DETAILED ACTION
Election/Restrictions
Applicant’s election of Group I, (prior claims 1-20, 27-33 and 44) in the reply filed on 12/5/25 is acknowledged. 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)).
With respect to the Species Election, Applicants elected with traverse SEQ ID NO: 3. Due to the elected polypeptide now sharing NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA and are exemplified by SEQ ID NOs: 3, 4, 17, 18, and 31-42 (as recited in amended claims 11 and 12), Applicants argue that exemplary SEQ ID NOs: 4, 17, 18, and 31-42 share structural similarity and common use with the elected species (i.e., SEQ ID NO:3) and the common use flows from the similar structural feature. Thus, Applicant requests that at least SEQ ID NOs: 3, 4, 17, 18, and 31-42 be searched and examined together, as such will serve the interest of compact prosecution and can be accomplished without undue burden.
These arguments to the Species election have been fully and carefully considered but are not deemed persuasive. The MPEP Section 2117 recites:
“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. Many of these sequences are only 75-80% identical to one another with large gaps and up to 200-300+ amino acid differences. They are different proteins, not just species of one another. See Markush rejection below for more details.
Claims 21-33 and 43 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected invention.
Claims 1, 7, 8, 11-20 are currently under examination.
Claim Objections
Claims 1, 7, 8, 11-20 are objected to because of the following informalities: the claims all refer to an “immunogen polypeptide” and should recite an “immunogenic polypeptide.” Appropriate correction is required.
Claim Rejections - 35 USC § 112-2nd paragraph
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 1, 7, 8, 11-20 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 1, 7, 8, 11-20 are rejected on the basis that it contains 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 any polypeptide comprising all or a portion of any NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA and exemplified by SEQ ID NOs: 3, 4, 17, 18, and 31-42 (as recited in amended claims 11 and 12) is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons:
These variants and different polypeptides do not comprise or 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. These polypeptides comprise amino acid sequences that vary greatly from one another, e.g., 75-80% only with up to 200-300 amino acid mismatches. SEQ ID NO: 5 (recited in claims 11 or 12) is the only protein in the group that shares substantial structural similarity, e.g., 97.5% identity to SEQ ID NO: 3. See sequence alignment in public PAIR, supplemental content tab. SEQ ID NO: 1 is the wild-type strain which shares 97.6% similarity. SEQ ID Nos: 4, 17, 18, and 31-42 (as recited in amended claims 11 and 12) do not have substantial structural similarity. These variants have up to 200-300 mismatched amino acids and vary from 75-80% similarity. They are different polypeptides which would not be expected to have the same binding capabilities or function. See sequence alignment dated 1/5/26, Pending_Patents 742kb, in supplemental content tab in Public PAIR.
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.
Claims 1, 7, 8 and 13-20 are vague and indefinite because it the mere recitation of a name, i.e., an immunogenic polypeptide consisting essentially of: a) all or a protein of each of the NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA; or (a) plus all or a portion of the ID1 region, to describe the invention is not sufficient to satisfy the Statute's requirement of adequately describing and setting forth the inventive concept. The claim should provide any structural properties, such as the amino acid sequence of the polypeptide, which would allow for one to identify the claimed polypeptide without ambiguity. While the specification can be used to provide definitive support, the claims are not read in a vacuum. Rather, the claim must be definite and complete in and of itself. Limitations from the specification will not be read into the claims. The claims as they stand are incomplete and fail to provide adequate structural properties to allow for one to identify what is being claimed. Appropriate clarification and/or correction is required.
Claims 1, 7, 8 and 13-20 are also vague and indefinite due to the recitation of “or a portion of” each of the NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA; or (a) plus all or a portion of the ID1 region because it is unclear what constitutes “a portion” and what amino acids are represented in this “portion”. A “portion” can read on a single amino acid or much more. While the specification can be used to provide definitive support, the claims are not read in a vacuum. Rather, the claim must be definite and complete in and of itself. Limitations from the specification will not be read into the claims. The claims as they stand are incomplete and fail to provide adequate structural properties to allow for one to identify what is being claimed. Appropriate clarification and/or correction is required.
Claim Rejections - 35 USC § 112-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.
Claims 1, 7, 8, 11 and 13-20 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 claims are drawn to, for example:
An immunogenic polypeptide consisting essentially of: a) all or a protein of each of the NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA; or (a) plus all or a portion of the ID1 region.
The immunogen polypeptide of claim 1, wherein the immunogen polypeptide comprises one or more conserved CSA binding channel residues.
The immunogen polypeptide of claim 7, wherein the conserved CSA binding channel residues are located in the major CSA binding channels of VAR2CSA.
