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 .
Election/Restrictions
Applicant's election with traverse of Group I in the reply filed on 06/10/2026 is acknowledged. The traversal is on the ground(s) that Groups II and III consist of claims directed to processes of using the product of claim 1, and there is no search and examination burden to examine all claims. This is not found persuasive because the instant application was filed under 35 USC 371, and thus the election requirement was made under the unity of invention guidelines, which do not consider search burden when restricting claims. Accordingly, Groups II and III still represent separate inventions under unity of invention (see MPEP §823 and §1893(d))
The requirement is still deemed proper and is therefore made FINAL.
Claims 11-14 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected inventions, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 06/10/2026.
Status of Claims
Claim 15 was previously cancelled, in the amendment filed 06/20/2024. Claims 1-14 are pending. Claims 11-14 are withdrawn. Claims 1-10 will be examined on the merits.
Information Disclosure Statement
The Information Disclosure Statement filed on 10/18/2024 has been considered. Signed copies are enclosed.
Claim Objections
Claims 1-10 are objected to because of the following informalities: each claim recites the phrase "characterized in that". Examiner requests this phrase be replaced with the term "wherein" to more closely resemble standard patent language. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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 8 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Regarding claim 8 , the phrase "such as" renders the claim indefinite because it is unclear whether the limitations following the phrase are part of the claimed invention. See MPEP § 2173.05(d). For the purposes of examination, Examiner will interpret claim 8 requiring any antibody moiety, not only the antibody of claim 1.
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 2 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 2 further limits the antibody of claim 1, characterized in that the antibody has three CDRs and framework regions on both the heavy and light chain of the antibody. This claim simply recites the structural characteristics of an antibody that are inherently present in the antibody of claim 1. It does not define any additional distinguishing features of this antibody, and thus does not further limit claim 1. 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.
Claim 4 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 4 recites a recombinant protein comprising the antibody according to claim 1, and, optionally, a tag sequence. As the tag sequence is optional, the claim can be interpreted as a recombinant protein comprising the antibody of claim 1, which does not further limit the antibody of claim 1. 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 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, 2, and 4-10 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. This is a written description rejection.
The instant claims are drawn to an anti-human MASP-2 antibody or antigen-binding fragment thereof with HCDRs of SEQ ID NOs 21-23, and LCDRs of SEQ ID NOs 18-20, “wherein any one of the amino acid sequences of the antibody or antigen-binding fragment thereof also comprises a derivative sequence that optionally has been added, deleted, modified, and/or substituted by at least one amino acid, and is capable of retaining MASP-2 binding affinity”, as recited in claim 1. Dependent claims 2 and 4-10 recite this antibody and do not provide any further clarification on the antibody sequence.
The instant specification discloses two anti-human MASP-2 antibodies – the claimed antibody, referred to as “169-IgG4” and an anti-MASP-2 antibody known in the art referred to as “Narsoplimab” in Example 2, and Table 1, pages 34-36. The specification does not recite a maximum number of amino acids that can be added, deleted, modified, and/or substituted in the derivative sequence of the claimed antibody, and does not limit which amino acids can be deleted, modified, and/or substituted in the derivative sequence of the claimed antibody. There is no evidence from the disclosure that anti-MASP-2 antibodies with substitutions of any kind within the CDRs or the variable chains of the disclosed antibodies were made. Neither instant claim 1 nor the specification teaches that any particular part of the sequence must be conserved when determining if an antibody comprises a derived sequence that has been added, deleted, modified, and/or substituted by at least one amino acid. Moreover, instant claim 1 recites the derivative sequence is capable of retaining MASP-2 binding affinity, not that the sequence is required to maintain MASP-2 binding affinity. This indicates the antibody must be, at best, able to loosely associate with MASP-2, but does not require that the antibody is able to bind MASP-2 with any particular specificity or strength. The instant specification does not provide an alternate definition of the term “capable of retaining MASP-2 binding affinity”, so this interpretation is deemed within the scope of the instant disclosure.
As is widely accepted in the art, the CDRs of an antibody are considered vital for binding. As claim 1 does not recite that the antibody must have limited or no substitutions in the recited CDRs, one cannot reasonably conclude that the derivative sequence of claim 1 will have the same function (i.e. will antagonize MASP-2) as the antibody with the recited CDRs. Therefore, claim 1 is drawn to a broad genus of antibodies with any substitution within the CDRs or VH regions.
