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 .
Preliminary Amendment
The preliminary amendment dated 03/04/2026 has been entered. Claims 1-32 are pending.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. The earliest possible effective filing date for the instant claims is January 26, 2022 based on the filing date of the provisional application 63/303,067.
Election/Restriction
Applicant’s election with traverse of Group I in the reply filed on 03/04/2026 is acknowledged.
Claims 24-32 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim.
Claims 1-23 are under examination.
Applicant’s species election is acknowledged. Applicant elected the following species within Group I:
- Heavy Chain CDR1: SEQ ID NO: 24; Heavy Chain CDR2: SEQ ID NO: 35 and Heavy Chain CDR3: SEQ ID NO: 61
- Framework Regions (FRs): FR1: SEQ ID NO: 14; FR2: SEQ ID NO: 28; FR3: SEQ ID NO: 43 and FR4: SEQ ID NO: 66
- Heavy Chain: SEQ ID NO: 85
2. The traversal filed by the Applicant is on the grounds that the Groups I to IV are closely related and searching these groups does not substantially increase the search burden.
Applicant’s arguments have been fully considered but are not found persuasive. According to MPEP § 808.02, the examiner must show a serious search burden by appropriate explanation one of the following:
(A) Separate classification thereof: This shows that each invention has attained recognition in the art as a separate subject for inventive effort, and also a separate field of search.
(B) A separate status in the art when they are classifiable together: Even though they are classified together, each invention can be shown to have formed a separate subject for inventive effort when the examiner can show a recognition of separate inventive effort by inventors.
(C) A different field of search: Where it is necessary to search for one of the inventions in a manner that is not likely to result in finding art pertinent to the other invention(s).
The following reasons apply as discussed in the Restriction requirement filed on 09/05/2025:
(a) the inventions or species have acquired a separate status in the art due to their different classification and/or recognized divergent subject matter;
(b) the inventions or species require a different field of search (e.g., searching different classes/subclasses or electronic resources, or employing different search strategies or search queries);
(c) each inventions or species have different issues under 35 U.S.C.112a or 101.
The requirement is still deemed proper and is therefore made FINAL.
Objections
Specification
The disclosure is objected to because of the following informalities:
3. The use of the term(s), e.g., Tween [00160] which are a trade name or a mark used in commerce, has been noted in this application. The terms should be accompanied by the generic terminology; furthermore, the terms should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM, and/or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks. Note that ‘Tween’ is merely an example and all improper uses of trademarks in the specification should be identified by applicant and properly addressed.
Appropriate correction is required.
4. The disclosure is objected to because of the following informalities: At paragraph [0086} sequences are described by reference to Uniprot IDs., which are subject to change, rather than to sequences set forth in the specification. This is an improper incorporation by reference, since the information required to describe and enable the required sequences is found in the Uniprot IDs database, extraneous to the application. Furthermore, since the sequences are not irrevocably fixed but are corrected and updated as additional sequence information becomes available, the accession numbers may refer to sequences which change after the application filing date. Thus, the disclosure is objected to for this improper incorporation by reference.
Furthermore, essential material such as that which provides written description or enablement, as here since the antigen is needed for functional antibody identification, should not come from NPLs. See 37 CFR 1.57d.
Appropriate correction is required.
Claim Rejections – Improper Markush Grouping
5. Claims 1-23 are rejected on the judicially-created basis that they contain an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class, and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of claims 1-23 are improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use that flows from the substantial structural feature for the following reasons:
Claim 1-23 are drawn to an antibody comprising a heavy chain variable region, wherein the heavy chain variable region comprises three complementarity determining regions (CDRs) CDR1, CDR2, and CDR3, wherein the CDR1 is selected from SEQ ID NOs:17- 25, the CDR2 is selected from SEQ ID NOs:30-36, and the CDR3 is selected from SEQ ID NOs:45-63, and wherein the antibody binds a glycoprotein D (gD protein). The antibodies of claim 1 do not share both a single structural similarity or feature (CDRs or FRs) and a common use that flows from the structural feature as shown in Table [00112], page 19. For example, a comparison of some of the Heavy chain CDRs amino acid sequences and their corresponding SEQ ID NOs of Table [00112 is listed in the table:
VH CDR 1
VH-CDR-2
VH-CDR-3
SEQ ID NO:
17
30
45
SFSFKNYA
MSGGGDET
AKGWITTDRFTNTP
SEQ ID NO:
18
32
47
SFSFENYA
MSGGGGDI
AKGWITTNRFTNTP
SEQ ID NO:
21
31
49
SFAFKDYA
MSGGGGDT
AKGWITTNQFADAP
SEQ ID NO:
22
31
52
SFAFKNYA
MSGGGGDT
AEGWITTDQFASAP
SEQ ID NO:
24
35
61
EQFFTTNA
TDWSGQST
ARAPGRVLLTSDLESYTI
The antibodies of claim 1 have distinct CDR set amino acid sequences thus will bind different epitopes. The claims recite discrete antibody binding domains and do not all share significant structural similarity since it is the entire CDR set that is required to bind antigen. This is evidenced by the fact that even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff (Proc Natl Acad Sci USA 1982 Vol 79 page 1979). Rudikoff teaches that the alteration of a single amino acid in a single CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (entire article, Abstract).
