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 .
Applicant’s election of group I, claims 18, 19, 21-31, 35, and 42-44, and the species of SEQ ID NO: 118 for the binding protein, SEQ ID NO: 87 for the di-block sequence, SEQ ID NO: 1 for the core polypeptide, and SEQ ID NO: 8 for the corona sequence in the reply filed on 10/27/25 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)).
Claims 47, 51, and 52 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 10/27/25.
Claims 18, 19, 21-31, 35, and 42-44 are under examination as they read on the elected species.
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.
Claims 18, 19, 21-31, 35, and 42-44 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 MPEP states that the purpose of the written description requirement is to ensure that the inventor had possession, as of the filing date of the application, of the specific subject matter later claimed. The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention.”
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, disclosure of drawings, or by disclosure of relevant identifying characteristics, for example, 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 Applicants were in possession of the claimed genus.
The instant claims are drawn to a protein nanoparticle comprising a fusion protein comprising at least one binding polypeptide and at least one unstructured polypeptide.
The specification discloses RLP20 (SEQ ID NO: 18-19), RLP-20-ELP-80 (SEQ ID NO: 81), RLP40-ELP80 (SEQ ID NO: 84), ELP80-ELP80 (SEQ ID NO: 87), RLP100-ELP80 (SEQ ID NO: 88), and an Fn3 domain (SEQ ID NO: 60) that binds the αvβ3 integrin. The specification teaches that these genes were fused with the gene that encodes the Fn3 domain. The specification teaches that genes encoding RLP20-ELP80 (SEQ ID NO: 81), RLP40-ELP80 (SEQ ID NO: 84), RLP80-ELP80 (SEQ ID NO: 87) were cloned to the N-terminus of an Fn3 (SEQ ID NO: 60). The specification discloses an RLP-RLP block co-polypeptide. The specification teaches that the core block sequence was SEQ ID NO: 1 and the corona sequence was SEQ ID NO: 8. The specification teaches that the core block size was controlled to be 20, 40, 60, or 80 repeat units of Gln-Tyr-Pro-Ser-Asp-Gly-Arg-Gly and the corona block was 80 repeats Val-Pro-Gly-[Ala/Gly]-Gly-YY (SEQ ID NO: 81, 84, 93, 87). The specification teaches that RLP40-ELP80 and RLP60-ELP80 likely self-assemble into spherical micelles. The specification teaches that RLP80-ELP-80 self-assembles in to much larger, non-spherical structures. The specification teaches that RLP-ELP block co-polypeptide was combined with human fibronectin Fn3 that targets the human αvβ3 integrin (SEQ ID NO: 95, 96, 97). The specification discloses RLPSS-40-RLPQHN-40 (SEQ ID NO: 100) and S-80-QHN-40 (SEQ ID NO: 101) self-assemble into worm-like micelles. The specification discloses block co-polypeptides SEQ ID NO: 104, 106, 108-109 that self-assemble.
The specification teaches that the fusion protein comprises at least one unstructured polypeptide and at least one binding polypeptide. The specification teaches that the term unstructured polypeptide comprises any polypeptide that has a minimal or no secondary structure as observed by OD, being soluble at a temperature below its LCST and/or at a temperature above its USCST, and comprise a repeated amino acid sequence. The specification teaches that the unstructured polypeptide may have LCST, UCST, or both. The specification teaches that the unstructured polypeptide comprises one or more thermally responsive polypeptides, such as ELP and RLP. The unstructured polypeptide can comprise one or more core polypeptides or one or more corona polypeptides. The specification teaches that the binding polypeptide may comprises any polypeptide that is capable of binding at least one target.
Although the claims are inclusive of the fusion polypeptides specifically described in the specification, the claims broadly encompass a vast genus of fusion proteins that are described solely by their function of comprising at least one binding polypeptide and at least one unstructured polypeptide. The specification teaches that binding polypeptide may comprises any polypeptide that is capable of binding at least one target and the unstructured polypeptide comprises any polypeptide that has a minimal or no secondary structure as observed by OD, being soluble at a temperature below its LCST and/or at a temperature above its USCST, and comprise a repeated amino acid sequence. The specification teaches that the unstructured polypeptide can comprise one or more core polypeptides or one or more corona polypeptides. This indicates that there are hundreds, if not thousands, of potential fusion proteins encompassed by the claims. Given the generic description of the component parts of the fusion protein, the claims encompass a vast genus of fusion proteins. These fusion proteins have no correlation between their structure and function. The specification discloses fusion proteins comprising di-block polypeptides comprising RLP-ELP repeats, and teaches exemplary fusion proteins comprising the di-block polypeptides fused to Fn3. The specification teaches that these proteins self-assemble into structures (e.g., micelles). However, the claims are not limited to these fusion proteins, and the components of the fusion protein are described only by function and/or a partial structure. The specification provides insufficient guidance regarding the structure of the fusion protein components required to maintain the required function.