The antibody comprising a VH set forth in Seq ID NO:12 and a VL set forth in SEQ ID NO: 11 (as recited in claim 3), and the antibody with HCDRs 1-3 of SEQ ID NO: 21-23, respectively, and LCDRs 1-3 of SEQ ID NO: 18-20, respectively, (as recited in the first half of instant claim 1) meet the written description requirement of 35 USC §112(a). However, instant claim 1 is drawn more broadly than just this antibody due to the recitation of “wherein any one of the amino acid sequences of the antibody or antigen-binding fragment thereof also comprises a derivative sequence that optionally has been added, deleted, modified, and/or substituted by at least one amino acid, and is capable of retaining MASP-2 binding affinity.” Therefore, claim 1, as written, does not have written description support under 35 USC 112(a). This rejection is inherited by claims 2 and 4-10, which do not provide enough information to overcome this rejection.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that "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." (See page 1117.) The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116.)
To fulfill the written description requirements set forth under 35 U.S.C. 112(a), the specification must describe at least a substantial number of the members of the claimed genus, or alternatively describe a representative member of the claimed genus, which shares a particularly defining feature common to at least a substantial number of the members of the claimed genus, which would enable the skilled artisan to immediately recognize and distinguish its members from others, so as to reasonably convey to the skilled artisan that Applicant has possession of the claimed invention. To adequately describe the genus of antibodies, Applicant must adequately describe which combination of variable regions and framework regions that give rise to an antibody with the claimed immunological function. The instant specification, however, does not disclose distinguishing and identifying features of a representative number of members of the genus of antibodies to which the claims are drawn, such as a correlation between the structure of the antibody and its recited function (binding MASP-2), so that the skilled artisan could immediately envision, or recognize, at least a substantial number of members of the claimed genus of antibodies. The specification fails to disclose which amino acids might be added, replaced, or deleted so that the resultant antibody retains the binding specificity of its parent, or by which other amino acids the essential amino acids might be replaced so that the resultant antibody retains the binding specificity of its parent. Therefore, the specification fails to adequately describe at least a substantial number of members of the genus of antibodies to which the claims refer; and accordingly, the specification fails to adequately describe at least a substantial number of members of the claimed genus of antibodies.
As evidenced by the teachings of Skolnick et al., the art is unpredictable. Skolnick et al. (Trends in Biotechnology (2000) 18:34-39) discloses the skilled artisan is well aware that assigning functional activities for any particular protein or protein family based upon sequence homology is inaccurate, in part because of the multifunctional nature of proteins (see, e.g., the abstract; and page 34, Sequence-based approaches to function prediction). Even in situations where there is some confidence of a similar overall structure between two proteins, only experimental research can confirm the artisan's best guess as to the function of the structurally related protein (see, in particular, the abstract and Box 2). Thus, one skilled in the art would not accept the assertion, which is based only upon an observed similarity in amino acid sequence that a variant of a given polypeptide would necessarily bind to a given antibody.
As stated above, the CDRs are vital for antigen binding, as evidenced by Kapingidza et al. (Vertebrate and invertebrate respiratory proteins, lipoproteins and other body fluid proteins, 2020, 465-497) (see page 468, lines 1-4, and pages 476-482). Sela-Culang et al. (Frontiers in immunology, 2016, 4:302) expands on the importance of antibody sequence and function, explaining that amino acid residues outside of the CDRs can influence antigen binding (abstract, whole document). Additionally, Clark et al. (Journal of Structural Biology, 2014, 185(2), 223-227) show that mutational effects on interfaces are often unpredictable (see pg. 223, 2nd col. 1st full para), and that it is easy to damage an interface and decrease binding affinity. Therefore, a person of ordinary skill in the art at the time of filling would understand residues within the CDRs are integral to antigen binding or maintaining the structure of the region that binds to the antigen and substitutions in these regions would affect one or both these attributes. As there is no art-recognized correlation between structure and function, it would be impossible for one of ordinary skill in the art to predict which variable CDRs, combinations of CDRs, or combinations of particular substitutions, would result in a structure that binds MASP-2.
Overall, based on the disclosure, the state of the art at the time of filing, a skilled artesian would have recognized that the applicant was not in possession of the claimed invention at the time of filing. Consequently, in accordance with the MPEP, only the antibody comprising the amino acid sequences of SEQ ID NOs 11 and 12, or the antibody comprising HCDRs 1-3 of SEQ ID NO: 21-23, respectively, and LCDRs 1-3 of SEQ ID NO: 18-20, respectively, but not the full breadth of claim 1 regarding any derivative sequence that has been added, deleted, modified, and/or substituted by at least one amino acid, meets the written description provision of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph.