Although only a few VH CDRs are used as an example, an artisan would understand that the sequence differences in the CDRs overall would amount to structural differences in the antibody binding region as a whole, and therefore there would be no structural similarity between the antibodies leading to be functionally equivalent and to their common use.
Lastly, while the claims recite “an antibody binding a glycoprotein D (gD protein), this is not an art-recognized class of molecules as defined in MPEP 2117 as: that it was known within the art that each member could be substituted one for the other, with the expectation that the same intended result (be functionally equivalent) would be achieved. Therefore, in the instant case, the structurally different antibodies are not art-recognized substitutions for each other.
Dependent claims are rejected for failing to resolve the improper Markush grouping.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 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.
Claims 6, 12-13, 15 and 21 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
6. Claims 6 and 21 recite the limitation "…. comprises an amino acid sequence as set forth in….”. This limitation can be interpreted as a full length sequence or a fragment of the sequence and therefore is indefinite. Recitation’s clarity is improved by the following change: "…. comprises the amino acid sequence as set forth in….”.
7. Claims 12-13 and 15 recite the term “about” which is subjective and a relative term. It is unclear the extend of the ranges included in the term “about” based on the very broad definition in the specification, which also depends on the context [0044} and therefore, this claim is indefinite.
Appropriate correction is required.
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.
8. Claims 1 and 5-23 are rejected under 35 U.S.C. 112(a) because the specification, while being enabling for the elected monoclonal VHH antibody, (VHH being SEQ ID NO: 85 (which is antibody G75, Table 3) comprising HCDR1: SEQ ID NO: 24; HCDR2: SEQ ID NO: 35 and HCDR3: SEQ ID NO: 61 and FR1: SEQ ID NO: 14; FR2: SEQ ID NO: 28; FR3: SEQ ID NO: 43 and FR4: SEQ ID NO: 66), binding to the gD protein of HSV-1 does not reasonably provide enablement for any kind of antibody (“antibody” refers to any immunoglobulin (Ig) molecules) comprising a VH region comprising all the possible combinations of the CDRs that can be obtained when the CDR1 is selected from SEQ ID NOs:17- 25, the CDR2 is selected from SEQ ID NOs:30-36, and the CDR3 is selected from SEQ ID NOs:45-63, with a VH region being at least 80% identical sequence and still be able to bind any gD protein. 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.
Claims 1 and 5-23 are drawn to/recite an antibody comprising a heavy chain variable region, wherein the heavy chain variable region comprises three complementarity determining regions (CDRs) CDR1, CDR2, and CDR3, wherein the CDR1 is selected from SEQ ID NOs:17- 25, the CDR2 is selected from SEQ ID NOs:30-36, and the CDR3 is selected from SEQ ID NOs:45-63, and wherein the antibody binds a glycoprotein D (gD protein).
The specification discloses the immunization of a llama with inactivated HSV-1 gD protein (specification, example 3) and a construction of a phage display library ((specification, example 5) and its characterization ((specification, examples 6-8). Expression and purification of soluble VHH is shown in specification, example 9. Size Exclusion Chromatography (SEC) and Surface Plasmon Resonance (SPR) Analysis is shown in specification, example 10. Specification, Table 6 shows the Kinetic Analysis Data and specification, Example 11 In Vitro Neutralization Assays for monoclonal VHH antibodies for the elected antibody (VHH being SEQ ID NO: 85 (which is antibody G75, Table 3), (Tables 4-6). The specification does not disclose Kinetic Analysis Data and In Vitro Neutralization Assays for all the potential antibodies claimed in the instant application and which ones still retain the binding efficacy to any gD protein.
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.
The claims are directed to a broad class of antibodies, only defined by its function “able to bind any gD protein”, with a partial structure at best. However, the specification did not give the skilled in the art enough information to choose candidate antigen binding structures from the vast number of options of thousands of candidates, and therefore required scientists to engage in a great deal of experimentation and failure. “That is not enablement”—it is a “hunting license.”
