DETAILED ACTION
Notice of Pre-AIA or AIA Status
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2. Under reconsideration, the examiner has extended the search to cover the following species: SEQ ID NO: 157, SEQ ID NO: 310, SEQ ID NO: 313, SEQ ID NO: 315, SEQ ID NO: 317, SEQ ID NO: 318, SEQ ID NO: 320, SEQ ID NO: 324, SEQ ID NO: 326, SEQ ID NO: 331, SEQ ID NO: 334, SEQ ID NO: 336, SEQ ID NO: 339, SEQ ID NO: 341, SEQ ID NO: 349, SEQ ID NO: 350, SEQ ID NO: 352, SEQ ID NO: 572, and SEQ ID NO: 609.
Status of Claims
3. Applicant’s Response to Non-Final Rejection received 06/24/2026 is acknowledged.
4. Claims 32-35, 44, 50, 52, 56, and 59-90 are pending in the instant application.
5. Claims 1-31, 36-43, 45-49, 51, 53-55, and 57-58 have been cancelled.
6. Claims 59-90 are new.
7. Applicant’s election of Group 1, claims 1-2, 4, 6, 8-11, 14-17, and 28 (now claims 59-69, and 81-85) drawn to isolated antibody fragments, polypeptides comprising them, and compositions comprising them and the species of SEQ ID NO: 322 and (AB)n motif in the reply filed on 10/06/2025 is maintained. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
8. Claims 32-35, 44, 50, 52, 56, 70-80, and 86-90 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species or nonelected group, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 10/06/2025.
9. Claims 59-69 and 81-85 are under consideration as they read on SEQ ID NO: 157, SEQ ID NO: 310, SEQ ID NO: 313, SEQ ID NO: 315, SEQ ID NO: 317, SEQ ID NO: 318, SEQ ID NO: 320, SEQ ID NO: 322, SEQ ID NO: 324, SEQ ID NO: 326, SEQ ID NO: 331, SEQ ID NO: 334, SEQ ID NO: 336, SEQ ID NO: 339, SEQ ID NO: 341, SEQ ID NO: 349, SEQ ID NO: 350, SEQ ID NO: 352, SEQ ID NO: 572, and SEQ ID NO: 609 and (AB)n motif.
Information Disclosure Statement
10. The information disclosure statement (IDS) submitted on 06/24/2026 is acknowledged and the references cited therein have been considered.
Priority
11. The present application is a 371 National Stage Application of PCT International Application No. PCT/EP2021/057946, filed 03/26/2021, which claims the benefit of Great Britain Patent Application No. GB2008095.8, filed 05/29/2020, and Great Britain Patent Application No. GB2004462.4, filed 03/27/2020. Applicant' s claim for the benefit of prior-filed application is acknowledged.
Response to Arguments
Rejections under 35 U.S.C. § 112
12. Applicant’s arguments filed on 06/24/2026 with respect to the rejections under 35 U.S.C. § 112(a) have been fully considered and are persuasive. The rejections of failing to comply with written description requirement and lacking enablement are now moot because all of the previously rejected claims have been cancelled. The rejections have been withdrawn.
Rejections under 35 U.S.C. § 102
13. Applicant’s arguments filed on 06/24/2026 with respect to the rejections under 35 U.S.C. § 102 have been fully considered and are persuasive. The art rejections are now moot because all of the previously rejected product claims have been cancelled. The rejections have been withdrawn.
Rejections under 35 U.S.C. § 103
14. Applicant’s arguments filed on 06/24/2026 with respect to the rejections under 35 U.S.C. § 103 have been fully considered and are persuasive. The art rejections are now moot because all of the previously rejected product claims have been cancelled. The rejections have been withdrawn.
New Rejections
15. The following new ground of rejections are necessitated by the amendment and new claims submitted 06/24/2026.
Claim Rejections - 35 USC § 112
Enablement
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.
16. Claims 59-65, 67-69, and 81-85 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for SEQ ID NO: 157, SEQ ID NO: 310, SEQ ID NO: 313, SEQ ID NO: 315, SEQ ID NO: 317, SEQ ID NO: 318, SEQ ID NO: 320, SEQ ID NO: 322, SEQ ID NO: 324, SEQ ID NO: 326, SEQ ID NO: 331, SEQ ID NO: 334, SEQ ID NO: 336, SEQ ID NO: 339, SEQ ID NO: 341, SEQ ID NO: 349, SEQ ID NO: 350, SEQ ID NO: 352, SEQ ID NO: 572, and SEQ ID NO: 609 binding to C5 of the Complement, does not reasonably provide enablement for more. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make or use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required to practice the claimed invention are summarized In re Wands (858 F2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988)). The factors most relevant to this rejection are the scope of the claim, the amount of direction or guidance provided, the lack of sufficient working examples, the unpredictability in the art and the amount of experimentation required to enable one of skill in the art to practice the claimed invention.
