Thus, the art teaches specific structures required for Fab-arm exchange and specific mutations required to disrupt Fab-arm exchange.
Pertaining to the principles of antibody binding:
It is well established in the art that the formation of an intact antigen-binding site in an antibody usually requires the association of the complete heavy and light chain variable regions of a given antibody, each of which comprises three CDRs (or hypervariable regions) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro et. al., Front. Immunol. 2018; 8:1751 (see Section “The IgG Molecule” in paragraph 1 and Figure 1). While affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody (page 3 “The IgG Molecule, second and third paragraphs), those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori. E.g., id., (page 6 ending paragraph onto page 7).
The prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is aptly noted that the art is characterized by a high level of unpredictability, since the skilled artisan still cannot accurately and reliably predict the consequences of amino acid substitutions, insertions, and deletions in the antigen-binding domains. For example, the unpredictability of single amino acid changes in an antibody is underscored by Winkler (J Immunol. 2000 Oct 15;165(8):4505-14) who teaches that a single amino acid change in a CDR can result in unpredictable and substantial changes in antibody specificity; see entire document (e.g., the abstract).
Antibody binding to the same antigen, or even the same epitope on that antigen, can be accomplished with an impressively wide variety of antibody structures, even when the antibodies are limited to those from a particular source (Gershoni et al., Epitope Mapping, Biodrugs 2007; 21 (3): 145-156, page 146 section 1.1). The skilled artisan therefore understood that antibodies from a variety of different sources may bind the same antigen and even mediate the same functional effects, but differ widely in the details of the structure of their antigen-binding sites, particularly in the amino acid sequence and length of VH-CDR3.
Further, it is not possible to predict the amino acid sequence when an epitope is recited, because there are many different epitope arrangements, such as linear and discontinuous epitopes that is dictated by the unique interaction between an antibody and its cognate epitope (Blythe et al., Benchmarking B cell epitope prediction: Underperformance of existing methods, Protein Science (2005), 14:246–248 pg. 246). 3D structural analyses of antibody-epitope binding highlighting that the deficiency in the ability to predict the structural features of an antibody when the epitope is disclosed (Schreiber et al.,3D-Epitope-Explorer (3DEX): Localization of Conformational Epitopes within Three-Dimensional Structures of Proteins, Wiley Interscience, 2005 42–44, 60596, page 879).
Claim analysis
In light of the guidance taught in the specification and the state of the relevant art, the claims have the following written description issues:
Claim 12 defines the IgG4 variant by intended result only. The claim does not provide any structure or modification to the native IgG4 that confers reduced ability or inability for Fab-arm exchange.
Claims 22-23, 25-26, 30, 32, 34, and 36-38 are directed to a method comprising administration of a binding agent that is defined by function only.
In light of the claim language that defines the antibody of the method only by function/epitope-binding, one of skill in the art would neither expect nor predict the appropriate functioning of the antigen binding molecules as claimed.
Given the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as claimed.
Response to Applicant’s Arguments
Applicant's arguments filed 03/12/2026 have been fully considered but they are not persuasive.
The applicant argues that the claims require a bivalent antibody that is monospecific, binding specifically to the lg-like I domain of MuSK, which are structural requirements that define and limit the scope of the claimed antibodies. The combination of these structural features-bivalent monospecificity for the lg-like I domain-is the identifying characteristic that distinguishes the claimed antibodies from other MuSK-binding antibodies and determines their function as MuSK agonists. (Remarks, Pg. 10)
In support of this argument, the applicant states: “The specification demonstrates this sequence-independence by showing that two different antibody clones (11-3F6 and 13-3B5), despite having different CDR sequences, both exhibited MuSK agonist activity when formatted as bivalent monospecific antibodies. This shows that the functional result (MuSK agonism) flows from the structural characteristic (bivalent monospecificity) rather than from any particular combination of CDR sequences.” (Remarks, Pg. 12)
In response, specificity for the Ig-like 1 domain does not impart structure or other physical and/or chemical properties and does not provide a correlation between function and structure. This requires defining the variable binding domains at minimum by disclosing the 6 CDR sequences. The examiner does not concede that two antibodies are sufficient to show possession of the method which encompasses the administration of every existing bivalent, monospecific antibody that specifically bind to an Ig-like 1 domain of a MuSK protein, both naturally-occurring and recombinant.