The specification discloses that the elected antibody (SEQ ID NO: 85 (which is antibody G75, Table 3)) is “able to bind HSV-1 gD protein”.
In Amgen Inc. et al. v. Sanofi et al., 598 U.S. 594, 2023 USPQ2d 602 (2023), the Supreme Court held that claims drawn to a genus of monoclonal antibodies, which were functionally claimed by their ability to bind to a specific protein, PCSK9, were invalid due to lack of enablement. The claims at issue were functional, in that they defined the genus by its function (the ability to bind to specific residues of PCSK9) as opposed to reciting a specific structure (the amino acid sequence of the antibodies in the genus). The Supreme Court concluded that the patents at issue failed to adequately enable the full scope of the genus of antibodies that performed the function of binding to specific amino acid residues on PCSK9 and blocking the binding of PCSK9 to a particular cholesterol receptor, LDLR. This decision reaffirmed the prior decision made by the Federal District Court in Amgen Inc. v. Sanofi, Aventisub LLC., 987 F.3d 1080 (Fed. Cir. 2021).
The Court clarified that the specification does not always need to "describe with particularity how to make and use every single embodiment within a claimed class." Id. at 610-11. However, "[i]f a patent claims an entire class of processes, machines, manufactures, or compositions of matter, the patent’s specification must enable a person skilled in the art to make and use the entire class….The more one claims, the more one must enable." Id.
The specification may require a reasonable amount of experimentation to make and use the invention and what is reasonable will depend on the nature of the invention and the underlying art. For example, "it may suffice to give an example (or a few examples) if the specification also discloses some general quality … running through the class that gives it a peculiar fitness for the particular purpose" and "disclosing that general quality may reliably enable a person skilled in the art to make and use all of what is claimed, not merely a subset." Id. at 611 (internal quotations omitted). However, the Supreme Court found that Amgen failed to enable all that it claimed, even if allowing for a reasonable degree of experimentation. Id. at 613; see also Baxalta Inc. v Genentech, Inc., 81 F.4th 1362, 1367, 2023 USPQ2d 1103 (Fed. Cir. 2023) ("[t]he facts of this case are more analogous to—and are, in fact, indistinguishable from—those in Amgen. We do not interpret Amgen to have disturbed our prior enablement case law, including Wands and its factors."). Moreover, "[w]e see no meaningful difference between Wands' ‘undue experimentation’ and Amgen's ‘[un]reasonable experimentation’ standards. Id. at footnote 4. See also Guidelines for Assessing Enablement in Utility Applications and Patents in View of the Supreme Court Decision in Amgen Inc. et al. v. Sanofi et al., 89 FR 1563 (January 10, 2024), which explains that regardless of the technology the Wands factors should be used when assessing enablement.
However, 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 which included "a ‘vast’ number of additional antibodies" that Amgen had not described by their amino acid sequences. Id. at 613. The Court found that Amgen sought to monopolize an entire class by their function, even though that class was much broader than the 26 exemplary antibodies disclosed by their amino acid structure. Id. at 613.
In Amgen Inc. v. Sanofi, Aventisub LLC, 987 F.3d 1080 (Fed. Cir. 2021), which the Supreme Court affirmed, the Federal Circuit explicitly applied the Wands factors to assess whether the specification of Amgen’s patent provided sufficient enablement, for purposes of 35 U.S.C. 112(a), to make and use the full scope of the claimed invention. 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. See also the following cases across various technology areas: McRO, Inc. v. Bandai Namco Games Am. Inc., 959 F.3d 1091, 2020 USPQ2d 10550 (Fed. Cir. 2020); Wyeth & Cordis Corp. v. Abbott Laboratories, 720 F.3d 1380, 107 USPQ2d 1273 (Fed. Cir. 2013); Enzo Life Sciences, Inc. v. Roche Molecular Systems, Inc., 928 F.3d 1340 (Fed. Cir. 2019); and Idenix Pharmaceuticals LLC v. Gilead Sciences Inc., 941 F.3d 1149, 2019 USPQ2d 415844 (Fed. Cir. 2019).
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 its 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.
This case is akin to the issue in Amgen Inc. v. Sanofi, Aventisub LLC, in which 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. Sanofi-Aventisub 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.