Applicant is reminded that Vas- Cath makes clear that the written description provision of 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, is severable from its enablement provision. (See page 1115).
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.
Claim(s) 1, 2, and 4-10 is/are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by US 2012/0282263 A1, Dudler et al., published 11/08/2012.
The instant claims are drawn to an antibody that binds MASP-2 with one or more amino acids added, deleted, modified, and/or substituted from the antibody with HCDRs of SEQ ID NOs: 21-23 and LCDRs of SEQ ID NOs: 18-20, As well as a polynucleotide, a vector, a cell, an antibody conjugate, and a pharmaceutical composition of this antibody. Claim 10 is drawn to a method of using this antibody comprising contacting a sample in vitro with the antibody of claim 1 and detecting if an antigen-antibody complex is formed.
Dudler et al. disclose an anti-human MASP-2 antibody (see abstract, whole document) with a heavy chain of Dudler SEQ ID NO: 20 and a light chain variable region of Dudler SEQ ID NO: 24, in Table 2 and claims 21, 33, 36, and 41-42. As seen in the alignments below, this antibody comprises a derivative sequence that has modified or substitute at least one amino acid, and is disclosed in Dudler et al. as capable of binding MASP-2. Therefore, this antibody meets the limitations of claim 1 as written.
Sequence Alignment 1: instant SEQ ID NO: 12 and Dudler et al. SEQ ID NO: 20
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263
671
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Greyscale
Sequence Alignment 2: instant SEQ ID NO: 11 and Dudler et al. SEQ ID NO: 24
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235
652
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Greyscale
Instant claim 2 redundantly describes an antibody, and is met by the antibody of Dudler et al. (see paragraphs [0162]-[0174] of Dudler et al. for antibody descriptions that match instant claim 2). Additionally, the antibody of Dudler et al. meets all required limitations of claim 4, and additionally discloses a tagged antibody in paragraph [0461], thereby anticipating instant claim 4. Dudler et al. further disclose a polynucleotide, or nucleic acid molecule, encoding the antibody, in claim 45, anticipating instant claim 5. Dudler et al. also disclose an expression cassette comprising the nucleic acid molecule, in claim 46, and a vector that contains the polynucleotide in Example 5, paragraph [0439], anticipating instant claim 6. Both the same example, paragraph [0439], and claim 47 disclose a cell containing this vector, anticipating claim 7. Claim 51 of Dudler et al. discloses a composition comprising the antibody and a pharmaceutically acceptable excipient, anticipating claim 9.
Instant claim 8 is drawn to an antibody conjugate, characterized in that the conjugate contains an antibody moiety and a conjugating moiety, which may be a detectable marker. As recited above, under paragraph 9, the use of “such as the antibody of claim 1” is indefinite and does not necessarily require the antibody of claim 1 to be used in the antibody conjugate of claim 8. As a result, the antibodies used for detection in the examples of Dudler et al. anticipate instant claim 8, such as the HRP-conjugated Rabbit anti-Mouse antibody in paragraph [0378], or the HRP conjugated Goat anti-Human IgG antibody of paragraph [0440]. Finally, Example 12 of Dudler discloses, in paragraph [0577], an ELISA assay wherein the plate is coated with a sample of recombinant human MASP-2, the claimed antibody is added to said sample, and then the bound antibody-antigen complex is detected with HRP-labeled goat anti-human IgG antibody. This experiment anticipates the method of claim 10, as it recites a method of in vitro detection of MASP-2 in a sample comprising contacting the sample in vitro with the anti-MASP-2 antibody and detecting if a complex is formed. Therefore, claims 1, 2, and 4-10 are anticipated by Dudler et al.
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.
Claim(s) 1, 2, and 4-10 are rejected under 35 U.S.C. 103 as being unpatentable over Dudler et al., US 2012/0282263 A1, in view of .
