DETAILED ACTION
Status of Application, Amendments and/or Claims
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
The amendment of 5/11/26 has been entered in full. Claims 1 and 15 are amended. Claims 16-17, 28-33 and 39-40 are canceled. New claims 44-54 are added. Claims 1-5, 15, 26-27 and 44-54 are pending.
Election/Restrictions
Applicants' election without traverse of Group I, currently all pending claims, in the reply filed on 5/11/26 is acknowledged. The election without traverse of antibody clone 4A2 as the species of antibody in the reply is also acknowledged.
Claims 1-5, 15, 26-27 and 44-54 are under consideration, as they read upon the elected species.
Specification
The disclosure is objected to for the following informalities:
---The title is not descriptive because it is directed generally to ASGR inhibitors, but the claims are limited to inhibitors that are antigen binding proteins. A new title is required that is clearly indicative of the invention to which the claims are directed. In view of the rejection of the claims under 35 U.S.C. 112(a), the following title is suggested: “ANTI-ASGR-1 INHIBITORY ANTIBODIES”.
Appropriate correction is required.
Claim Objections
Claims 1-5, 15, 26-27 and 44-54 are objected to for the following informalities:
In claim 1, lines 3 and 5, the word "ligand" is missing an article, e.g., "a ligand".
In claim 15, line 4, “VH CDR2 and VH CDR3” should be “a VH CDR2 and a VH CDR3”. Compare with “a VL CDR2 and a VL CDR3” in lines 4-5.
In claim 49, line 3, “VH CDR2 and VH CDR3” should be “a VH CDR2 and a VH CDR3”. Compare with “a VL CDR2 and a VL CDR3” in line 4.
In each of claims 50 and 51, line 3 of each claim, “29170,28966” should be “29170, 28966”.
The remaining claim(s) are objected to for depending from an objected claim.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
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.
Claim 3 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention.
Claim 3 limits the antibody of claim 1 to one wherein that "inhibits the internalization of ASGR". However, parent claim 1 is limited to an antibody that inhibits "ASGR-1 binding to ligand". Because claim 1 uses "ASGR-1", and claim 3 uses "ASGR", and the term "ASGR" is broader in scope (as it can encompass ASGR-2), it is unclear whether the term as used in claim 3 is meant to refer to ASGR-1 as in claim 1, or more broadly refer to ASGR-1 or ASGR-2.
Claim Rejections - 35 USC § 112(a), written description
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 1-4 and 27 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
In making a determination of whether the application complies with the written description requirement of 35 U.S.C. 112(a), it is necessary to understand what Applicants are claiming and what Applicants have possession of.
The claims are directed to products; specifically, claim 1 is directed to an isolated antigen-binding protein (ABP) that binds to human asialoglycoprotein-1 receptor (hASGR-1; SEQ ID NO: 5), wherein the ABP inhibits ASGR-1 binding to ligand, and wherein the ABP (1) binds hASGR-1 with an equilibrium dissociation constant of 10-8 M or less, and/or (2) inhibits hASGR-1 binding to a ligand with a half-maximal inhibitory concentration (IC50) of 90 nM or less. Claims 2-5 and 26 further limit the claimed ABP. Claim 27 is directed to a pharmaceutical composition comprising the ABP of claim 1 and a pharmaceutically acceptable excipient. The elected species under consideration is antibody clone 4A2, which comprises a heavy chain variable domain (VH) of SEQ ID NO: 29170 (including HCDRs1-3 of SEQ ID NO: 5136, 13148 and 21160) and a light chain variable domain (VL) of SEQ ID NO: 25164 (including LCDRs1-3 of SEQ ID NO: 1130, 9142 and 17154).
