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 .
Status of Application, Amendments and/or Claims
The amendment, filed 18 February 2026, has been entered in full. Claims 50 and 51 are canceled. Claims 3, 4, 6, 7, 9, 11-33, 35, 38, 39, 41-44, 46-49 and 52 are amended. New claims 53-61 are added. The amendment, filed 17 April 2026, has been entered in full. Claims 1-61 are canceled. New claims 62-86 are added. The amendment, filed 05 June 2026, has been entered in full. Claims 62-86 are canceled. New claims 87-111 are added.
Applicant’s election of Group I (claims 87-99, 110 and 111; drawn to an anti-IL-11 antibody or antigen-binding fragment thereof, a pharmaceutical composition comprising the anti-IL-11 antibody or antigen-binding fragment thereof, and a diagnostic kit comprising said antibody or antigen-binding fragment thereof) and
the species election of (HCDR1 SEQ ID NO:1; HCDR2 SEQ ID Nos; 3, 5; HCDR3 SEQ ID NO:7; LCDR1 SEQ ID NO:9; LCDR2 SEQ ID Nos: 10, 12; LCDR3 SEQ ID NO:13; VH SEQ ID Nos: 14, 17; VL SEQ ID Nos: 19, 21; HC SEQ ID Nos: 26, 29 and LC SEQ ID Nos: 31, 33), in the reply filed on 10 August 2026 is acknowledged.
Upon allowance of a generic claim, Applicant will be entitled to consideration of claims to additional species.
Because Applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Claims 100-109 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 10 August 2026.
Claims 87-99, 110 and 111 are under examination.
Information Disclosure Statement
The information disclosure statement(s)(IDS) (filed 6/5/26, 6/10/26 and 8/10/26) were received. They have been placed in the application file and the information referred to therein has been considered as to the merits.
It is noted that some of the references fail to comply with the provisions of 37 CFR §§1.97, 1.98 and MPEP § 609. MPEP 609.05 [R-3] states that information disclosure statements will be reviewed for compliance with the requirements of 37 CFR 1.97 and 37 CFR 1.98 as discussed in MPEP 609.04(a) and MPEP 609.04(b). The references will be lined through and not considered by the Examiner.
References: The references should include the name of the author, title of the article, name of the item (i.e. book, magazine, Journal, symposium, catalog, etc.), the volume-issue number, the pages, and date.
BOOKS: Books should be identified by publisher, author, relevant pages, date and place of publication. The following are examples of non-patent bibliographical citations: (A) For books: Winslow. C. E. A. Fresh Air and Ventilation. N.Y., E. P. Dutton, 1926. p. 97-112. TI17653.W5. (B) For parts of books: Smith, J. F. "Patent Searching." in: Singer, T.E.R., Information and Communication Practice in Industry (New York, Reinhold, 1958), pp. 157-165. T 175.S5.
See MPEP § 707.05(e) III, for more information on data that should be used when citing publications.
The following references not considered by the Examiner for the following reasons:
1. The US National Institute of Health reference is missing page number(s).
2. The Kabat et al. reference, listed on IDS 8/10/26, appears to be from a book and is not cited properly.
3. The following references listed on IDS 6/10/26 appear to be from books and are not cited properly: Zola et al; Hurrell; Ciliberto et al and Boardman et al.
Applicant is advised that the date of any re-submission of any item of information contained in this information disclosure statement or the submission of any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the statement, including all certification requirements for statements under 37 CFR 1.97(e). See MPEP § 609.05(a).
Claim Objections
Claim 110 is objected to because of the following informalities:
Claim 110 recites, “A diagnostic kit or diagnostic method comprising the anti-IL-11 antibody or antigen-binding fragment thereof according to claim 87”.
The claim is objected to because it refers to a composition (i.e. a diagnostic kit) and a method (i.e. diagnostic method) in the same claim.
Furthermore, Applicant elected Group I (claims 87-99, 110 and 111; drawn to an anti-IL-11 antibody or antigen-binding fragment thereof, a pharmaceutical composition comprising the anti-IL-11 antibody or antigen-binding fragment thereof, and a diagnostic kit comprising said antibody or antigen-binding fragment thereof).
Amending claim 110 to recite, “A diagnostic kit comprising the anti-human IL-11 antibody or antigen-binding fragment thereof according to claim 87”, would be remedial. 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.