Though the term ‘knob domain peptide’ of claim 59 is defined in the instant specification, it is overly broad and therefore not enabled to be made or used. For example, the specification does not specify a means of production for the knob domain peptide (simply states that an ‘isolated antibody fragment may be produced recombinantly or synthetically’), which would entail undue experimentation.
The claims are directed to a broad genus of knob domain peptides and that class is defined by its function – the ability to bind an antigen of interest/C5/Human Serum Albumin. However, the specification did not give the skilled in the art enough information to choose candidate bovine ultralong HCDR3 knob domain peptides from the millions of options and therefore required scientists to engage in a great deal of experimentation and failure. “That is not enablement” – it is a “hunting license”.
In Sanofi-Aventisub, the Federal Circuit relied on its prior precedential opinions when determining whether the full scope of a genus was enabled. These decisions included McRO, Inc. v. Bandai Namco Games Am. Inc., 959 F.3d 1091 (Fed. Cir. 2020) (hereafter McRO); Wyeth & Cordis Corp. v. Abbott Laboratories, 720 F.3d 1380 (Fed. Cir. 2013) (hereafter Wyeth); Enzo Life Sciences, Inc. v. Roche Molecular Systems, Inc., 928 F.3d 1340 (Fed. Cir. 2019) (hereafter Enzo); and Idenix Pharmaceuticals LLC v. Gilead Sciences Inc., 941 F.3d 1149 (Fed. Cir. 2019) (hereafter Idenix).
The Federal Circuit, citing McRO, provided guidance on the application of enablement to genus claims, holding that “[a]lthough a specification does not need to describe how to make and use every possible variant of the claimed invention, when a range is claimed, there must be reasonable enablement of the scope of the range.” Sanofi-Aventisub 987 F.3d at 1085 (internal quotations omitted). Additionally, the Federal Circuit characterized Wyeth as holding “that due to the large number of possible candidates within the scope of the claims and the specification’s corresponding lack of structural guidance, it would have required undue experimentation to synthesize and screen each candidate to determine which compounds in the claimed class exhibited the claimed functionality.” Id. at 1086. Similarly, the Federal Circuit characterized Enzo as holding “that the specification failed to teach one of skill in the art whether the many embodiments of the broad claims would exhibit that required functionality.” Id. Finally, the Federal Circuit characterized Idenix as affirming “the district court’s determination that the claims had both structural and functional limitations, and that undue experimentation would have been required to synthesize and screen the billions of possible compounds because, given a lack of guidance across that full scope, finding functional compounds would be akin to finding a ‘needle in a haystack.’ “ Id.
This case is akin to the issue in Sanofi-Aventisub, the court relied on evidence showing that the scope of the claims encompassed millions of antibodies and that it was necessary to screen each candidate antibody in order to determine whether it met the functional limitations of the claim. Id. at 1088. Consequently, the Federal Circuit concluded that there was a lack of enablement. While the specification in Amgen identified 26 exemplary antibodies that performed the claimed function by their amino acid sequences, the claims at issue were directed to a class that included “a ‘vast’ number of additional antibodies” that Amgen had not described by their amino acid sequences. Id. at 1256. The Supreme Court found that Amgen sought to monopolize an entire class of antibodies by their function, which was much broader than the 26 exemplary antibodies disclosed by their amino acid structure. In the instant case, the specification discloses K8, K57, K60, K92, K136, and K149 that bind human/mouse/rabbit C5 species that perform the claimed function by their amino acid sequences, with the claimed genus of millions of different knob domain peptides which bind an antigen of interest/C5/HSA. The instant claims are directed to a class of bovine ultralong HCDR3 anti-antigen/C5/HSA knob domain peptides which include “a ‘vast’ number of additional…” species that the instant specification fails to describe their amino acid sequences.
The scope of the instant claims encompasses millions of bovine ultralong HCDR3 anti-antigen/C5/HSA knob domain peptides and that it was necessary to first generate and then screen each candidate to determine whether it met the functional limitations. The Federal Circuit concluded that there was a lack of enablement, which was affirmed by the Supreme Court in Amgen.
