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 .
Priority
This application is a divisional of Application No. 16/509,366, which claims benefit to U.S. Provisional Application No. 61/892,283, filed October 17, 2013.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on November 8, 2023 and January 21, 2025 are compliance with the provisions of 37 CFR 1.97. Accordingly, the IDSs are being considered by the examiner. The publication dates for CO1122 and CO1123 on the IDS from 11/8/2023 have been added.
Claim Status
Claims 1-9 are under consideration in this office action.
Claim Objections
Claim 3 is objected to because of the following informalities:
In line 2 of claim 3 there is an unnecessary comma between “antibody” and “or”. Appropriate correction is required.
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.
Claims 1-9 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.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991). See also MPEP 2163.04.
Claim 8 recites a “human antibody”; in the specification, “human antibody” is not defined. “Humanized antibody” is defined as an antibody from a non-human species whose protein sequences have been modified to increased similarity to antibody variants produced naturally in humans (instant specification, pg 30). While humanized antibodies are an example of a human intervention, human antibodies are a natural product because the intervention is only isolation, which does not significantly change or manipulate the naturally occurring product. The specification does not clearly set forth what “human antibody” means and how “human” antibodies are made and isolated; thus, “human” is interpreted to mean an antibody isolated from a human. Claim 8 fails to meet the written description requirement because the disclosure fails to describe clearly these human antibodies or show that the inventor was in possession of the human antibodies at the time the invention was filed. Therefore, the limitation of claim 8 directed to a human antibody must be cancelled from the claim.
Claim 1 is directed to a method of treating a subject suffering from Degos disease by administering a MASP-2 inhibitory agent. According to the specification (pg 28), the inhibitor agent is an anti-MASP-2 inhibitory antibody or fragment thereof, a small molecule inhibitor, a peptide inhibitor, or an antisense RNA or DNA molecule. The state of the art recognizes that numerous molecules of highly diverse structure are within the scope of the genus of MASP-2 inhibitory agent. Further, this genus is defined entirely by its function, i.e. what it binds and what it inhibits. In the dependent claims, the inhibitor of MASP-2 is only further limited to anti-MASP-2 antibodies and antibody fragments thereof, and, thus, the discussion below will focus on why the antibody, as claimed, does not meet the written description requirement.
Antibodies generally share certain characteristics such as Fc regions or hinge regions. However, these structures are not correlated with the binding function of the antibody. It is well established in the art that the formation of an intact antigen-binding site generally requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three complementarity determining regions (CDRs) that 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 immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences, which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (see Almagro et al, Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1; instant PTO-892).
There is no way to a priori look at an antigen sequence (e.g., MASP-2) and envisage the combination of six CDRs that will bind that antigen. First, even highly related CDRs may not bind the same target. See for example Kussie (IDS from 11/8/2023, CO1654), who demonstrates that a single amino acid change in the heavy chain of an antibody that binds p-azophenylarsonate (Ars) completely abrogates the ability of the antibody to bind Ars but adds the functionality of binding the structurally related p-azophenylsulfonate (see abstract). Second, even when provided with several related antibodies that bind the desired target, this does not represent the astronomical and potentially unknowable breadth of all possible amino acid sequences which will result in the desired binding properties. This is exemplified by the Court decision in Abbvie (Abbvie v Janssen 759 F.3d 1285 (Fed. Cir. 2014)), where Abbvie developed over 200 antibodies that shared 99.5% identity in the variable regions (pg 7) and which bound the target, but in no way allowed one to envisage the unique structure of Centocor’s antibodies which bound the same target but shared only 50% sequence similarity (see table on pg 11).
While the prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is 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.
According to the specification, the applicant has disclosed two specific species of anti-MASP-2 antibody, which are comprised of specific combinations of heavy chain CDRs and light chain CDRs. However, the specification does not provide adequate written description for the entire claimed genus of anti-MASP-2 antibodies, because one skilled in the art would be unable to immediately envision, recognize, or distinguish most of the members comprised within the genus claimed, specifically which heavy chain and light chain amino acid sequences should be combined to yield an antigen-binding region that is capable of binding Gal3 and capable of crossing the blood brain barrier.
To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention.
In the instant case, the specification provides insufficient direction or guidance concerning the relationship between the structure of the possible antibody to demonstrate possession of the breadth of the genus of anti-MASP-2 antibodies encompassed by the instant claim, especially in view of the unpredictability of such an endeavor. The prior art, as evidenced by Edwards et al., 2003 (instant PTO-892), teaches there is a substantially huge antibody diversity produced to one single antigen target. Edwards provides evidence that over 1000 antibodies, all different amino acid sequences, were generated towards one single protein antigen target (see abstract). Without a correlation between structure and function, the claims do little more than define the claimed invention by function. That is not sufficient to satisfy the written description requirement. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406 (“definition by function … does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is”).
