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 .
Examiner’s Note
Examination of the instant application has been transferred to Examiner Jeff Sifford of Art Unit 1671. The Examiner may be contacted at 571-272-7289 or Jeffrey.Sifford@uspto.gov.
Election/Restrictions
Applicant's election with traverse of Group I, and the required species of SEQ ID NO: 2 in the reply filed on 4/2/2026 is acknowledged. The traversal is on the ground(s) that Group I-II share the feature wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at the position corresponding to position 31 of SEQ ID NO: 1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1. This is not found persuasive because the restriction requirement includes three inventive groups, Groups I-III. However, Applicant merely argued that Groups I and II share a technical feature, rather than there is a unifying special technical feature of all of Groups I-III. Applicant’s argument appears to only attempt to unify two of the three inventive groups outlined in the restriction requirement, whereas the shared technical feature must be between all three groups.
The requirement is still deemed proper and is therefore made FINAL.
Claims 118-122 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on 4/2/2026.
Claims 1 and 105-117 are under examination on the merits.
Information Disclosure Statement
The Information Disclosure Statements (IDSs) submitted on 10/24/2023 and 4/2/2026 are in compliance with 37 CFR 1.97. Accordingly, the IDSs are being considered by the examiner.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code on p. 45. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http://, www, or other browser-executable code. See MPEP § 608.01.
The disclosure is objected to because of the following informalities: the “BRIEF DESCRIPTION OF THE DRAWINGS” refers to use of colors in the drawings (paras. [0038]-[0048]), which is impermissible, since no petition for use of colored drawings has been granted.
Appropriate correction is required.
Claim Objections
Claims 1, 107-110, and 113 is objected to because of the following informalities: claims 1 and 107-110 recite “from the group consisting of”, on lines 4, 2, 2, 2, and 2, respectively, which should have a “:” inserted after “from the group consisting of”; claim 113 uses the subpart designators “a.”, “b.”, “c.,”, “d.”, “e.”, and “f.”, which are of an improper format “[e]ach claim begins with a capital letter and ends with a period. Periods may not be used elsewhere in the claims except for abbreviations. See Fressola v. Manbeck, 36 USPQ.2d 1211 (D.D.C. 1995).” MPEP §608.01(m). Claim 113 is also objected to for typographical mistakes, where “SEQ IDNO:2” should instead read “SEQ ID NO: 2” on lines 6 and 10. Appropriate correction is required.
Claim Rejections - 35 USC § 112
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.
Scope of Enablement
Claims 1, 105-113, and 115-117 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 a protein comprising the amino acid sequence SEQ ID NO: 2, does not reasonably provide enablement for a protein comprising an amino acid sequence having an amino acid sequence at least 90% sequence homology over the entire length of SEQ ID NO: 2. 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.
The breadth of the claims is found in claim 1.
The nature of the invention is proteins comprising an amino acid sequence selected from the group consisting of i) an amino acid sequence having at least 90% sequence homology over the entire length of a sequence selected from the group consisting of SEQ ID NO: 2, wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at the position corresponding to position 31 of SEQ ID NO: 1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1 (claim 1). SEQ ID NO: 2 is 194 amino acids long, so 90% sequence homology allows for 19 amino acids to be different or missing from SEQ ID NO: 2. The specification indicates that the claimed proteins are novel compositions of matter having better neutralizing responses than other spike-based immunogens for COVID-19 vaccines (para. [0053]). The proteins contain sequences that are not found in nature, but are derived from the RBD of the spike protein, and contain engineered amino acid changes that increase protein yield and stability, and improve immune response upon immunization of animals (para. [0054]).
The level of skill of one skilled in this art is high.
The specification teaches a computational strategy to create 40,000 decoys each of which has an average of 10 amino acid changes from the native SARS-CoV-2 sequence, 28 sequences of which were screened in vitro, identifying 5 lead candidates (para. [039]).