Claim 111 is 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 instant claim is drawn to an anti-human IL-11 antibody or antigen-binding fragment thereof, wherein when bound to human IL-11, the antibody or antigen-binding fragment thereof binds to amino acid residues R15, D19, L23, R26, S27 L29, A30, D31, R33, R40, N50, L57, A58, R111, H161, L162, D165, W166, V168, R169, L172, L173, K175, or T176 as set forth in SEQ ID NO: 49, and wherein the antibody blocks binding of IL-11 to IL-11Rα.
The claimed subject matter is not supported by an adequate written description. The instant claim encompasses a genus of undisclosed anti-human IL-11 antibodies or antigen-binding fragments thereof based entirely on function: binding to amino acid residues R15, D19, L23, R26, S27 L29, A30, D31, R33, R40, N50, L57, A58, R111, H161, L162, D165, W166, V168, R169, L172, L173, K175, or T176 as set forth in SEQ ID NO: 49 and blocking the binding of IL-11 to IL-11Rα.
Accordingly, the claim recites a vast genus of molecules that must have the recited functional limitations, but no structural limitations.
The number of structures encompassed by the genus may be vast or conversely there may be no structures that possess the claimed function. The claim reads on an anti-human IL-11 antibody or antigen-binding fragment thereof, having any number of substitutions, deletions and/or insertions at every position with respect to the wild-type sequence as long as it retains function.
MPEP§ 2163 states that the written description requirement for a claimed genus may be satisfied through establishment of a structure-function correlation (show a structure is correlated with the function) OR through a sufficient description of a representative number of species (show a representative number of species that have the function. There must be enough species that are representative of the full breadth of the genus).
Regarding structure-function correlation:
The formation of an intact antigen-binding site of all antibodies 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 (Reference submitted by Applicant; Al Qaraghuli et al. Antibody‑protein binding and conformational changes: identifying allosteric signaling pathways to engineer a better effector response. Nature Scientific Reports 10:13969, 2020).
The art recognizes that a single protein can be bound by a very large and structurally diverse genus of antibodies (i.e., there is no common structural relationship even for antibodies that bind to the same protein, epitope, or overlapping epitopes). For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences, and representative of almost the entire extensive heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines), and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well (Reference submitted by Applicant; Edwards et al. The remarkable flexibility of the human antibody repertoire; isolation of over one thousand different antibodies to a single protein, BLyS. Journal of Molecular Biology 334:103-118; 2003).
Goel et al. teach that three mAbs that bind to the same short (12-mer) peptide, exhibit diverse V gene usage, indicating their independent germline origin. Said reference further teaches that two of these mAbs recognize the same set of amino acid residues defining the epitope (alternate amino acid residues spread over the entire sequence), however, the relative contribution of each set of residues in the peptide showed significant variation. The reference notes that all of the mAbs do not show any kind of V gene restriction among themselves, implying variable paratope structure, despite that two of these mAbs bind to the peptide through a common set of residues. (See entire reference)(Reference submitted by Applicant; Goel et al. Plasticity within the antigen-combining site may manifest as molecular mimicry in the humoral immune response. J. Immunol. 173: 7358-7367; 2004).
Khan et al. teach that two structurally diverse germline mAbs recognizing overlapping epitopes of the same short peptide do so in different topologies, the antibodies possessing entirely different CDR sequences. Said reference teaches that unrelated mAbs structurally adjust to recognize an antigen, indicating that the primary B cell response is composed of BCRs having a high degree of structural adaptability. Said reference also teaches that the common epitope(s) also adopt distinct conformations when bound to different mAbs, with the higher degree of structural plasticity inherent to the mAbs. Said reference further teaches “It has been shown that both the framework region and the CDRs have a considerable amount of inherent conformational plasticity...Therefore, it is not surprising that distinct germline Abs recognize the same epitope by rearranging the CDR conformations. This may well have implications of Ag specificity beyond the naive BCR repertoire, because Kaji et al... .have shown in a recent report that the B cell memory can contain both germline-encoded and somatically mutated BCRs” (See entire reference)(Reference submitted by Applicant; Khan et al. Adjustable locks and flexible keys: plasticity of epitope-paratope interactions in germline antibodies. J. Immunol. 192: 5398-5405; 2014).