11.The immunogen polypeptide of claim 1, wherein the immunogen polypeptide has at least 80% identity with any one of SEQ ID NO: 3.
To fulfill the written description requirements set forth under 35 USC § 112, first paragraph, the specification must describe at least a substantial number of the members of the claimed genus, or alternatively describe a representative member of the claimed genus, which shares a particularly defining feature common to at least a substantial number of the members of the claimed genus, which would enable the skilled artisan to immediately recognize and distinguish its members from others, so as to reasonably convey to the skilled artisan that Applicant has possession the claimed invention. Applicants have not described the Genus of immunogenic polypeptides, such that the specification might reasonably convey to the skilled artisan that Applicants had possession of the claimed invention at the time the application was filed.
The purpose of the "written description" requirement is broader than tomerely explain how to "make and use"; the applicant must convey with reasonableclarity to those skilled in the art that, as of the filing date sought, he or she was inpossession of the invention. The invention is, for purposes of the "writtendescription" inquiry, whatever is now claimed. See Vas-Cath, Inc. v. Mahurkar,935 F.2d 1555, 1563-64, 19 USPQ2d 1111, 1117 (Federal Circuit, 1991).Furthermore, the written description provision of 35 USC § 112 is severable fromits enablement provision; and adequate written description requires more than amere statement that it is part of the invention and reference to a potential methodfor isolating it. The nucleic acid [product] itself is required. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. The Guidelines for Examination of Patent Applications Under the 35 U.S.C. 112, paragraph 1, "'Written Description" Requirement (66 FR 1099-1111, January 5,2001) state, "[p]ossession may be shown in a variety of ways including description of an actual reduction to practice, or by showing the invention was 'ready for patenting' such as by disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention" (Id. at 1104). Moreover, because the claims encompass a genus of variant species, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. However, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; nor has Applicant shown the invention was "ready for patenting" by disclosure of drawings or structural chemical formulas that show that the invention was complete; nor has Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed. The Guidelines further state, "[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus'" (Id. at 1106);accordingly, it follows that an adequate written description of a genus cannot beachieved in the absence of a disclosure of at least one species within the genus. Asevidenced by Greenspan et al (Nature Biotechnology 7: 936-937, 1999), definingepitopes is not as easy as it seems. Greenspan et al recommends defining anepitope by the structural characterization of the molecular interface between theantigen and the antibody is necessary to define an "epitope" (page 937, column 2).According to Greenspan et al, an epitope will include residues that make contactswith a ligand, here the antibody, but are energetically neutral, or even destabilizingto binding. Furthermore, an epitope will not include any residue not contacted by the antibody, even though substitution of such a residue might profoundly affectbinding. There is a limit to how much substitution can be tolerated before the originaltertiary structure is lost. Therefore, absent a detailed and particular description of arepresentative number, or at least a substantial number of the members of thegenus of mutants, the skilled artisan could not immediately recognize that Applicants were in possession of the claimed genus of at the time of filing.
Therefore, because the art is unpredictable, in accordance with the WrittenDescription Guidelines there is not full written description for the breadth of the claims. The scope of the claim includes numerous structural variants/portions, and the genus is highly variant because a significant number of structural differences between genus members is permitted. One of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the claimed genus. The claimed subject matter is not supported by an adequate written description because a representative number of species has not been described. There is no teaching in the specification regarding which 20% of the structure (e.g., 80% homology) can be varied and still produce a polypeptide which has the functional activity. Although the disclosure of SEQ ID NO: 3 combined with the knowledge in the art, may put one in possession of peptides that are at least 80% identical to SEQ ID NO: 3, the level of skill and knowledge in the art is such that one of ordinary skill would not be able to identify without further testing which of those peptides would have the required functional activities. Based on the lack of knowledge and predictability in the art, those of ordinary skill in the art would not conclude that the applicant was in possession of the claimed genus of polypeptides.
Applicant is referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov
Claim Rejections - 35 USC § 112-Scope of 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.
Claims 1, 7, 8, 11 and 13-20 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:
An immunogenic polypeptide consisting essentially of the amino acid sequence set forth in SEQ ID NO: 3
, does not reasonably provide enablement for the full breadth of the claims, including:
An immunogenic polypeptide consisting essentially of: a) all or a protein of each of the NTS, DBL1X, DBL2X, ID2a, ID2b DBL4ε, and ID3 regions of VAR2CSA; or (a) plus all or a portion of the ID1 region.
The immunogen polypeptide of claim 1, wherein the immunogen polypeptide comprises one or more conserved CSA binding channel residues.
The immunogen polypeptide of claim 7, wherein the conserved CSA binding channel residues are located in the major CSA binding channels of VAR2CSA.