The instant claims are directed to a class of antibodies that include “a ‘vast’ number of antibodies comprising a VH region comprising all the combinations of the CDRs that can be obtained when the CDR1 is selected from SEQ ID NOs:17- 25, the CDR2 is selected from SEQ ID NOs:30-36, and the CDR3 is selected from SEQ ID NOs:45-63, with a VH region being at least 80% identical sequence and still be able to bind any gD protein, in which the instant specification fails to describe the amino acid sequences of. It would be necessary to first generate and then screen each candidate antibody and fragments thereof, with the recited function) to determine whether it met the functional limitations of “able to bind any gD protein”. The Federal Circuit concluded that there was a lack of enablement, which was affirmed by the Supreme Court in Amgen.
The instant specification does not disclose any common structural feature delineating which of the claimed antibodies will have the function of “able to bind any gD protein”, or how to distinguish structures with this function from structures without. The only structure-function relationship guidance the specification provides is to disclose 5 monoclonal VHH antibodies binding to HSV-1 gD protein.
The instant claims simply direct skilled artisans to engage in the same iterative, trial-and-error process the inventors followed to discover the antigen binding CDRs 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.
The Supreme Court’s 2023 decision in Amgen v. Sanofi, which mainly involves the enablement requirement, states that “where a patentee purports to invent an entire genus, it must enable the entire genus”; “disclosing how to produce some antibodies that perform a specified function is not equivalent to disclosing how to produce all such antibodies – and it is the latter that petitioners claim as their invention”; S. Ct.
Additionally, in its recent decision in Baxalta Inc. v. Genentech, Inc., No. 2022-1461, 2023 WL 6135930 (Fed. Cir. Sept. 20, 2023) the Federal Circuit found the facts of this case to be "materially indistinguishable from those in Amgen." Baxalta, 2023 WL 6135930, at *4. According to the Federal Circuit, claim 1 covers "millions of potential candidate antibodies" (id.) that bind to Factor IX/IXa and increase the procoagulant activity of Factor IXa. The court, however, noted that the specification discloses the amino acid sequence of just 11 of those antibodies. And like the roadmap in the patents at issue in Amgen, "the '590 patent's roadmap simply directs skilled artisans to engage in the same iterative, trial-and-error process the inventors followed to discover the [11] antibodies they elected to disclose." (Id.) Missing from the specification, according to the Federal Circuit, was "'a quality common to every functional embodiment' ... that would allow a skilled artisan to predict which antibodies will perform the claimed functions" (id.; quoting Amgen Inc. v. Sanofi., 598 U.S. 594, 614 (2023)), such as a common structural or other feature that would allow the antibodies to perform the claimed functions, or an explanation as to why the 11 antibodies do so and others do not. (Baxalta, 2023 WL 6135930, at *4). And the Federal Circuit was not persuaded by Baxalta's argument that its disclosed hybridoma-and screening process "predictably and reliably generates new claimed antibodies every time it is performed" (id.), because "it is undisputed that to practice the full scope of the claimed invention, skilled artisans must make candidate antibodies and screen them to determine which ones perform the claimed functions." (Id.).
The specification does not reasonably provide enablement to use the invention of claims 1 and 5-23 as they are currently written. The specification does reasonably provide enablement to make and use the invention discussed supra.
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.
Bang Yu (Molecular Immunology, Vol. 34, No. 16-17. pp.11211131. 1997) teaches a comparison of llama VH sequences from conventional and heavy chain antibodies (title). Bang Yu described the features of the llama VHH domains derived from the heavy chain antibody cDNA (entire article). Based on those features, when the three CDRs are complete, they are VHH antibodies. However, any CDR mutation, which can happen when you recombine all these CDRs into different species is not predictable. This is evidenced by the fact that even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff (Proc Natl Acad Sci USA 1982 Vol 79 page 1979). Rudikoff teaches that the alteration of a single amino acid in a single CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (entire article, Abstract).) Thus, all claims rejected above, which read on VHH with mixed and matched CDRs, which are mutated CDR sets, or VHH recited by percent identity without all parental CDRs being fixed, are rejected here as failing the enablement requirement.
Moreover, claims not containing elements critical or essential to the practice of the invention, such as antibodies or antibody fragments not having all of the relevant functional complementarity determining regions (CDRs) in the proper site on an appropriate antibody heavy or light chain framework, are not enabled by the disclosure. See In re Mayhew, 527 F.2d 1229, 188 USPQ 356 (CCPA 1976).
Note that an enabling disclosure for the preparation and use of only a few analogs of a product does not enable all possible analogs where the characteristics of the analogs are unpredictable. See Amgen Inc. v. Chugai Pharmaceutical Co. Ltd. (18 USPQ 2d 1027 (CAFC 1991)).
Conclusion
No claims are allowed.
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/IMMA BARRERA/
Examiner, Art Unit 1671
/Michael Allen/ Supervisory Patent Examiner, Art Unit 1671