The instant specification defines an “antigen binding protein” as “a protein comprising an antigen binding fragment that binds to an antigen and, optionally, a scaffold or framework portion that allows the antigen binding fragment to adopt a conformation that promotes binding of the antigen binding protein to the antigen” (¶ 117, published application). As the scaffold or framework is optional, the term broadly encompasses any "antigen binding fragment that binds to an antigen". The term “antigen binding fragment” is not further provided with a limiting definition in the specification. As such, the term “antigen binding protein”, or ABP, is limited structurally only as it must be a protein; i.e., a sequence of two or more amino acids. While the specification further teaches that in certain embodiments, the fragment “comprises at least one CDR from an antibody that binds to the antigen" (¶ 118), the term "antigen binding protein" also encompasses non-antibody protein structures that have the required functions, including binding to human ASGR-1 (SEQ ID NO: 5, 291 amino acids in length), inhibiting its binding to ligand, and wherein the binding is defined by its equilibrium dissociation constant, and/or the inhibition is defined by its half maximal inhibitory concentration. Thus, the claims are genus claims encompassing a genus of proteins (of two or more amino acids in sequence) having the required functionality.
The specification teaches that the ASGR receptor "is a C-type lectin that is expressed on the surface of hepatocytes and is made up of 48 kDa major subunit(s) (ASGR-1) and 40 kDa minor subunit(s) (ASGR-2)"; is "formed by the oligomerization of the ASGR-1 and ASGR-2 subunits"; and is made of "homo-oligomers and hetero-oligomers of the ASGR-1 and ASGR-2 subunits, with (ASGR-1)2-(ASGR-2)1 trimer being the most common form and having the highest affinity to substrate" (¶ 105). The specification provides the sequences for ASGR-1 and ASGR-2 proteins from several mammalian species (e.g., Figure 1; ¶ 106), including humans (SEQ ID NO: 5 and 32713, respectively). Figure 3 shows an alignment between human ASGR-1 and -2. The art recognizes a homology of 58% between the two human subunits (Spiess et al, 1985. Proc Natl Acad Sci USA. 82:6465-6469; cited on the 11/15/24 IDS), which are 291 and 287 amino acids in length, respectively (SEQ ID NO: 5 and 32713).
The Federal Circuit in Amgen v. Sanofi, 872 F.3d 1367 (Fed. Circ. 2017) held that a claim directed to an antibody requires written description of the antibody itself rather than being satisfied solely by a written description of the antigen to which it binds (the so-called "newly characterized antigen" test). Thus, a description of the target protein (e.g. ASGR-1 or ASGR-2) itself is not sufficient to provide a written description of the genus of antibodies (or other antigen binding proteins) of said target protein. Thus, in the instant case the specification must provide a written description of the structure of the claimed antibodies.
The specification provides the following working example(s) in support of the claimed invention. Tables A, B and C (starting at ¶ 254) provide the sequences of exemplary anti-ASGR antibodies. Table A provides the VH and VL sequences of 175 different anti-ASGR antibody clones, and Table B provides another the sequence of another 86. Table C provides the CDR sequences (HCDR1-3 and VCDR1-3) for 30 of these clones. The specification indicates that each of these antibodies binds to ASGR-1 (e.g., at ¶ 222). Table 7.4 shows the results of "epitope binning" for 162 of these antibodies, with the antibodies binding to 14 different epitopes across the ASGR-1 protein. Table 7.1 shows the results of testing 32 of antibodies for binding to various mammalian ASGR-1 sequences, with all binding to human and cynomolgus monkey ASGR1, and subsets binding to mouse, rat, dog and/or pig ASGR-1.
Example 6B teaches that antibodies "having the ability to reduce ligand binding ≥60% were identified (Table 6.1), and sequenced", with the "sequences of unique ASGR-1-specific, ligand blocking antibodies" being included in Table 2-7 (¶ 518). Table 6.1 indicates that Table 3 provides the sequence of 2,603 unique ligand blockers (¶ 516). Example 13 describes an assay for testing whether the antibodies inhibit AGSR-1 binding to the ligand GalNAc-PAA and/or the ligand asialofetuin (¶ 799), with the results for over 30 different clones showing inhibition reported in Table 13.1. Table 11.1 provides the dissociation constant for 47 of the antibody clones; 42 of these, including the elected species of 4A2, have dissociation constants that are less than 10 x 10-9 nM, which is equivalent to less than 10-8 M, as required by instant claim 1 in the alternative. Table 13.1 provides the IC50 for 35 of the antibody clones; 30 of these have an IC50 of 90 nM or less, as required by instant claim in the alternative.