The immunogen polypeptide of claim 1, wherein the immunogen polypeptide has at least 80% identity with any one of SEQ ID NO: 3.
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 and/or use the invention commensurate in scope with these claims.
The specification states that substitutions, additions, or deletions may be made to the defined sequences; however, the specification provides no guidance as to what the amino acids may be changed without causing a detrimental effect to the protein and its ability to function properly. While it is known that many amino acid substitutions are possible in any given protein, the position within the protein’s sequence where amino acid substitutions can be made with a reasonable expectation of success are limited. Other positions are critical to the protein’s structure/function relationship, e.g., such as various positions or regions directly involved in binding, catalysis in providing the correct three-dimensional spatial orientation of binding and catalytic sites. These regions can tolerate only very little or no substitutions. Selective point mutation to one key residue could eliminate the function of the polypeptide. It could eliminate its functional properties. If the range of decreased binding ability after single point mutation of a protein antigen varies, one could expect point mutations in the protein antigen to cause varying degrees of loss of protection/function, depending on the relative importance to the binding interaction of the altered residue. Alternatively, the combined effects of multiple changes, as instantly claimed, in an antigenic determinant could again result in loss of function. A protein having multiple antigenic sites, multiple point mutations, or accumulated point mutations at key residues could create a new antigen that is precipitously or progressively unrecognizable by any of the antibodies in the polyclonal pool. As stated above, Applicants have not shown the particular substitution and the result it produces. Applicants have provided no guidance to enable one of ordinary skill in the art how to determine, without undue experimentation, the effects of different amino substitutions and the nature and extent of the changes that can be made. It is expensive and time consuming to make amino acid substitutions at more than one position, in a particular region of the protein, in view of the many fold possibilities for change in structure and the uncertainty as to what utility will be possessed. See Mikayama et al. (Nov.1993. Proc.Natl.Acad.Sci. USA, vol. 90 : 10056-10060) which teaches that the three-dimensional structure of molecules is important for their biological function and even a single amino acid difference may account for markedly different biological activities. Amino acids owe their ‘significance’ to their inclusion in a pattern which is directly involved in recognition by, and binding to, the receptor and the significance of the particular amino acids and sequences for different amino acids cannot be predicted a priori, but must be determined from case to case by painstaking experimental study. The instant claims allow for substitutions with amino acids of vastly different properties and they do not recite the specific changes in the claims. The claims also recite “a portion of” each of the regions and a portion is unclear and can read on as little as a single amino acid or more.
Genentech Inc. v. Novo Nordisk A/S (CAFC) 42 USPQ2d 1001 clearly states: “Patent protection is granted in return for an enabling disclosure of an invention, not for vague intimations of general ideas that may or may not be workable. See Brenner v. Manson, 383 U.S. 519, 536, 148 USPQ 689, 696 (1966) (stating, in context of the utility requirement, that "a patent is not a hunting license. It is not a reward for the search, but compensation for its successful conclusion.") Tossing out the mere germ of an idea does not constitute enabling disclosure. While every aspect of a generic claim certainly need not have been carried out by an inventor, or exemplified in the specification, reasonable detail must be provided in order to enable members of the public to understand and carry out the invention.”
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claim(s) 1, 7, 8, 11 and 13-20 is/are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Salanti et al (US20150004099; corresponds to WO2013117705 Aug 2013 and US Patent No. 11,787,844)
Clausen teaches Plasmodium falciparum 3D7 erythrocyte membrane protein 1, SEQ ID 55. This protein is 97.6% identical to Applicants’ SEQ ID NO: 3, e.g., at least 80% identity (instant claim 11). See sequence alignment of 1/5/26 in Public PAIR, Published_Applications, 401kB, 4th result. Clausen recites that the present invention relates to a novel isolated protein fragment of VAR2CSA (a member of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMPl) protein family), where the fragment consists of a sequential amino acid sequence of ID1, DBL2Xb and optionally ID2a. Given that Clausen’s polypeptide meets the structural requirements of the claims it would inherently possess the portions recited in the claims. Paragraph [0184] teaches that the composition may be formulated in nanoparticles. Paragraph [0009] teaches hat VAR2CSA polypeptides bind with high and specific affinity to cancer cells and tissues, which binding by the present inventors is suggested to be through a specific interaction with chondroitin sulfate proteoglycans expressed on the surface of the cancer cells or in the surrounding extracellular matrix. Accordingly, the Clausen suggest to use this specific and high affinity binding for the targeting of cancer cells or other tissues or cells with high or otherwise expression, such as inappropriate expression of this particular type of chondroitin sulfate proteoglycans. Paragraph [0155] recites that the VAR2CSA polypeptide, derivative, or conjugate as defined in the present specification may be administered simultaneously or sequentially with one or more other cancer agent, and/or be used in a combination treatment with other known therapies.