In a post-filing disclosure, Lim et al. (Sci Rep. 2023 May 8;13(1):7478) teaches the generation of antibodies specific to the Ig-like 1 domain derived from the parental antibodies of the instant disclosure. Lim et al. teaches variants of the 13-3B5 parental patient-isolated antibody had critically impaired agonistic potential, as shown by the inability of clone 13-3B5c to induce MuSK phosphorylation and AChR clustering (Pg. 5, MuSK agonist antibodies show varying agonistic potential on MuSK activation and AChR clustering in mouse myotube cultures and Fig. 1b,c).
Additionally, the Ig-like 1 domain comprises multiple binding epitopes, therefore the method is not even directed to antibodies with a single shared epitope, but rather to a collection of potential epitopes. Fig. 1a, of Lim et al. is a graphic depiction of the epitopes of the Ig-like 1 agonist antibodies.
For these reasons, a recitation of the general binding region is not sufficient description to support that the instant applicants were in possession of the invention as broadly claimed.
ENABLEMENT
Claims 22-23, 25-26, 30, 32, 34, 36-38, 41 and 46 remain rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains 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.
The factors to be considered in determining whether a disclosure would require undue experimentation include:
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, 8 USPQ2d, 1400 (CAFC 1988) and MPEP 2164.01.
The breadth of the claims and the nature of the invention
With respect to claim breadth, the standard under 35 U.S.C. §112, first paragraph, entails the determination of what the claims recite and what the claims mean as a whole. As such, the broadest reasonable interpretation of the claimed method is that any bivalent, monospecific antibody that specifically binds to an Ig-like 1 domain of a MuSK protein will induce or increase MuSK activity and can be used to treat any symptom, condition and/or disorder associated with impaired neuromuscular transmission.
The specification provides evidence that recombinant anti-MuSK antibody clones 13-3B5 and 11-3F6 induce MuSK phosphorylation and activation (see for example, Fig.1 and Fig. 7), but does not distill to practice a clinically relevant correlation between MuSK phosphorylation and treatment of a subject.
The state of the relevant art
The state of the prior art indicates there is no consensus as to the divergent effects of divalent and monovalent anti-MuSK antibodies on the MuSK signaling pathway. As an example, Mori et al. (J Neuroimmunol. 2012 Mar;244(1-2):1-7, IDS filed 03/29/2022) teach that both divalent and monovalent MuSK antibodies interfere with the MuSK signaling pathway and inhibit AChR clustering (Pg. 2, Left column, Lines 2-6, Fig. 2). Mori et al. also teach that their data suggest that divalent IgG4 antibodies activate MuSK while monovalent antibodies block MuSK activation and inhibit signaling in the neuromuscular junction (Pg. 4, Left column, Lines 4-8).
In a post-filing disclosure, Lim et al. (Sci Rep. 2023 May 8;13(1):7478) teaches the generation of antibodies specific to the Ig-like 1 domain derived from the parental antibodies of the instant disclosure. Lim et al. teaches variants of the 13-3B5 parental patient-isolated antibody had critically impaired agonistic potential, as shown by the inability of clone 13-3B5c to induce MuSK phosphorylation and AChR clustering (Pg. 5, MuSK agonist antibodies show varying agonistic potential on MuSK activation and AChR clustering in mouse myotube cultures and Fig. 1b,c).
Very importantly, Lim specifically teaches MuSK Ig‑like 1 domain agonist antibodies do not improve MuSK myasthenia gravis in vivo (emphasis added, bottom of Pg. 6). In investigating the therapeutic potential of the most potent agonist antibody 11-3F6c in the pre-clinical mouse model, the 11-3F6c-treated mice had significantly greater body weight loss than mice treated with the negative control and reached the humane endpoint earlier (Pg. 6, bottom paragraph continuing into Pg. 7 and Fig. 3b,e).