Therefore, the specification does not provide adequate written description to identify the broad genus of the claims because, inter alia, the specification does not disclose a correlation between the necessary structure of the fusion protein and the claimed function to be maintained (e.g., binding a particular target and self-assemble into a nanoparticle); and thus, the specification does not distinguish the claimed genus from others, except by function. Accordingly, the specification does not define the structural features commonly possessed by the genus, because, while the description of an ability of the claimed fusion protein may generically describe the protein’s function, it does not describe the protein itself. A definition by function does not suffice to define the genus because it is only an indication of what the protein does, rather than what it is; therefore, it is only a definition of a useful result rather than a definition of what achieves the result. In addition, because the genus of fusion proteins is highly variable (i.e., each fusion protein would necessarily have a unique structure, See MPEP 2434), the generic description of the fusion protein is insufficient to describe the genus. Further, given the highly diverse nature of proteins, even one of skill in the art cannot envision the structure of the fusion protein by knowing a partial structure and/or its functional characteristics. Thus, the specification does not provide substantive evidence for possession of this large and variable genus, encompassing a potentially massive number of fusion proteins claimed only by a functional characteristic and/or partial structure.
A biomolecule sequence described by only a function characteristics A biomolecule sequence described only by a functional characteristic, without any known or disclosed correlation between that function and the structure of the sequence, normally is not sufficient identifying characteristics for written description purposes, even when accompanied by a method of obtaining the agent. The specification does not adequately describe the correlation between the chemical structure and function of the genus, such as structural domains or motifs that are essential and distinguish members of the genus from those excluded. Thus, the genus of antibodies has no correlation between their structure and function.
Furthermore, Applicants have not shown possession of a representative number of species that have the claimed function(s). While the specification clearly sets forth a correlation between the fully disclosed fusion proteins, and the claimed function(s), this correlation does not appear to be clearly present in the breadth of the claims. As noted above, the claims are not limited to the disclosed fusion proteins and encompass fusion proteins comprising any binding protein and any unstructured polypeptide. Thus, the genus has substantial variation because of the numerous alternatives and combinations permitted. There is no description of the structure common to the members of the genus such that one of skill in the art can visualize or recognize the members of the genus. Therefore, only a few species have been described and this is not considered to be representative of the breadth of the genus.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that "applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the 'written description' inquiry, whatever is now claimed." (See page 1117.) The specification does not "clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed." (See Vas-Cath at page 1116.)
With the exception of the fully described fusion proteins, the skilled artisan cannot envision the detailed chemical structure of the encompassed agents, regardless of the complexity or simplicity of the method of isolation. Adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. The nucleic acid and/or protein itself is required. See Fiers v. Revel, 25 USPQ2d 1601,1606 (CAFC 1993) and Amgen Inc. V. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481,1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
Finally, University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404. 1405 held that: ...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines Inc., 107 F.3d 1565, 1572, 41 USPQ2dl961,1966 (1997); In re Gosteli, 872 F.2dl008,1012,10 USPQ2dl614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d 1966.
Protein chemistry is probably one of the most unpredictable areas of biotechnology. Consequently, the effects of sequence dissimilarities upon protein structure and function cannot be predicted. Punta et al. (PLoS Comput Biol 4(10): e1000160, 2008) teach that homology (both orthology and paralogy) does not guarantee conservation of function (See page 2). Punta et al. teach that relatively small difference in sequence can sometimes cause quite radical changes in functional properties, such as a change of enzymatic action, or even loss or acquisition of enzymatic activity itself (See page 2). Punta et al. teach that it is also apparent that there is no sequence similarity threshold that guarantees that two proteins share the same function (see page 2). Punta et al. teach that homology between two proteins does not guarantee that they have the same function, not even when sequence similarity is very high (including 100% sequence identity) (See page 2 and table 2). Punta et al. teach that proteins live and function in 3D, and therefore structural information is very helpful for predicating function (See page 4). However, as with sequence, two proteins having the same overall architecture, and even conserved functional residues, can have unrelated functions (See page 4). Punta et al. teach that still; structural knowledge is an extremely powerful tool for computational function prediction (See page 5).
