DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Applicant’s response and claims amendments received September 17, 2025 are acknowledged.
Claims 8, 9, 12, 14, and 15 have been amended.
Claims 1-22 are pending in the instant application.
Applicant’s election without traverse of the invention of group I, drawn to antibodies that bind IGFBP5, and the antibody species of B09 (VH of SEQ ID NO:66, VL of SEQ ID NO:81, CDRS of SEQ ID NOS:1, 6, 17, 27, 39, and 51) in the reply filed on September 17, 2025 is acknowledged.
Claims 2, 8, 20, and 21 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected groups or species, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on September 17, 2025.
Information Disclosure Statement
The IDS forms received 8/17/2022, 10/19/2023, and 3/5/2025 are acknowledged and the references cited therein have been considered.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. See for example pages 5 and 6 of the specification as filed 2/1/2023. 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.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and/or amino acid sequences appearing in the specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
More specifically, Tables 4.1 and 5.1 disclose polypeptide sequences in the absence of an accompanying SEQ ID number. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 12 is 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 12 depends from claim 11, and recites that the six CDRs in the claimed antibodies are the same as those of named clones, with the six CDRs recited by SEQ ID number. However, claim 11 recites that the claimed inhibitor is an antibody selected from named antibody clones, with the same clone names appearing in claims 11 and 12. As evidenced by Tables 4 and 5 of the instant specification, the named clones refer to a fully sequenced pairing of a VH and VL isolated from panning a phage display library. Thus claim 11 is limited to exact pairing of VH and VL sequences defined by SEQ ID number as the specification defines the named clones as being limited to the requisite paired VH and VL sequences even though such sequences are not explicitly recited in claim 11 by SEQ ID number. Again, see Tables 4 and 5. Thus, claim 12 is improperly dependent because it either a) fails to further limit as the CDRs are already necessarily present in the VH and VL of the named clone, or b) applicant is attempting to “read out” the framework sequences necessarily present in the VH and VL of the named clones by just reciting the CDR sequences, thus broadening the scope of the claimed invention. Neither interpretation is permissible.
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.
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.
Claims 11 and 18 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
With regard to claim 11, the claim recites that the inhibitor is chosen from a Markush group of antibody clone names. The claim then recites “optionally the antibody … is B06 or B09”. Clones B06 and B09 are present in the Markush group found on line 2 of claim 11. Thus, how is “optional” to be interpreted? Does one or more of B06 or B09 need to actually be present to anticipate claim 11 or is such a recitation more of an “example” and thus something that does not need to be met to satisfy the claim limitations? See also MPEP 2173.05(d).
With regard to claim 18, the claim initially recites that the inhibitor of the independent claim “reduces or inhibits the binding of IGFPB5 to at least one of its receptors” and then goes on to recite “optionally wherein the at least one receptor is alpha2beta1 integrin or alphaVbeta6 integrin”. Thus, what activity is actually required to satisfy the claim? Will blocking any receptor satisfy, or must it be either alpha2beta1 integrin or alphaVbeta6 integrin? If the named integrins are not actual limitations that must be met, they should not be recited in the claim. See again MPEP 2173.05(d).
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, 3-7, 10, 13-19, and 22 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.
Applicant has broadly claimed “inhibitors” which have the functional properties of inhibiting IGFBP5, one or more receptors of IGFPB5, or the combination of IGFBP5 and its receptor(s). The broadest claims recite no structure whatsoever for such “inhibitors” and thus they are claimed using only functional language, in other words claiming such products by what they do (function) rather than what they actually are (structure). Depending claims add some structural limitations at varying levels of specificity, such as generic antibodies (see for example claim 4) as well as antibody clones recited by way of six specific CDR sequences defined by non-degenerate SEQ ID numbers (see for example claim 9). To support such breadth, the specification discloses that applicant generated 15 lead antibody clones that bind IGFBP5 via screening an antibody library (working example 1) and that two lead clones (B09 and B06) demonstrated inhibitory activity in an in vitro cell based assay (working example 3). No working examples concerning production of antibody variants, such as via CDR mutagenesis, appear to be disclosed.