Applicant has not described the claimed invention sufficiently to show they had possession of the claimed genus of antibodies that bind MASP-2. 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 v. G.D. Searle & Co., 358 F.3d 916, 69 USPQ2d 1886 (Fed. Cir. 2004).
To provide adequate written description and evidence of possession of the claimed genus, the specification must provide sufficient distinguishing identifying characteristics of the genus. The factors to be considered include disclosure of complete or partial structure, physical and/or chemical properties, functional characteristics, structure/function correlation, methods of making the claimed product, or any combination thereof. In the instant case, the only factors present in the claims are a recitation of one generic, broad genus that encompassed a diverse and huge number of possible antibodies and other agents that bind the disclosed epitope. The specification does not provide a consistent structure for all of the possible antibodies and fails to provide a representative number of species for the claimed genus. Accordingly, in the absence of sufficient recitation of distinguishing identifying characteristics, the specification does not provide adequate written description of the claimed genus.
Satisfactory disclosure of a "representative number" depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features of the elements possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only 20 species within the genus.
For claims drawn to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). The recitation of a functional property alone, which must be shared by the members of the genus, is merely descriptive of what the members of the genus must be capable of doing, not of the substance and structure of the members. The Federal Circuit has cautioned that, for claims reciting a genus of antibodies with particular functional properties (e.g., high affinity, neutralization activity, competing with a reference antibody for binding), “[c]laiming antibodies with specific properties, e.g., an antibody that binds to human TNF-α with A2 specificity, can result in a claim that does not meet written description even if the human TNF-α protein is disclosed because antibodies with those properties have not been adequately described." Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875, 1877-78 (Fed. Cir. 2011). An antibody described only by functional characteristic, such as antibody that binds MASP-2, without any known or disclosed correlation between that function and the structure of the sequence, is not a sufficient identifying characteristic for written description purposes, even when accompanied by a method of obtaining the biomolecule of interest. In re Bell, 991 F.2d 781, 26 U.S.P.Q.2d 1529 (Fed. Cir. 1993). In re Deuel, 51 F.3d 1552, 34 U.S.P.Q.2d 1210 (Fed. Cir. 1995).
With the exception of specifically disclosed antibodies with specific CDRs, the skilled artisan cannot envision the detailed chemical structure of all of the encompassed antibodies, 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 product 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. Applicant is reminded that Vas-Cath makes clear that the written description provision of 35 U.S.C. §112 is severable from its enablement provision (see page 1115).
Given the vast structural diversity of compounds encompassed by the recited genus of inhibitors, and in the absence of a disclosure of a representative number of species falling within the scope of the genus, or of a description of sufficiently detailed, relevant identifying characteristics, such as complete or partial structure, other physical and/or chemical properties, functional characteristics coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics, the skilled artisan cannot envision the range of compounds encompassed by the instant claims, based upon the knowledge in the art and the disclosure provided in the specification as filed. See MPEP 2163. Consequently, Applicant is not in possession of the method of using the genus of the claimed MASP-2 inhibitor agents.
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.
(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 1-7 and 9 are rejected under 35 U.S.C. 102(a)(1) and 102 (a)(2) as being anticipated by US 20120225056, published September 6, 2012 (“Rother”; see instant PTO-892).
Rother teaches compositions and methods for treating complement-associated disorders (see abstract), including Degos disease [0019], which reads on instant claim 1. The compositions comprise an inhibitor of human complement, including antibodies directed against MASP-2 ([0090]-[0091]), which reads on the MASP-2 inhibitory agent of instant claim 1 and the anti-MASP-2 antibody of instant claim 2. As there is no evidence to the contrary that the antibody of Rother does not bind the epitope of instant SEQ ID NO: 6, Rother anticipates the antibody of instant claim 3.
Rother teaches that anti-C5 antibodies, which inhibit terminal complement formation [0093], can be used in combination with other therapies [0179], which reads on the limitations of instant claim 4-5 directed to administering a terminal complement inhibitor with a MASP-2 inhibitor agent. The anti-C5 antibody may be humanized or be eculizumab [0024], which reads on instant claims 6-7
The pharmaceutical compositions can be administered subcutaneously, intravenously, intra-arterially, intranasally, or intramuscularly ([0138]; [0227]), which reads on the modes of administration of instant claim 9.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 as of the effective filing date of the claimed invention(s) 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 as of the effective filing date of the later invention 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 1-9 are rejected under 35 U.S.C. 103 as being unpatentable over US 20120225056, published September 6, 2012 (“Rother”) in view of US 20070172483, published July 26, 2007 (“Schwaeble”; see IDS from 11/8/2023, CU079).