Dudler et al. disclose an anti-human MASP-2 antibody (see abstract, whole document) with a heavy chain of Dudler SEQ ID NO: 20 and a light chain variable region of Dudler SEQ ID NO: 24, in Table 2 and claims 21, 33, 36, and 41-42. As seen in the alignments above, this antibody comprises a derivative sequence that has modified or substitute at least one amino acid, and is disclosed in Dudler et al. as capable of binding MASP-2. Therefore, this antibody meets the limitations of claim 1 as written. Instant claim 2 redundantly describes an antibody, and is met by the antibody of Dudler et al. (see paragraphs [0162]-[0174] of Dudler et al. for antibody descriptions that match instant claim 2). Additionally, the antibody of Dudler et al. meets all required limitations of claim 4, and additionally discloses a tagged antibody in paragraph [0461], thereby teaching instant claim 4. Dudler et al. further disclose a polynucleotide, or nucleic acid molecule, encoding the antibody, in claim 45, teaching instant claim 5. Dudler et al. also disclose an expression cassette comprising the nucleic acid molecule, in claim 46, and a vector that contains the polynucleotide in Example 5, paragraph [0439], anticipating instant claim 6. Both the same example, paragraph [0439], and claim 47 disclose a cell containing this vector, teaching claim 7. Claim 51 of Dudler et al. discloses a composition comprising the antibody and a pharmaceutically acceptable excipient, teaching claim 9. Example 12 of Dudler discloses, in paragraph [0577], an ELISA assay wherein the plate is coated with a sample of recombinant human MASP-2, the claimed antibody is added to said sample, and then the bound antibody-antigen complex is detected with HRP-labeled goat anti-human IgG antibody. This experiment teaches the method of claim 10, as it recites a method of in vitro detection of MASP-2 in a sample comprising contacting the sample in vitro with the anti-MASP-2 antibody and detecting if a complex is formed.
Instant claim 8 is drawn to an antibody conjugate, characterized in that the conjugate contains an antibody moiety and a conjugating moiety, which may be a detectable marker. As recited above, under paragraph 9, the use of “such as the antibody of claim 1” is indefinite and may not require the antibody of claim 1. Nevertheless, Dudler et al. do not disclose a conjugated anti-MASP-2 antibody. However, as reviewed in Beck et al. (Nature Reviews Drug Discovery, (2017) 16(5), 315-337), making antibody drug conjugates are well understood, routine, and conventional in the art. Any antibody may be adapted and conjugated to an effector molecule; the most important factor in antibody design for antibody drug conjugates for treating a disease is the specificity of the antibody for the target antigen (see Figure 1, page 317). Therefore, as instant claim 8 does not claim the conjugated antibody for any specific function, it would be obvious to create any conjugated antibody with the antibody of Dudler et al. One would be motivated to do so in order to target a drug to the complement system MASP-2 is a part of. One would have a reasonable expectation of success because generation of such an antibody is generally known in the art, as seen in Beck et al. Finally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that a claim would have been obvious if the substitution of one known element for another yields predictable results to one of ordinary skill in the art. It would be obvious to apply the known antibody of Dudler et al. for any other antibody to be used in the method of creating a conjugated antibody, a method known in the art, to yield predictable results. Thus, the combination of prior art references as combined provided a prima facie case of obviousness, absent convincing evidence to the contrary.
Therefore, claims 1, 2, and 4-10 are rejected as obvious over Dudler et al. in view of Beck et al.
Allowable Subject Matter
Claim 3 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
The following is a statement of reasons for the indication of allowable subject matter: Claim 3 is drawn to the antibody of instant claim 1, wherein the VH is SEQ ID NO: 12, and the VL is SEQ ID NO: 11. As can be seen above, the sequences of Dudler et al., considered the closest prior art, do not have 100% identity to SEQ ID NO: 12 and SEQ ID NO:11. Therefore, an antibody comprising a VH and a VL as set forth in SEQ ID NO: 12 and 11, respectively, that binds human MASP-2, is free of the art as of the effective filing date of the invention, 12/21/2021.
Examiner also notes that an antibody with the specific CDRs recited in claim 1 (HCDR1 of SEQ ID NO: 21, HCDR2 of SEQ ID NO: 22, HCDR3 of SEQ ID NO: 23, LCDR1 of SEQ ID NO: 18, LCDR2 of SEQ ID NO: 19, and LCDR3 of SEQ ID NO: 20) would also be free of the art, as the antibodies of Dudler et al. are derivative sequences as defined in claim 1, lines 14-17.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Amelia Stephens whose telephone number is (571)272-1006. The examiner can normally be reached M-F 8-5 EST.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Anne Gussow can be reached at (571) 272-6047. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/AMELIA STEPHENS/ Examiner, Art Unit 1645
/ANNE M. GUSSOW/ Supervisory Patent Examiner, Art Unit 1683
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