The disclosure of the large genus of anti-ASGR antibodies, including the tested clones exhibiting the requisite functional activities, corresponds to a disclosure of a representative number of species antibodies encompassed by claim 1. However, the working examples do not provide an examples (i.e., amino acid sequences) of antigen-binding proteins having structures other than antibodies than have the requisite functional activities; i.e., binding human ASGR-1, inhibiting its binding to a ligand, and wherein the binding is defined by a specific equilibrium dissociation constant, and/or the inhibition is defined by a specific half maximal inhibitory concentration. The specification further does teach how the disclosed antibody sequences describe other non-antibody protein sequences having the required functions; i.e., by establishing a correlation between the structure of the antibodies and the structure of other non-antibody proteins having the same functionality.
MPEP 2163 provides guidance for complying with the written description requirement of 35 U.S.C. 112(a) that the “specification shall contain a written description of the invention…”; this requirement is separate and distinct from the enablement requirement (Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1355 (Fed. Cir. 2010)). Written description for a claimed genus may be satisfied through sufficient description of a relevant number of species. This is dependent on whether one of skill in the art would recognize necessary common attributes or features possessed by the members of the genus. Generally, in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus. Written description for a claimed genus can also be satisfied when relevant identifying characteristics are disclosed. Per MPEP 2163, “[d]etermine whether the specification discloses other relevant identifying characteristics sufficient to describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize applicant was in possession of the claimed invention. For example, if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function. Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function.” However, claiming by function does not necessarily satisfy the written description requirement. “[A] generic statement such as "vertebrate insulin cDNA" or "mammalian insulin cDNA," without more, is not an adequate written description of the genus because it does not distinguish the claimed genus from others, except by function. It does not specifically define any of the genes that fall within its definition. It does not define any structural features commonly possessed by members of the genus that distinguish them from others … 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. It is only a definition of a useful result rather than a definition of what achieves that result” (Regents of the University of California v. Eli Lilly Co., 119 F.3d 1559 (Fed. Cir. 1997)). Also, “[w]hen 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" (Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005)), and “[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” (AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69).
Vas-Cath Inc. v. Mahurkar, 19USPQ2d 1111 (Fed. Cir. 1991), clearly states “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the ‘written description’ inquiry, whatever is now claimed” (pg 1117). The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed” (pg 1116). As discussed above, the skilled artisan cannot envision the detailed chemical structure of the encompassed genus of antigen-binding proteins, and therefore conception is not achieved until reduction to practice has occurred, regardless of the complexity or simplicity of the method of isolation. 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 (Fed. Cir. 1991). One cannot describe what one has not conceived. See Fiddes v. Baird, 30 USPQ2d 1481 at 1483 (BPAI 1993)., where claims directed to mammalian FGFs were found unpatentable due to lack of written description for that broad class.
Therefore, an isolated antibody that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO: 5, wherein the antibody inhibits ASGR-1 binding to a ligand, and wherein the antibody binds to human ASGR-1 with an equilibrium dissociation constant of 10-8 M or less, and/or inhibits human ASGR-1 binding to a ligand with a half maximal inhibitory concentration (IC50) of 90 nM or less, but not the full breadth of the claims meets the written description provision of 35 U.S.C. §112(a). Applicants are reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (pg 1115).
Furthermore, with respect to claim 3, the working examples do not provide a representative number of species falling within the scope of the genus of antibodies that inhibit ASGR-1 binding to ligand, and also inhibit internalization of ASGR (a term that is indefinite for the reasons set forth above, but is here interpreted as reading on ASGR-1 or ASGR-2). Example 8 of the specification describes as "ASGR Internalization Assay", but this example appears to be prophetic as it concludes that the assay "can be performed to assay the antigen binding proteins of the invention to determine how much they reduce or inhibit internalization", and does not appear to report any results for such an assay. As such, the specification fails to describe which of the antibodies of claim 1 disclosed in the specification are also able to inhibit internalization of an ASGR protein.
Furthermore, with respect to claim 4, the working examples do not provide a representative number of species falling with the scope of the genus of antibodies that bind to ASGR-2 or "ASGR" generally, which is a genus that includes ASGR-1, ASGR-2 and complexes of such. Table 7.1 shows that only 2 of the 30 tested anti-ASGR-1 antibody clones also bind to ASGR-2; specifically clones 7F4 and 6G7. Clone 6G7, however, also does not have an IC50 of 90 nM or less; see Table 13.1. While the disclosure one example, i.e., 7F4, is sufficient to provide written description for antibodies comprising the disclosed CDRs of the example, the disclosure of such is not sufficient to define the structure of a genus of antibodies that inhibit ASGR-1 ligand binding and that further bind to the ASGR-2 protein.