The state of the prior art is such that it is well established in the art that SARS-CoV-2 S protein variants with mutations in the RBD confer resistance to monoclonal antibodies or convalescent plasma, and such mutations may be readily selected (Weisblum. Elife. 2020 Oct 28;9:e61312; Abstract).
Thus, the state of the art recognized that it would be highly unpredictable to generate SARS-CoV-2 spike RBD mutants that maintain neutralizing epitopes. Mutation of up to 10% of the SARS-CoV-2 spike RBD would likely interfere with epitopes recognized by antibodies specific for SARS-CoV-2 RBD. One of skill in the art would neither expect nor predict the appropriate functioning of the proteins as broadly as currently claimed.
In view of the lack of the predictability of the art to which the invention pertains as evidenced by, the lack of guidance and direction provided by applicants, and the absence of working examples, undue experimentation would be required to make and use a protein comprising an amino acid sequence having an amino acid sequence at least 90% sequence homology over the entire length of SEQ ID NO: 2 that increase protein yield and stability, and improve immune response upon immunization of animals (para. [0054]), particularly since the scope of the claims allow for the mutation of 19 of 194 amino acids of SEQ ID NO: 2, many of which would result in loss of native SARS-CoV-2 RBD epitopes, absent a specific and detailed description in applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed proteins are functional, commensurate in scope with the claimed invention.
Moreover, claims not containing elements critical or essential to the practice of the invention, such as SARS-CoV-2 spike RBD proteins that maintain the antigenic epitopes and engineered amino acid changes that increase protein yield and stability, and improve immune response upon immunization of animals, are not enabled by the disclosure. See In re Mayhew, 527 F.2d 1229, 188 USPQ 356 (CCPA 1976).
Regarding claim 116, Applicant broadly claims a nucleic acid molecule encoding the protein of claim 1. The claim reads on a cell within a transgenic animal or a transgene therein given that the term "isolated" is not denoted in describing the nucleic acid molecule.
With respect to the unisolated host cells and transgenes as “nucleic acids” or “vectors “of the instant claims discussed above, the state of the art at the time of filing was such that one of skill could not predict the phenotype of transgenics. The art of transgenic animals has for many years stated that the unpredictability lies, in part, with the site or sites of transgene integration into the target genome and that "the position effect" as well as unidentified control elements are recognized to cause aberrant expression of a transgene (Wall et al., Theriogenology, Vol. 45, Pg. 57-68, 1996).
The elements of the particular construct used to make transgenic animals are also held to be critical, and they must be designed case by case without general rules to obtain good expression of a transgene; e.g., specific promoters, presence or absence of introns, etc. (Houdebine et al., Journal of Biotechnology, Vol. 34, Pg. 269- 287, 1994). Furthermore, transgenic animals are regarded to have within their cells, cellular mechanisms that prevent expression of the transgene, such as methylation or deletion from the genome (Kappell et al., Current Opinions in Biotechnology, Vol. 3, Pg. 548-553, 1992). Houdebine (Comparative Immunology, Microbiology, and Infectious Diseases, Vol. 32, Pg. 107-121, 2009) teaches progress has been made in the field of transgenic animals for production of foreign proteins (Abstract); however, constructing an efficient expression vector to produce a therapeutic protein is not a standard operation (Pg. 116, Paragraph, second). Therefore, undue experimentation is required to make and use a transgene and transgenic animal to produce the proteins of the instant claims.