The teachings of Rother are discussed above. Rother does not teach the limitation of instant claim 8 directed to an anti-MASP-2 antibody selected from the group consisting of a recombinant antibody, an antibody having reduced effector function, a chimeric antibody, a humanized antibody, and a human antibody.
Schwaeble teaches anti-MASP-2 antibodies and methods for inhibiting MASP-2-dependent complement activation (abstract). Schwaeble teaches monoclonal antibodies that bind to MASP-2 and inhibit MASP-2 dependent complement activation [0021], as in the inhibitory agent of instant claim 1 and the anti-MASP-2 antibody of instant claim 2. Instant SEQ ID NO: 6 is identical to SEQ ID NO: 6 of Schwaeble, which is the mature form of human MASP-2 protein [0088]. SEQ ID NO: 6 may be used to induce anti-MASP-2 antibodies useful in the method of treating [0320], as in instant claim 3. The anti-MASP-2 antibody of Schwaeble may be recombinant, chimeric, or humanized [0139], as in instant claim 8.
The antibody of Schwaeble encompasses recombinant antibodies, humanized antibodies, and chimeric antibodies [0139], as in instant claim 8.
The antibody of Schwaeble may be administered subcutaneously, inhalational, intra-arterially, intravenously, or intramuscularly [0169], as in instant claim 9.
Given that Rother teaches a method of inhibiting complement activation by administering an anti-MASP-2 antibody in Degos disease and further given that Schwaeble teaches recombinant, humanized, and chimeric anti-MASP-2 antibodies for the treatment of MASP-2 dependent complement activation, it would have been obvious to one of ordinary skill in the art to replace the anti-MASP-2 antibody of Rother with the recombinant, humanized, or chimeric anti-MASP-2 antibody of Schwaeble. One of ordinary skill in the art would have been able to carry out such a substitution, and the results would have been reasonably predictable. As is stated in MPEP §2144.06, substituting one equivalent element for another known for the same purpose renders an invention obvious and an “express suggestion to substitute one equivalent component or process for another is not necessary to render such substitution obvious. In re Fout, 675 F.2d 297, 213 USPQ 532 (CCPA 1982)."
Furthermore, although Schwaeble teaches a method of inhibiting MASP-2-dependent complement activation in a subject (see abstract, [0020]-[0023], [0036],[0317]), Schwaeble does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of Schwaeble, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and It would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
Claims 1-3 and 8-9 are rejected under 35 U.S.C. 103 as being unpatentable over US 20070172483, published July 26, 2007 (“Schwaeble”).
Schwaeble teaches anti-MASP-2 antibodies and methods for inhibiting MASP-2-dependent complement activation (abstract). Schwaeble teaches monoclonal antibodies that bind to MASP-2 and inhibit MASP-2 dependent complement activation [0021], as in the inhibitory agent of instant claim 1 and the anti-MASP-2 antibody of instant claim 2. Instant SEQ ID NO: 6 is identical to SEQ ID NO: 6 of Schwaeble, which is the mature form of human MASP-2 protein [0088]. SEQ ID NO: 6 may be used to induce anti-MASP-2 antibodies useful in the method of treating [0320], as in instant claim 3. The anti-MASP-2 antibody of Schwaeble may be recombinant, chimeric, or humanized [0139], as in instant claim 8.
The antibody of Schwaeble encompasses recombinant antibodies, humanized antibodies, and chimeric antibodies [0139], as in instant claim 8.
The antibody of Schwaeble may be administered subcutaneously, inhalational, intra-arterially, intravenously, or intramuscularly [0169], as in instant claim 9.
Although Schwaeble teaches a method of inhibiting MASP-2-dependent complement activation in a subject (see abstract, [0020]-[0023], [0036],[0317]), Schwaeble does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of Schwaeble, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and It would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claim 1-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4-14 of U.S. Patent No. 8,951,522. Although the claims at issue are not identical, they are not patentably distinct from each other because they are both directed to overlapping embodiments: method for inhibiting MASP-2 dependent complement activation in subjects with an inhibitory anti-MASP-2 antibody.