Therefore, (1) dependent claim 3 fails to meet the written description provision 35 U.S.C. §112(a); and (2) dependent claim 4 fails to meet the written description provision 35 U.S.C. §112(a), except with respect to an antibody comprising the VL CDR1-3 and VH CDR1-3 from antibody clone 7F4. Applicants are reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (pg 1115).
Note on Prior Art Rejection(s)
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 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.
Claim Rejections - 35 USC § 102
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.
Claims 1, 2 and 5 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Born, September 2005, "Benefits and Application of Antibodies Against the H1 Carbohydrate Recognition Domain of the Human Hepatic Asialoglycoprotein Receptor", Dissertation, 324 pages as published (cited on the 11/15/24 IDS). The earliest date to which the instant application claims priority is 9/25/15.
Claim 1 encompasses an isolated antigen-binding protein (ABP) that binds to human asialoglycoprotein-1 receptor (hASGR-1; SEQ ID NO: 5), wherein the ABP inhibits ASGR-1 binding to ligand, and wherein the ABP (1) binds hASGR-1 with an equilibrium dissociation constant of 10-8 M or less, and/or (2) inhibits hASGR-1 binding to a ligand with a half-maximal inhibitory concentration (IC50) of 90 nM or less.
Born teaches that the asialoglycoprotein receptor, or ASGPR, is composed of two subunits, H1 and H2. Born identifies H1 as having the sequence P07306; see Figure 27 (numbered page 114 [page 150 as printed]). The NCBI Protein Database record for P07306 provides the 291 amino acid sequence for this protein, which is identical to instant SEQ ID NO: 5 (NCBI Record for P07036, dated 2/23/22, 6 pages as printed, no author indicated; available on-line at www.ncbi.nlm.nih.gov/protein/P07036; cited here solely to provide evidence of the inherent amino acid sequence of P07306; cited on the 11/15/24 IDS). Born further teaches "Production and purification of monoclonal antibodies" against the carbohydrate recognition domain (CRD) of H1 in section 2.4 (see numbered page 83 [page 119 as printed]). Born further teaches an assay for determining whether an anti-H1 mAb competes for binding with the ASGRP1 ligand GalNAc (Section 2.5.1.3.3; page 93 [page 123 as printed]). Born further provides examples of isolated mAbs that tested positive in this assay; e.g., clone B01.4 (section 3.5.2.2.3, numbered pages 159-160 [page 195 as printed]). Burn further provides the IC50 of said antibodies in in inhibiting GalNAc binding, with most having values of 90 nM or less, e.g., clone B01.4 (Figure 170, numbered page 249 [page 285 as printed]). Thus, Born teaches an isolated ABP (i.e., antibody) that binds to hASGR-1 of SEQ ID NO: 5 and inhibits binding of ASGR-1 to a ligand with an IC50 of 90 nm or less. As such, the teachings of Born anticipate claim 1.
Claim 2 limits the ABP of claim 1 to one wherein the ABP binds a carbohydrate recognition domain of human ASGR-1. The teachings of Born described above are directed to an antibody that binds a CRD of human ASGR-1. As such, the teachings of Born also anticipate claim 2.
Claim 5 limits the ABP of claim 1 to one wherein the ABP is a monoclonal antibody. The teachings of Born described above are directed to monoclonal antibody clones. As such, the teachings of Born also anticipate claim 5.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were effectively filed absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned at the time a later invention was effectively filed in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 26 and 27 are rejected under 35 U.S.C. 103(a) as being unpatentable over Born, September 2005, "Benefits and Application of Antibodies Against the H1 Carbohydrate Recognition Domain of the Human Hepatic Asialoglycoprotein Receptor", Dissertation, 324 pages as published (cited on the 11/15/24 IDS), as applied to claim 1 above, and further in view of Queen et al, U.S. Patent 5,693,762, published 12/2/1997 (cited on the 11/15/24 IDS).