The claims simply direct skilled artisans to engage in the same iterative, trial-and-error process the inventors followed to discover the knob domain peptides they elected to disclose and that “[u]nder Amgen, such random trial-and-error discovery, without more, constitutes unreasonable experimentation that falls outside the bounds required by § 112(a).” Id. at *8, *10.
Amgen attempted to claim an entire class of compounds by their function, namely antibodies that bind to the “sweet spot” of PCSK9 thereby inhibiting it from binding to LDL, while only describing 26 amino acid sequences in the specification. The two processes, the “roadmap” and “conservative substitution” did not save Amgen. According to the Court, these amounted to “little more than two research assignments” which forced scientists to conduct “painstaking experimentation” to see what worked. (citing Incandescent Lamp). The Court therefore held that Amgen’s specification did not enable the claims.
In terms of binding an ‘antigen of interest’ – at its broadest, this language would be taken to mean any antigen of interest. This is not enabled in the specification, as the instant specification is only enabled for two specific antigens of interest (C5 of the Complement, and human serum albumin).
In the context of comprising a bridging moiety between two amino acids, instant claim 83 is not enabled due to breadth of the claim.
Instant claims 84-85 recite “wherein the knob domain peptide is fused to one or more effector molecule(s)”, and “wherein the one or more effector molecule(s) are selected from: (i) an antibody; (ii) a Fc polypeptide, (iii) a group consisting of a full IgG, a Fab, a VHH, a VH, a VL, a scFv, and a dsscFv; (iv) an albumin binding domain; or (v) albumin or a protein comprising an albumin binding domain.”, respectively. These claims are also not enabled due to breadth of the claim, and that very little direction or guidance is presented for one of skill in the art.
Reasonable correlation must exist between the scope of the claims and scope of the enablement set forth. In view on the quantity of experimentation necessary, the limited working examples, the nature of the invention, the state of the prior art, the unpredictability of the art and the breadth of the claims, it would take undue trials and errors to practice the claimed invention.
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.
17. Claims 59-65, 67-69, and 81-85 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.
Claim 59 encompasses a broad genus of knob domain peptide of a bovine ultralong CDR-H3, wherein the knob domain peptide binds to an antigen of interest and consists of the sequence of formula (I), wherein: (i) C represents one cysteine residue; (ii) Z1 is present or absent, and when Z1 is present, Z1 represents 1 amino acid or 2, 3, 4, or 5 independently selected amino acids; (iii) X1 is present or absent, and when X1 is present, X1 is any amino acid residue; (iv) X2 is an amino acid selected from the list consisting of proline, arginine, histidine, lysine, glycine, and serine; (v) Z2 is present or absent, and when Z2 is present, Z2 represents 1 amino acid or 2, 3, 4, or 5 independently selected amino acids; (vi) n2, n4, n6, n8, n10, n12, n14, and n16 are independently 0 or 1; (vii) Y represents any amino acid or any sequence of amino acids that may be the same or different, and n1, n3, n5, n7, n9, n11, n13, n15, and n17 represent the number of amino acids in Y, and are independently selected from 0 to 22, and at least one of n1, n3, n5, n7, n9, n11, n13, n15, and n17 is not equal to 0; (viii) X3 is present or absent, and when X3 is present, X3 represents any amino acid; and wherein the knob domain peptide is between 15 and 55 amino acids in length.
Claim 60 encompasses a subgenus of knob domain peptide, claiming the knob domain peptide of claim 59, wherein: (iii) X1 is present and X1 is an amino acid selected from the list consisting of serine, threonine, asparagine, alanine, glycine, proline, histidine, lysine, valine, arginine, isoleucine, leucine, phenylalanine, and aspartic acid; and/or (vii) n1, n3, n5, n7, n9, n11, n13, n15, and n17 represent the number of amino acids in Y, and are independently selected from 1 to 15; and/or (viii) X3 is present and X3 represents an amino acid selected from the list consisting of leucine, serine, glycine, threonine, tryptophan, asparagine, tyrosine, arginine, isoleucine, aspartic acid, histidine, glutamic acid, valine, and proline.
Claim 61 encompasses a subgenus of knob domain peptide, claiming the knob domain peptide of claim 59, wherein the knob domain peptide comprises a (Z1) X1 C X2 motif at its N-terminal extremity, wherein: (i) C is cysteine; (ii) Z1 is present or absent, and when Z1 is present, Z1 represents 1 amino acid or 2, 3, 4, or 5 independently selected amino acids; (iii) X1 is any amino acid residue; and (iv) X2 is an amino acid selected from the list consisting of proline, arginine, histidine, lysine, glycine, and serine.