Claims of ‘522 are directed to a method of inhibiting MASP-2-dependent complement activation in a subject suffering from paroxysmal nocturnal hemoglobinuria by administering a MASP-2 antibody that binds to a portion of SEQ ID NO: 6, wherein the subject has previously undergone or is currently undergoing treatment with an anti-C5 antibody. The anti-MASP-2 antibody may be a recombinant antibody, an antibody having reduced effector function, a chimeric antibody, a humanized antibody, or a human antibody, and the antibody may be administered subcutaneously, intramuscularly, intraarterially, intravenously, or as an inhalant.
‘522, however, does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of ‘522, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and it would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
The scope of the ‘522 claims fully overlaps with the instant claims, and thus, it would have been obvious to one of ordinary skill in the art that the methods of treating disease associated with elevated MASP-2 complement activation are not patentably distinct from each other.
Claim 1-3 and 8-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 of U.S. Patent No. 11,525,011. Although the claims at issue are not identical, they are not patentably distinct from each other because they are both directed to overlapping embodiments: method for inhibiting MASP-2 dependent complement activation in subjects with an inhibitory anti-MASP-2 antibody.
Claims of ‘011 are directed to a method of inhibiting MASP-2-dependent complement activation in a subject suffering from catastrophic antiphospholipid syndrome by administering a MASP-2 antibody that binds to a portion of SEQ ID NO: 6. The anti-MASP-2 antibody may be a recombinant antibody, an antibody having reduced effector function, a chimeric antibody, a humanized antibody, or a human antibody, and the antibody may be administered subcutaneously, intramuscularly, intraarterially, intravenously, or as an inhalant.
‘011, however, does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of ‘011, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and it would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
The scope of the ‘011 claims fully overlaps with the instant claims, and thus, it would have been obvious to one of ordinary skill in the art that the methods of treating disease associated with elevated MASP-2 complement activation are not patentably distinct from each other.
Claim 1-3 and 8-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 12-15 of U.S. Patent No. 9,644,035. Although the claims at issue are not identical, they are not patentably distinct from each other because they are both directed to overlapping embodiments: method for inhibiting MASP-2 dependent complement activation in subjects with an inhibitory anti-MASP-2 antibody.
Claims of ‘035 are directed to a method of inhibiting MASP-2-dependent complement activation in a subject suffering from atypical hemolytic uremic syndrome by administering a MASP-2 antibody that binds to a portion of SEQ ID NO: 6. The anti-MASP-2 antibody may be a recombinant antibody, a humanized antibody, or a human antibody, and the antibody may be administered subcutaneously.
‘035, however, does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of ‘035, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and it would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
The scope of the ‘035 claims fully overlaps with the instant claims, and thus, it would have been obvious to one of ordinary skill in the art that the methods of treating disease associated with elevated MASP-2 complement activation are not patentably distinct from each other.
Claim 1-3 and 8-9 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4, and 6-8 of U.S. Patent No. 7,919,094. Although the claims at issue are not identical, they are not patentably distinct from each other because they are both directed to overlapping embodiments: method for inhibiting MASP-2 dependent complement activation in subjects with an inhibitory anti-MASP-2 antibody.
Claims of ‘094 are directed to a method of inhibiting MASP-2-dependent complement activation in a subject suffering from age-related macular degeneration by administering a MASP-2 antibody that binds to a portion of SEQ ID NO: 6. The anti-MASP-2 antibody may be a recombinant antibody, a humanized antibody, or a human antibody.
‘094, however, does not explicitly teach inhibition of MASP-2-dependnet complement activation in a subject suffering from Degos disease, as required by instant claim 1. However, it would have been obvious to one of ordinary skill in the art that a method of inhibiting MASP-2-dependent complement activation in a subject suffering from MASP-2-dependent complement activation that contributes to the pathogenesis of disease could also be applied to Degos disease. Based on the teachings of ‘094, the ordinary artisan would immediately envision the treatment of other disorders associated with MASP-2-dependent complement activation, and it would be obvious that treatment with an inhibitor of MASP-2 described for one disease would be applicable to another disease associated with the same defect; applying a known technique to a known disease ready for improvement will yield predictable results (see MPEP 2143).
The scope of the ‘094 claims fully overlaps with the instant claims, and thus, it would have been obvious to one of ordinary skill in the art that the methods of treating disease associated with elevated MASP-2 complement activation are not patentably distinct from each other.
Conclusion
No claim is allowed.
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Jennifer Benavides
Examiner
Art Unit 1675
/JENNIFER A BENAVIDES/Examiner, Art Unit 1675