Claim 26 encompasses an ABP of claim 1 that is a humanized antibody.
The teachings of Born that anticipate parent claim 1 are set forth above. These teachings include how to make the antibody. Born further teaches that the monoclonal antibodies of the invention are valuable for diagnostic and therapeutic applications (numbered page 258 [page 294 as printed]).
Born does not teach such a humanized version of such a mAb.
Queen teaches improved methods for humanizing a monoclonal antibody of interest, with the advantage that the humanized antibody is "less immunogenic when injected in humans" (col 2, lines 8-9). These methods are for use with any "donor immunoglobulin" of interest (col 2, line 39).
It would have been obvious to the person of ordinary skill in the art before the effective filing date of the claimed invention to make an isolated mAb that binds to human ASGR-1 comprising the amino acid sequence of SEQ ID NO:5, wherein the mAb inhibits ASGR-1 binding to ligand, as taught by Born, and to further modify such an mAb to make it a humanized antibody as taught by Queen. The person of ordinary skill in the art would have been motivated to make such a modification in order to improve the antibody for use in diagnostic and/or therapeutic applications where humanization would be expected to reduce the immunogenicity of the antibody when administered. The person of ordinary skill in the art would have had a reasonable expectation of success in making such an antibody because Born demonstrates examples of anti-AGSR1 antibodies produce by such techniques, and Queen teaches that the humanization methods are generally applicable to any donor immunoglobulin of interest. This rationale supports a prima facie conclusion of obviousness in accord with KSR International Co. v. Teleflex Inc., 82 USPQ2d 1385 (2007).
Claim 27 is directed to a pharmaceutical composition comprising the isolated monoclonal antibody of claim 1 and a pharmaceutically acceptable excipient. Queen further teaches that the humanized antibodies of the invention are suitable for administration in a pharmaceutical composition also comprising an acceptable carrier, which meets the limitation of a "pharmaceutically acceptable excipient" (col 23, lines 55-66). Thus, it would have further been obvious to take the humanized antibodies obvious over the teachings of Born in view of Queen, and further modify it to place it in a pharmaceutical composition also comprising a pharmaceutically acceptable excipient, for the purposes of administering the antibody for diagnostic or therapeutic use.
Notes
No prior art has been identified that teaches or suggests an isolated monoclonal antibody, or antigen binding fragment thereof, that binds to human ASGR-1 and comprises heavy and light chain variable domains comprising VH CDR1-3 and VL CDR1-3 having the specific sequences recited in parts (i)-(xxiv) of independent claim 15 (also required by claims 44-48 that depend from claim 15) or having the specific sequences recited in parts (i)-(xxv) of independent claim 49 (also required by claims 50-54 that depend from claim 49).
The following articles, patents, and published patent applications were found by the Examiner during the art search while not relied upon for a rejection are considered pertinent to the instant application:
Hofer et al, WO 2014023709, published 2/13/14 (cited on the 11/15/24 IDS) teaches anti-ASPGR antibodies; however, each antibody taught by Hofer differs from the antibody of claim 1 in that the antibody of Hofer "does not compete with a natural ligand of ASGPR for binding to ASGPR" (page 4, lines 15-16), whereas as instant claim 1 (and claims 2-4, 27, 44 and 45 depending from claim 1) specifically requires that the antibody "inhibits ASGR-1 binding to ligand". Furthermore, Hofer specifically teaches the lack of competition as an advantage; e.g., "[a] further advantage of the antibodies of the invention is that they do not compete for binding to ASGPR with natural ligands of the receptor (asialoglycoproteins such as e.g. asialofetuin), i.e. antibody binding is not affected by the presence of ASGPR ligand and does not interfere with the natural function of ASGPR" (page 34). Thus, Hofer teaches away from modifying the teachings of Hofer to identify an antibody that does compete for binding to ASGRP with a ligand.
Conclusion
No claims are allowable.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ZACHARY C HOWARD whose telephone number is (571)272-2877. The examiner can normally be reached on Monday to Friday from 9 AM to 5 PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Vanessa Ford, can be reached at telephone number (571) 272-0857. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ZACHARY C HOWARD/Primary Examiner, Art Unit 1674
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