Therefore, a disclosure of MuSK agonism does not correlate directly to clinically relevant treatment methods.
The amount of direction provided by the inventor and the existence of working examples
The working examples disclosed in the specification point to the potential use of 13-3B5 and 11-3F6 in the claimed method based on MuSK phosphorylation. The art teaches however, that agonist potential in vitro does not necessarily correlate with treatment efficacy.
In view of the lack of the predictability of the art to which the invention pertains, the lack of guidance and direction provided by applicant, and the absence of appropriate working examples, undue experimentation would be required to use the claimed invention.
Response to Applicant’s Arguments
Applicant's arguments filed 03/12/2026 have been fully considered but they are not persuasive.
The applicant argues the specification provides evidence that that enables the invention. The bivalent and monovalent versions of the antibodies 13-3B5 and 11-3F6 were used to show that the bivalent antibodies were effective in inducing phosphorylation of MuSK and thereby are useful in treating the symptoms of MuSK MG(Remarks, Pg. 13)
In response, the applicants seek to patent the administration of every bivalent, monospecific antibody that specifically binds to an Ig-like 1 domain of a MuSK protein, both naturally occurring and recombinantly produced. The applicant has shown in vitro functional data pertaining two isolated and recombinantly-produced antibodies. Two antibodies are not representative of every possible binding agent multivalent binding agent as claimed. As stated in the rejection above, there is an absence of appropriate working examples commensurate with the scope of the claims. The instant specification and the art does not support the method as claimed, as one cannot readily determine which antibodies, if any, can be used in the method.
Further pertaining to the suitability of the claimed method, Lim et al. teaches MuSK Ig‑like 1 agonist antibodies caused sudden death in wild-type male C57BL/6 (Pg. 7, bottom paragraph).
New Grounds of Objection and Rejection
Claim Objections
Claim 1, 8, 22, 41, and 45-46 objected to for the following reasons:
Claims 1, 41, and 45-46 are objected to for: (1) the use of the phrase “a sequence selected from” which does not make clear that the antibody comprises all 6 CDRs recited in the subsections and (2) for ending the antibody groupings with “or” instead of “and”.
As examples of appropriate corrections, the claim could be corrected to read:
“antibody comprising six CDR sequences selected from the list comprising:” and concluding the list with “and” instead of “or” in subsection (e).
“antibody comprising a VH CDR1, CDR2, CDR3 and VL CDR1, CDR2, and CDR3 selected from the list comprising:” and concluding the list with “and” instead of “or” in subsection (e).
Claims 22, 41, and 45-46 are objected to for reciting “a bivalent, monospecific antibody comprising at least two binding regions that specifically bind to an Ig-like 1 domain of MuSK protein”. The claims were amended to state that the antibody is “bivalent, monospecific” which already indicates that the antibody has only two binding regions and they both specifically bind to an Ig-like 1 domain of MuSK protein. Therefore, the phrase “at least two binding regions” is redundant.
Claims 8 and 30 are objected for reciting the antibody is humanized. The specification teaches the claimed CDRs are human CDRs sequence from human antibodies. Therefore, it is unclear what is meant by humanized.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim is 25 rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends. Claim 25 recites “wherein the region that specifically binds to an Ig-like 1 domain of the MuSK protein is a variable region”, while claim 22 on which it depends states that the antibody comprises “at least two binding regions that specifically bind to an Ig-like 1 domain of a MuSK protein”. It is unclear if claim 25 is directed to one or both regions.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CAROL ANN CHASE whose telephone number is (571)270-0934. The examiner can normally be reached Monday-Friday 9:00am-6:00pm.
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/CAROL ANN CHASE/Examiner, Art Unit 1646
/HONG SANG/Primary Examiner, Art Unit 1646