Claim 62 encompasses a subgenus of knob domain peptide, wherein the knob domain peptide consists of the sequence of formula (IV), wherein Z1, X1, C, X2, Y, n1, n3, n5, n7, n9, X3, and Z2 are as defined in claim 59.
Claim 63 claims the knob domain peptide of claim 62, wherein n1=2 to 9 and/or n3=1 to 10 and/or n5=2 to 9 and/or n7=1 to 15 and/or n9=1 to 14.
Claim 64 depends from claim 59, wherein the knob domain peptide consists of the sequence of formula (IVd), wherein Z1, X1, C, X2, Y, n1, n3, n5, n9, X3, and Z2 are as defined in claim 59.
Claim 65 encompasses a subgenus of knob domain peptides that comprises from 20 up to 55 amino acids in length.
Claims 67-69, and 81 are included because they depend from claim 59.
Claims 82-84 are included because they depend from claim 81, which depends from claim 59.
Claim 85 is included because it depends from claim 84, which depends from claim 81, which depends from claim 59.
However, there does not appear to be an adequate written description in the specification as-filed of the essential structural feature that provides the recited function of knob domain peptides binding any antigen/C5/HSA. The Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, first paragraph “Written Description” Requirement make clear that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the genus.
The claims encompass a broad genus of knob domain peptides that bind to a broad genus of antigen.
The USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018.
See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf.
The Memo clarifies the applicability of USPTO guidance regarding the written description requirement of 35 U.S.C. § 112(a) concerning the written description requirement for claims drawn to antibodies, including the following.
“In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional”.
In contrast to applicant’s reliance of describing the epitope of an antigen of interest rather than providing a fully characterized antigen / specific epitope as wells as claiming structural elements of the antigen, Complement C5 and human serum albumin, there is insufficient written description of the required kind of structure-identifying information about the corresponding makeup of the claimed bovine ultralong HCDR3 knob domain peptides that bind antigen to demonstrate possession. Also, see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017).
There is no evidence that knowledge of the chemical structure of an antigen gives the required kind of structure identifying information about the corresponding bovine ultralong HCDR3 knob domain peptides. Applicant attempts to describe the invention by describing something that is not the invention: viz., the antigens to which the peptides may bind. There is nothing in the disclosure that describes the peptides as required by the test set forth in Ariad.
However, the anti-antigen/C5/HSA peptides are required to practice the invention. The specification fails to provide any specific structural or physical information so as to define a genus of peptides having the desired therapeutic properties. Applicant is merely relying on the identification of antigen/C5/HSA as the antigen and the well-known structure of bovine ultralong HCDR3 knob domain peptides in general.
“When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus.” (Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005)).
“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).
Possession is not shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. Sufficient description to show possession of such a genus may be achieved by means of a recitation of a representative number of bovine ultralong HCDR3 knob domain peptides, portions or variants falling within the scope of the genus or of a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
With respect to a representative number of species of the claimed genus of bovine ultralong HCDR3 knob domain peptides that bind a genus of antigens – with respect to a representative number of species, see Abbvie Deutschland GmbH & Co. v. Janssen Biotech, Inc. (Fed. Cir. 2014)
Also, see MPEP 2163 II(A)(3)(a)(ii):
A representative number of species means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See Abbvie Deutschland GmbH & Co., KG v. Janssen Biotech, Inc., 759 F.3d 1285, 1300, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (Claims directed to a functionally defined genus of antibodies were not supported by a disclosure that “only described one type of structurally similar antibodies” that “are not representative of the full variety or scope of the genus.”).
The instant specification discloses six primary examples: K8, K57, K60, K92, K136, and K149 (see pages 114-118 of the instant specification). The Applicant discloses the amino acid sequences of K8 (SEQ ID NO: 322), K57 (SEQ ID NO: 334), K60 (SEQ ID NO: 336), K92 (SEQ ID NO: 317), K136 (SEQ ID NO: 339), and K149 (SEQ ID NO: 313). Each of the knob domain peptides bound human C5 with high affinity, except K60 (see Table 11, page 118). Both K8 and K92 were cross reactive to mouse and rabbit C5 as well (see Table 12, page 119).
It is noted that the broadest claim (claim 59) does not indicate a specific structure or specific antigen for the genus of knob domain peptides claimed. There is no structure/function correlation.