Poosarla et al. teach substantial diversity in designed mAbs (sharing less than 75% sequence similarity to all existing natural antibody sequences) that bind to the same 12-mer peptide, binding to different epitopes on the same peptide. Said reference further teaches “most B-cell epitopes... in nature consist of residues from different regions of the sequence and are discontinuous...de novo antibody designs against discontinuous epitopes present additional challenges..." (See entire reference)(Reference submitted by Applicant; Poosarla et al. Computational De Novo Design of Antibodies Binding to a Peptide With High Affinity. Biotechn. Bioeng. 114(6): 1331 -1342; 2017).
The combination of evidentiary publications thus underscores a lack of structure-function correlation in antibody molecules.
Regarding a representative number of species: the instant specification fails to describe a representative number of species to provide adequate written description of the claimed genus as per MPEP § 2163. There must be enough species that are representative of the full breadth of the genus. A "representative number of species" means that the species, which is adequately described, is representative of the entire genus. When there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
The specification teaches that Antibodies A through O were assessed to determine if they are capable of blocking IL-11 signaling. Antibodies A through O were tested in a phospho-STAT3 assay in IL-11-stimulated human lung carcinoma cells (HTB183 cells) with endogenous IL-11Rα. The specification teaches Antibodies A through O dose-dependently reduced p-STAT3 in 50 ng/ml (2.5 nM) of IL-11-stimulated HTB183.
The specification fails to teach which antibodies (i.e. Antibody A through Antibody O) bind to amino acid residues R15, D19, L23, R26, S27 L29, A30, D31, R33, R40, N50, L57, A58, R111, H161, L162, D165, W166, V168, R169, L172, L173, K175, or T176 as set forth in SEQ ID NO: 49.
However, even with such disclosure of which antibodies bind to the recited amino acid residues, it is not be representative of an entire genus of antibodies comprising an unlimited number of different structures with the claimed function.
The claimed genus is highly variant and encompasses an unlimited number of individual and combination substitutions. The specification does not describe the structure for substitution variants, deletion variants or insertion variants with the biological function. There is no information regarding what structural features would likely be associated the claimed function. The specification fails to teach the structural identifying characteristics that are applicable to the genus.
The courts have specifically stated that the skilled artisan cannot envision the detailed chemical structure of an encompassed molecule until the structure is disclosed, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation.
In the instant case, the skilled artisan cannot envision the detailed chemical structure of the encompassed antibodies which have the claimed activity without further testing.
Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method of isolating it. The compound itself is required. See Fiers v. Revel, 25 USPQ2d 1601 at 1606 (CAFC 1993) and Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. One cannot describe what one has not conceived.
See Fiddes v. Baird, 30 USPQ2d 1481 at 1483. In Fiddes, claims directed to mammalian FGF’s were found to be unpatentable due to lack of written description for that broad class. The specification provided only the bovine sequence.
Accordingly, it is deemed that the instant specification fails to provide adequate written description for the genus of the claims and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Allowable Subject Matter
Claim objection
An anti-interleukin (IL-11) antibody or antigen-binding fragment thereof comprising the elected species of heavy chain variable region (VH) comprising (HCDR1 SEQ ID NO:1); (HCDR2 SEQ ID NO: 3 or 5); (HCDR3 SEQ ID NO:7) AND light chain variable region (VL) comprising (LCDR1 SEQ ID NO:9); (LCDR2 SEQ ID NO: 10 or 12); LCDR3 SEQ ID NO:13) is free of the art.
The Examiner notes that search and consideration of the additional species will not be carried out because the generic claim has not been allowed (i.e. claim 111).
Therefore, Claim 87 would be allowed if amended to delete the limitation “with the proviso that if the VH comprises the amino acid sequence of SEQ ID NO:1 (H-CDR1), the amino acid sequence of SEQ ID NO: 4 (H-CDR2), and the amino acid sequence of SEQ ID NO: 7 (H-CDR3), then the VL comprises the amino acid sequence of SEQ ID NO: 10 (L-CDR2) or SEQ ID NO: 12 (L-CDR2)”.
Additionally, claims 87-99 would be allowed if amended to delete the non-elected species.
Conclusion
Claim 111 is rejected.
Claims 87-99 and 110 are objected to.
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to REGINA M DEBERRY whose telephone number is (571)272-0882. The examiner can normally be reached M-F 9:00-6:30 pm (alt Fri).
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/R.M.D/Examiner, Art Unit 1647 8/31/2026
/JOANNE HAMA/Supervisory Patent Examiner, Art Unit 1647