Examples in the literature aptly demonstrate that even closely related species carrying the same transgene construct can exhibit widely varying phenotypes. Mullins (1993, Hypertension, Vol. 22, No. 4, pp. 630-633) states that not all animals express a transgene sufficiently to provide a model for a disease as the integration of a transgene into different species of animal has been reported to give divergent phenotypes. For example, several animal models of human diseases have relied on transgenic rats when the development of mouse models was not feasible. Mullins (1990, Nature, Vol. 344, 541-544) produced outbred Sprague-Dawley x WKY rats with hypertension caused by expression of a mouse Ren-2 renin transgene. Hammer (1990, Cell, Vol. 63, 1099- 1112) describes spontaneous inflammatory disease in inbred Fischer and Lewis rats expressing human class I major histocompatibility allele HLA-B27 and human 02- microglobulin transgenes. Both investigations were preceded by the failure to develop human disease-like symptoms in transgenic mice expressing the same transgenes that successfully caused the desired symptoms in transgenic rats (Mullins, 1989, EMBO J., Vol. 8, pages 4065-4072). Thus, the use of nonmurine species for transgenesis will continue to reflect the suitability of a particular species for the specific questions being addressed, bearing in mind that a given construct may react very differently from one species to another.
The examiner notes here, in addition to these issues, even assuming arguendo PHOSITA could make a host organism with functional transgene that encodes the instant protein, there is no predictability that the host will survive its expression. The transgene depends on the host for function and harm to the host, including death, renders the transgene nonfunctional and thus not enabled.
At the time of filing, the phenotype of a transgene and transgenic cell contained within any animal was unpredictable. The claims as written, encompassing a transgene and cell in a transgenic animal, is not adequately described in the specification as to prevent excessive experimentation by the public to generate and use the invention. Applicants can obviate the instant rejection by amending the claim to recite the term "isolated" before the recitation, "nucleic acid molecule" and by amending the polynucleotide claims to specify they are not in a transgenic animal. Applicant may consider using purified in such claims if description is appropriate for such a term and it is not redefined away from standard meaning. Method claims using these products should also carry the appropriate adjectives above.
In view of the lack of the predictability of the art to which the invention pertains as evidenced by the art above, the lack of guidance and direction provided by Applicant, and the absence of working examples, undue experimentation would be required to make and use functional nucleic acid molecules that produce proteins, absent a specific and detailed description in Applicant’s specification of how to effectively practice this and absent working examples providing evidence which is reasonably predictive that the claimed proteins are functional, commensurate in scope with the claimed invention. The same can be said for the transgenes and transgenic animals encompassed by the instant claims. Thus, the claim is rejected here.
Written Description
Claims 1, 105-113, and 115-117 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.
The instant claims above are drawn to a genus of proteins comprising an amino acid sequence selected from the group consisting of i) an amino acid sequence having at least 90% sequence homology over the entire length of a sequence selected from the group consisting of SEQ ID NO: 2, wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at the position corresponding to position 31 of SEQ ID NO: 1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1 (claim 1). They are not defined by any structure other than requiring an amino acid sequence at least 90% identical to SEQ ID NO: 2. SEQ ID NO: 2 is 194 amino acids long, so 90% sequence homology allows for 19 amino acids to be different or missing from SEQ ID NO: 2. Similarly, claim 113 encompasses a protein that is at least 90% identical to SEQ ID NO: 2 with a methionine at position 1, proline at position 16, tyrosine at position 30, tyrosine at position 31, glutamine at position 62, phenylalanine at position 64, threonine at position 136, aspartic acid at position 187, or proline at position 190, which also allows for 19 amino acids to be different or missing from SEQ ID NO: 2. Accordingly, there is insufficient structure described for the claimed proteins.
Even if the prior art is aware of such proteins, the totality of known proteins would not be representative of each entire genus for the reasons discussed below. Claims 105-113, and 115-117 depend from claim 1 but fail to resolve this lack of defined structure.
“[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.
An applicant may show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613.
Furthermore, to satisfy the written description requirement for the genus proteins comprising an amino acid sequence selected from the group consisting of i) an amino acid sequence having at least 90% sequence homology over the entire length of a sequence selected from the group consisting of SEQ ID NO: 2, wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at the position corresponding to position 31 of SEQ ID NO: 1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1, Applicant must adequately describe representative proteins to reflect the structural diversity of the claimed genus. See Eli Lilly, 119 F.3d at 1568 (“[N]aming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.”); Fiers v. Revel, 984 F.2d 1164, 1171 (Fed. Cir. 1993) (“Claiming all DNA[s] that achieve a result without defining what means will do so is not in compliance with the description requirement; it is an attempt to preempt the future before it has arrived.”).