Regarding state of the art, it has been well established that there is extensive diversity in the cow ultralong HCDR3 knob domain peptide repertoire, especially in terms of structure (see Haakenson et al., Front. Immunol. 9:1262;1-10 (2018), IDS NPL Reference #2, Submitted 9/23/2022, and Wang et al., Cell June 6; 153(6): 1379-1393 (2013), IDS NPL Reference #7, Submitted 9/23/2022). As such, it does not seem possible to predict the sequence/structure of a knob domain peptide that binds a given antigen, as there does not appear to be common or core structure present within all fragments that gives rise to the function of antigen binding. Taken together, the art suggests that identifying isolated knob domain peptides of bovine ultralong CDRH3 origin which bind a specific antigen is highly unpredictable. Further, given such data as that of Haakenson et al. and Wang et al., no number of representative species appears to be reasonably representative of the breadth of the genus of knob domain peptides that bind the given antigen (C5 of the Complement and human serum albumin, in the instant case).
From Haakenson et al.: “Although these ultralong CDR H3 antibodies share the general “stalk & knob” scaffold, each antibody also possesses distinct structural variations in the CDR H3 (Figure 1C). These structural variations are reflected in differences in the length of the stalk and the orientation of the knob relative to the rest of the antibody structure (25). For example, the stalk length of BLV1H12 is the longest among these five antibodies, while the stalk length of A1 is the shortest (25). When the five Fab structures are superimposed by the shared type I β-turn and the three antiparallel β strands in the knob region, obvious differences in stalk positions are observed, reflecting different knob orientations that are supported by the stalks (25). Furthermore, as the number and positions of cysteine residues in the knob region differ significantly among these cow ultralong antibodies, each of them possesses a knob region with unique disulfide bond patterns (25). Therefore, different stalk lengths, knob orientations, and disulfide bond patterns, in addition to diverse amino acid content within the knob regions of these antibodies provide remarkable structural diversity generated in the bovine ultralong CDR H3 antibody repertoire.” Taken together, any of the listed changes make antigen binding unpredictable.
From Macpherson et al. (PLOS Biology 18(9):1-14 (2020), IDS NPL #3, Submitted 9/23/2022): “From our initial screening with CDRH3-ScFc constructs, we observed a 27% hit rate for C5 binding. While entirely practicable for knob domain discovery, the attrition at this stage may indicate that not all ultralong CDRH3 can function entirely independently of their parent antibody. Previous studies have suggested that the β-ribbon stalk of an ultralong CDRH3 is obligate to orientate the knob domain peptide [6-8, 38]. Inspection of bovine Fab structures in the Protein Data Bank (PDB) frequently reveals stabilising interactions between the knob domain peptide and the β-ribbon stalk, and numerous interactions between the β-ribbon stalk and neighbouring CDRs and VH framework residues [6-8]. In one recent structure (BOV-7, PDB accession code: 6E9U [7]), a disulphide bond was observed between cysteine residues of the stalk and knob domain [7]. Therefore, for certain ultralong CDRH3, removal of the stalk may in turn remove critical interactions required to stabilise the knob domain.” This indicates there is a need to screen for CDRH3s which can independently bind antigen. There is no structure/function correlation.
Thus, one of ordinary skill in the art cannot envision from the disclosed species provided, the breadth of knob domain peptide of the instant invention. Therefore, in view of the breadth of the claims and the limitations of the instant specification, artisans would reasonably conclude that Applicant was not in possession of the full breadth of knob domain peptide encompassed by the claims at the time the instant application was filed.
Allowable Subject Matter
18. Claim 66 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, additionally specifying binding to the antigen C5 of the Complement. Sequences searched: SEQ ID NO: 157, SEQ ID NO: 310, SEQ ID NO: 313, SEQ ID NO: 315, SEQ ID NO: 317, SEQ ID NO: 318, SEQ ID NO: 320, SEQ ID NO: 322, SEQ ID NO: 324, SEQ ID NO: 326, SEQ ID NO: 331, SEQ ID NO: 334, SEQ ID NO: 336, SEQ ID NO: 339, SEQ ID NO: 341, SEQ ID NO: 349, SEQ ID NO: 350, SEQ ID NO: 352, SEQ ID NO: 572, and SEQ ID NO: 609.
Conclusion
19. No claim is allowed.
20. Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
21. Any inquiry concerning this communication or earlier communications from the examiner should be directed to ALAN ALFANO whose telephone number is (571)272-3092. The examiner can normally be reached M-F 8-5 EST.
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/ALAN ALFANO/Examiner, Art Unit 1641
/MAHER M HADDAD/Primary Examiner, Art Unit 1641
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