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by 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 genus. See MPEP 2163. In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted: “A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.” The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606). Also see Enzo-Biochem v. Gen-Probe 01-1230 (CAFC 2002). Recent court cases have emphasized the need for correlation between a well-defined structure and recited functional limitations. For example, the courts have indicated that recitation of an antibody which has specific functional properties in the absence of knowledge of the antibody sequences that give rise to said functional properties do not satisfy the requirements for written description. See for example AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014). Such cases have indicated that that it is improper to allow patentees to claim antibodies by describing something that is not the invention, i.e. the antigen, as knowledge of the chemical structure of an antigen does not provide information as to what an antibody binding that antigen necessarily looks like (i.e. the primary amino acid structure of the antibody). Applicant is reminded that the courts have long ruled that “Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. As such, disclosure of a screening assay to test for functional properties of an antibody (such as its ability to bind IGFBP5) does not provide evidence of possession of the antibody itself. Further, courts have long ruled that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” See Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005). Also, “A sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can "visualize or recognize" the members of the genus.” See AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69.
It should be pointed out that it is well established in the art that the formation of an intact antigen-binding site requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three different complementarity determining regions, CDR1, 2 and 3, which provide the majority of the contact residues for the binding of the antibody to its target epitope. 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 parent immunoglobulin (Janeway et al., see entire selection). It is also known that single amino acid changes in a CDR can abrogate the antigen binding function of an antibody (Rudikoff et al., see entire document, particularly the abstract and the middle of the left column of page 1982). Thus, based upon the prior art, skilled artisans would reasonably understand that it is the structure of the CDRs within an antibody which gives rise to the functional property of antigen binding, the epitope to which said CDRs bind is an inherent property which appears to necessarily be present due to conservation of critical structural elements, namely the CDR sequences themselves.
Artisans are well aware that knowledge of a given antigen (for instance human IGFBP5) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al. teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire 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, see entire document). Similarly, Lloyd et al. teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al. disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). Further, it should be noted that degenerate binding of the same structural motif by antibodies does not require the existence of sequence homology or identity at any of their CDRs or other chemical similarities at the antigen-binding sites; side chain mobility of epitope residues can confer steric and electrostatic complementarity to differently shaped combining sites, allowing functional mimicry to occur (Lescar et al., see entire document, in particular Abstract and Discussion). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen, no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen. Indeed, Kanyavuz et al. teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 × 1014).
As discussed above, applicant screens a human antibody library and identified 15 lead clones that bind IGFBP5, all of which are markedly district from one another in sequence as can be readily be seen by inspection of Table 2 spanning pages 29-30, most particularly the CDR3 sequences. Based upon the knowledge in the art such as that of Edwards et al., Goel et al., and Lloyd et al. such a result is hardly surprising as a vast number of distinct antibody sequences can bind the same exact antigen. Given that the number of potential antibody structures (i.e. sequences) which can bind to the same antigen is literally astronomical the 15 clones recovered by applicant as binding IGFBP5 do not reasonably appear to be representative of such breadth. It should also be apparent that the structure of an antibody that binds IGFBP5 provides no information concerning the structures of antibodies that bind receptors of IGFPB5, and that antibody structures do not appear to have any information to provide concerning for example the structures of small molecules or other peptides that bind IGFPB5. As such there is inadequate written description in the specification as filed to support the genus of inhibitors, antibody based or otherwise, that are recited simply as having the functional property of inhibiting IGFBP5. It should be noted that some dependent claims, such as claims 5 and 6, recite additional functional properties yet still recite no specific structure responsible for giving rise to said functional properties and thus also fail to set forth a meaningful correlation between structure and function regarding the claimed “inhibitors”.
Other dependent claims do recite specific antibody structures, such as claim 7 which recites CDR sequences by SEQ ID number, and claim 10 which recites VH and VL sequences by SEQ ID number. However, such claims still do not correlate structure with function. With regard to claim 6, even though as discussed above the art generally recognizes that six specific CDRs in combination collectively give rise to the function of antigen binding, the term “and/or” is recited between parts a and b of the claim such that only three, rather than six, fully defined CDR sequences are required. Even if the “or” is deleted, as written the claims allow for random reassortment of CDR sequences isolated from independent clones. While it is often reasonable to allow for mixing and matching of CDRs from a clonal family (i.e. a collection of sequences derived by mutation from a single common ancestor, such as a naïve BCR that undergoes somatic hypermutation as part of an immune response to increase antigen binding affinity, or the mutations introduced to the Joe9 lead antibody clone in AbbVie that were considered to be a single “species” even though a large number of variants were made and tested) as can be readily seen by visual inspection of the sequences isolated from the 15 recovered clones no such single ancestry is present. Given that six CDRs are generally accepted as needed for binding, randomly choosing such CDRs from unrelated clones is not expected to yield an antibody that binds anything at all even if all of the starting clones were specific for IGFBP5. This is because the epitopes bound, as well as the way the epitopes are bound, are likely to be completely different among the clones even though they all bind the same antigen. The same logic applies to claim 10 in that it allows random reassortment of variable domain sequences among unrelated clones, and such assortment reasonably will pair three heavy chain CDRs with three light chain CDRs isolated form structurally dissimilar antibodies such that no antigen binding is reasonably expected.