Claim(s) 1, 7, 8, 11 and 13-20 is/are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Salanti et al (WO 2013/117705; August 15, 2013; provided by Applicants);
Salanti et al discloses an immunogen polypeptide comprising all or portion of VAR2CSA and the use thereof in therapy either for vaccinating against malaria or for preventing or treating cancer. See: abstract, p. 3 line 14-p. 9 line 10, p. 95 lines 3-14, p. 99 lines 7-11, examples 1-22 and claims. Salanti discloses an immunogen polypeptide comprising all or a portion of VAR2CSA conjugated or not to anti-cancer agent for use in therapy. It is important to note the SEQ ID NO 55 of Salanti has 81.8% identity with SEQ ID NO 3 of the instant application, and allow a synthesis of recombinant immunogen polypeptide that could be used in therapy (cf. D2 abstract, p. 3 line 14 - p. 9 line 10, p. 95 lines 3-14, p. 99 lines 7-11, examples 1-22 and claims).
Claim(s) 1, 7, 8, 11 and 13-20 is/are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Babcook et al (US-2018193473; provided by Applicants)
Babcook et al discloses an immunogenic polypeptide comprising all or portion of VAR2CSA and the use thereof in therapy either for vaccinating against malaria or treating or preventing cancer. See: abstract, paragraphs [0007]-[0011], examples 1-6 and claims. Babcook discloses an immunogen polypeptide comprising all or a portion of VAR2CSA conjugated or not to anti-cancer agent for use in therapy for the treatment of prevention of cancer. It is important to note the SEQ ID NO 55 of Babcook has 81.8% identity with SEQ ID NO 3 of the instant application, and allow a synthesis of recombinant immunogen polypeptide that can be used in therapy (cf. abstract paragraphs [0007]-[0011], examples 1-6 and claims).
Claim(s) 1, 7, 8, 11 and 13-20 is/are rejected under 35 U.S.C. 102(a)(2) as being anticipated by Theander et al (US Patent No. 7,745,580; corresponds to WO2004067559-A1. 8/12/2004 and US20070053928A1).
Theander teaches a CSA-binding malarial variant surface antigen comprising SEQ ID NO: 2 which is 97.6% to Applicants’ SEQ ID NO: 3 (instant claim 11 recites at least 80% identity to SEQ ID NO: 3). See sequence alignment of 1/5/26 in Public PAIR, Published_Applications, 401kB, 4th result. The sequence corresponds to a Plasmodium falciparum (malaria) variant surface antigen which binds to the glycosaminoglycan chondroitin sulphate. The protein is designated vsa2csa. The protein is capable of inducing an immune response against a molecule expressed on the surface of an intact erythrocyte infected by a placental parasite. Sub-sequences comprise at least one B-cell epitope or one or more GAG-binding motifs and do not comprise a CIDR domain or DBL-gamma domain. Given that Clausen’s polypeptide meets the structural requirements of the claims it would inherently possess the portions recited in the claims.
Claim(s) 1, 7, 8, 11 and 13, 14, 15, 18 and 20 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Marion Avril et al ("Antibodies to a Full-Length VAR2CSA Immunogen Are Broadly Strain-Transcendent but Do Not Cross- Inhibit Different Placental-Type Parasite Isolates" - 1 January 2011 - PLOS ONE, vol. 6(2): e16622; provided by Applicants);
Avril et al disclose an immunogen polypeptide comprising all or portion of VAR2CSA and the use thereof in therapy either for vaccinating against malaria (Avril et al abstract, p. 2 left-hand column first and second full paragraphs, right-hand column first and second full paragraphs, p. 3 right-hand column first full paragraph - p. 6 right-hand column line 6 and fig. 1-4) or for preventing or treating cancer. Avril discloses a vaccine composition comprising all or a portion of VAR2CSA and the use thereof for producing antibodies able to inhibit adhesion to CSA-proteoglycan (cf. D1 abstract, p. 2 left-hand column first and second full paragraphs, right-hand column first and second full paragraphs, p. 3 right-hand column first full paragraph - p. 6 right-hand column line 6 and fig. 1-4). In particular Avril discloses the production of a recombinant protein having the accession number PFL0030c, which is an immunogenic polypeptide that presents 81.8% identity with SEQ ID NO 3 of the instant application, and its use in vaccine preparation.
Prior art not presently relied upon:
Ma R et al (Nat. Microbiol. 6:380-391(2021). 97.6% identity to SEQ ID NO: 3)
"Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.";
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/JENNIFER E GRASER/Primary Examiner, Art Unit 1645 2/25/26