MPEP § 2163 states 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, 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 claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 759 F.3d 1285, 111 USPQ2d 1780 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, as here in which the proteins claimed can have a high degree of variability within the sequence of the proteins. The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure “indicates that the patentee has invented species sufficient to constitute the gen[us].” See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615. “A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.” One of skill in this art cannot envision the structure of a representative number of species of the very large genus of a protein that is 194-amino acids in length that allows for up to 19 mutations. Therefore, since a relatively low number of species is provided to represent this genus, the claims encompassing the same clearly fail the written description requirement.
Functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support, especially in technology fields that are highly unpredictable, where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus. See ABBVIE DEUTSCHLAND GMBH & 2 CO. v. JANSSEN BIOTECH, INC., Appeals from the United States District Court for the District of Massachusetts in Nos. 09-CV-11340-FDS, 10-CV-40003-FDS, and 10-CV-40004-FDS, Judge F. Dennis Saylor, IV. See also Ariad, 598 F.3d at 1351 (“[T]he level of detail required to satisfy the written description requirement varies depending on the nature and scope of the claims and on the complexity and predictability of the relevant technology.”); see also Centocor Ortho Biotech, Inc. v. Abbott Labs., 636 F.3d 1341, 1352 (Fed. Cir. 2011) (noting the technical challenges in developing fully human antibodies of a known human protein).
For a claim 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.
“Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species.” Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010). Since the claimed protein genus allows for up to 10% residue mutation, there is no correlation between structure and function between the members of the protein genus. One cannot “represent” the entire genus defined only by function with any structural consensus. Thus, functional language should not be used to define a protein genus. Rather, structure should be used.
Even when several species are disclosed, these are not necessarily representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014) (“The ’128 and ’485 patents, however, only describe species of structurally similar antibodies that were derived from Joe-9. Although the number of the described species appears high quantitatively, the described species are all of the similar type and do not qualitatively represent other types of antibodies encompassed by the genus.”). Thus, when there is substantial variation within the genus, as here, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. Since each genus recited in the instant claims is large, it would be very challenging to describe sufficient species to cover the structures of the entire genus. The specification discloses a computational strategy to create 40,000 decoys each of which has an average of 10 amino acid changes from the native SARS-CoV-2 sequence, 28 sequences of which were screened in vitro, identifying 5 lead candidates (para. [039]). This number of representative species is certainly not adequate, further, these are not necessarily within 90% sequence identity to SEQ ID NO: 2 and/or comprising an amino acid having a larger side chain than alanine at position 31, a polar or charged amino acid at position 136, or an amino acid more hydrophilic than histidine at position 187 corresponding to SEQ ID NO: 1.
Overall, at the time the invention was made, the level of skill for preparing mutated proteins with desired functional properties was high.
As discussed above, an applicant may show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613. Therefore, it is recommended that the instant claims be amended to recite complete structural information of the claimed proteins, such as decreasing the scope of the genus of proteins by increasing the amino acid sequence identity requirement of the claim 1 and 113.
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 105 and 106 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.
Claims 105 and 106 recite “wherein the amino acid at the position corresponding to position 31 of SEQ ID NO: 1 is selected from the group comprising” on lines 1-2. The claims are indefinite because the group is open-ended, it is not clear what all amino acids may be members of the group.
Claim Rejections – Improper Markush Grouping
Claims 1, and 105-117 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).