At first glance, the claimed products of dependent claims 14 and 15 appear to be limited by biological sequences but in actuality they are not. Specifically, claim 14 claims antibodies that in embodiment a) bind the same epitope of IGFBP5 as named clones, in embodiment b) compete for binding IGFBP5 with named clones, in embodiment c) show the same or similar binding affinity as named clones, in part d) have one or more biological properties as named clones, and in embodiment e) have one or more pharmacokinetic properties as a named clone. Notably, the biological sequences recited in the claim are those of the named clones, i.e. the references against which a comparison is being made and thus such sequences do not have to be present in any way in the actual inhibitory anti-IGFBP5 antibody that is being claimed. Thus such a recitation is a very elaborate way of saying what the claimed antibody does without limiting the actual structure of the claimed antibody in any way. It should be apparent that the most obvious “biological property” of the recited antibody clones is their antigen binding specificity, and that claim 15 appears essentially identical in wording to claim 14 apart from claim dependency. As discussed earlier in this rejection, the prior art recognizes that a vast multitude of antibody sequences can bind the exact same antigen/epitope, and thus reciting that the claimed antibody binds in the same manner as a known reference antibody provides zero structural information about the antibody that is actually being claimed.
Therefore, in view of the breadth of the claims artisans would reasonably conclude that while applicant was in possession of the 15 anti-IGFBP5 clones recovered as part of the working examples, applicant was not in possession of the full breadth of inhibitory anti-IGFBP5 antibodies, or “inhibitors” more generically as presently recited at the time the instant application was filed. Amendment of the claims to minimally require that the anti-IGFBP5 antibodies comprise six fully defined CDRs known to collectively be capable of binding IGFBP5 when present as a set of six sequences is one possible approach to obviating the issues discussed above.
Claim 3 is rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of claim 3 is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons: Specifically, claim 3 recites that the claimed inhibitor can be chosen from structurally unrelated items including polypeptides, nucleic acids, and small molecules and as such there is no single structural similarity amongst the recited Markush members. Claim 3 depends directly from independent claim 1, which recites that the inhibitor can be specific for IGPBP5, one or more receptors of IGFPB5, or the combination of IGFBP5 and its receptor(s). Thus there is no common structure or function necessarily present in the claimed inhibitor Markush members.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 102
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.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 3, 4, 6, 7, 10, 14, and 15 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Scheepers C., and Morris L. "Multiple Antibody Lineages from Donor CAP314."; Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
Specifically Scheepers and Morris submitted an antibody sequence that is 100% identical to SEQ ID NO:81 of the instant specification, and note that SEQ ID NO:81 comprises the CDR sequences of SEQ ID NOs:27, 39, and 51 (see enclosed sequence alignment).
It is noted that the database entry does not say anything about binding IGFBP5. However, the courts have long ruled that "Products of identical chemical composition can not have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id. See also MPEP 2112. Note that as evidenced by instant claim 10 and its recitation of “and/or” an isolated VL of SEQ ID NO:81 is asserted by applicant as having the biological function of binding and inhibiting IGFPB5, and it is this exact structure which was identified by Scheepers and Morris. Thus, as evidenced by part b) of claim 10, the VL sequence of SEQ ID NO:81 by itself has the functional property of binding and inhibiting IGFBP5.
Therefore the prior art anticipates the instant claimed invention.
Claims 1, 3-6, 14, and 15, are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Melone et al. (of record on the 892 mailed 7/17/2025).
Melone et al. disclose antibodies that bind human IGFBP5 and are able to neutralize its activity in fibroblast conditioned media (see entire document, particularly the abstract, introduction, and Figure 8). Note that binding to and inhibiting the activity of IGFBP5 is a biological property shared by the antibodies of Melone and the antibodies identified by clone name in claims 14 and 15.
Therefore, the prior art anticipates the instant claimed inventions.
Claim 9 is are objected to as being dependent upon a rejected independent claim, but would be allowable if rewritten in independent form including all of the limitations of the independent claim and any intervening claims.
No claims are allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Michael Szperka whose telephone number is (571)272-2934. The examiner can normally be reached Monday-Friday 8:30-5:00.
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Michael Szperka
Primary Examiner
Art Unit 1641
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641