The improper Markush grouping includes species of the claimed invention that do not share both a substantial structural feature and a common use that flows from the substantial structural feature. The members of the improper Markush grouping do not share a substantial structural feature and a common use that flows from the substantial structural feature for the following reasons:
MPEP 803.02 provides guidance on the analysis of a proper Markush group. Members of a proper Markush group are disclosed in the specification to possess at least one property in common which is mainly responsible for their function in the claimed relationship, and it is clear from their very nature or from the prior art that all of them possess this property. The MPEP further provides that in the members of a proper Markush group there should be (1) a common utility, and (2) a substantial structural feature essential to that utility.
In the instant case, claim 1 recites a protein comprising an amino acid sequence selected from the group consisting of i) an amino acid sequence having at least 90% sequence homology over the entire length of a sequence selected from the group consisting of SEQ ID NO: 2-6; and ii) an amino acid sequence having at least 85% sequence homology over the entire length of SEQ ID NO: 7, wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at the position corresponding to position 31 of SEQ ID NO: 1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1 (claim 1), but they do not appear to share a substantial structural feature. The shared utility of the group of proteins is that they are coronavirus spike proteins for use as vaccines against SARS-CoV-2. The amino acid sequences recited in parts i) and ii) represent an improper Markush group.
The claimed amino acid sequences do not share a conserved core, even if all of them have a similar function. For example, the claimed amino acid sequences may have at least 90% sequence homology to SEQ ID NOs: 2-6, or 85% sequence homology over the entire length of SEQ ID NO: 7, which allows for up to 19 amino acid substitutions for a 194-amino acid long sequence (SEQ ID NOs: 2-6), or 29 amino acid substitutions for an amino acid sequence with 85% sequence homology over the entire length of SEQ ID NO: 7. With the broad sequence identity encompassed by the genus of proteins, no single residue has to be conserved amongst all of the embodiments, and so they could never have one core consensus sequence. Thus, the proteins represent improper Markush groups. Accordingly, a common use cannot flow from a shared substantial structural feature in these claims. Since the instant claims contain Markush groups with members of proteins comprising different amino acid sequences associated with the claimed function of being a protein, the claims contain an improper Markush group and are rejected here. Claims 105-117 depend from claim 1 but do not introduce a proper Markush group for these issues.
In response to this rejection, Applicant should either amend the claim(s) to recite only individual species or grouping of species that share a substantial structural feature as well as a common use that flows from the substantial structural feature, or present a sufficient showing that the species recited in the alternative of the claims(s) in fact share a substantial structural feature as well as a common use that flows from the substantial structural feature. This is a rejection on the merits and may be appealed to the Board of Patent Appeals and Interferences in accordance with 35 U.S.C. §134 and 37 CFR 41.31(a)(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 115 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 115 requires the protein of claim 1 to be a SARS-CoV-2 spike protein. However, the mutations that are the difference between SEQ ID NO: 2 and wild-type RBD are relatively minor, and a person having ordinary skill in the art would still recognize SEQ ID NO: 2 as a SARS-CoV-2 spike protein. Applicant may cancel the claim, amend the claim to place the claim in proper dependent form, rewrite the claim in independent form, or present a sufficient showing that the dependent claim complies with the statutory requirements.
Art-free Subject Matter
SEQ ID NO: 2, and an amino acid sequence having at least 90% sequence homology over the entire length of SEQ ID NO: wherein the amino acid sequence comprises an amino acid having a larger side chain than alanine at position 31 of SEQ ID NO:1, a polar or charged amino acid at the position corresponding to position 136 of SEQ ID NO: 1, or an amino acid more hydrophilic than histidine at the position corresponding to position 187 of SEQ ID NO: 1 are free of the prior art of record.
Conclusion
No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to JEFFREY MARK SIFFORD whose telephone number is 571-272-7289. The examiner can normally be reached 8:30 a.m. - 5:30 p.m. ET with alternating Fridays off.
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/JEFFREY MARK SIFFORD/Examiner, Art Unit 1671 /Michael Allen/Supervisory Patent Examiner, Art Unit 1671
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