Similarly, Whisstock et al. (Quarterly Reviews in Biophysics. 36(3):307-340, 2007) teach that the prediction of protein function from sequence and structure is a difficult problem (See abstract). Although many families of proteins contain homologues with the same function, homologous proteins often have different functions as the sequences progressively diverge (See page 309). Whisstock et al. teach that moreover, even closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function (See page 309). Further, Whisstock et al. note that in some instances, even sequences that are the same can have different functions. For example, eye lens proteins in the suck are identical in sequence to active lactate dehydrogenase and enolase in other tissues, although they do not encounter the substrates in the eye (See page 310). Whisstock et al. teach that assigning a function to an amino acid sequence based upon similarity becomes significantly more complex as the similarity between the sequence and a putative homologue fall (See page 321). Whisstock et al. teach that while it is hopeful that similar proteins will share similar functions, substitution of a single, critically placed amino acid in an active-site may be sufficient to alter a protein’s role fundamentally (See pages 321-323).
The sensitivity of proteins to alterations of even a single amino acid in a sequence are exemplified by Burgess et al. (J. Cell Biol. 111:2129-2138, 1990) who teach that replacement of a single lysine reside at position 118 of acidic fibroblast growth factor by glutamic acid led to the substantial loss of heparin binding, receptor binding and biological activity of the protein and by Song et al. (Molecular Biology of the Cell, 15:1287–1296, March 2004) who teach that substitution of alanine for aspartate in survivin results in the conversion of survivins’ apoptotic function from anti-apoptotic to proapoptotic and changes in its subcellular localization (See page 1287-1289). Moreover, Defeo-Jones et al. (Molecular and Cellular Biology, Sept. 1989, p. 4083-4086) teach that the conservative substitution of lysine for arginine at position 42 completely eliminated biological activity (See abstract and pages 4084-4085). These references demonstrate that even a single amino acid substitution will often dramatically affect the biological activity and characteristics of a protein.
Additionally, Bork (Genome Research, 2000; 10:398-400) clearly teaches the pitfalls associated with comparative sequence analysis for predicting protein function because of the known error margins for high-throughput computational methods. Bork specifically teaches that computational sequence analysis is far from perfect, despite the fact that sequencing itself is highly automated and accurate (p. 398, column 1). One of the reasons for the inaccuracy is that the quality of data in public sequence databases is still insufficient. This is particularly true for data on protein function. Protein function is context dependent, and both molecular and cellular aspects have to be considered (p. 398, column 2). Conclusions from the comparison analysis are often stretched with regard to protein products (p. 398, column 3). Further, although gene annotation via sequence database searches is already a routine job, even here the error rate is considerable (p. 399, column 2). Most features predicted with an accuracy of greater than 70% are of structural nature and, at best, only indirectly imply a certain functionality (see legend for table 1, page 399). As more sequences are added and as errors accumulate and propagate it becomes more difficult to infer correct function from the many possibilities revealed by database search (p. 399, paragraph bridging columns 2 and 3). The reference finally cautions that although the current methods seem to capture important features and explain general trends, 30% of those features are missing or predicted wrongly. This has to be kept in mind when processing the results further (p. 400, paragraph bridging cols 1 and 2).
Given not only the teachings of Punta et al., Whisstock et al., Song et al., Burgess et al., and Defeo-Jones et al., but also the limitations and pitfalls of using computational sequence analysis and the unknown effects of alternative splicing, post translational modification and cellular context on protein function as taught by Bork, the claimed proteins having the required function(s) could not be predicted based on sequence identity. Clearly, it could not be predicted that a polypeptide or a variant that shares only partial homology with a disclosed protein or that is a fragment of a protein will function in a given manner. Therefore, the state of the art supports that even the skilled artisan requires guidance on the critical structures of the nucleic acid and amino acid sequences per se and thereby does not provide adequate written description support for which structural features of any given polypeptide would predictably retain their functional activities.
Applicant is reminded that generally, 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 (Enzo Biochem, Inc. v. Gen- Probe Inc., 323 F.3d 956 (Fed. Cir. 2002); Noelle v. Lederman, 355 F.3d 1343 (Fed. Cir. 2004); Regents of the University of California v. Eli Lilly Co., 119 F.3d 1559 (Fed. Cir. 1997)). A patentee must disclose “a representative number of species within the scope of the genus of structural features common to the members of the genus so that one of skill in the art can visualize or recognize the member of the genus” (see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017) at page 1358). An adequate written description must contain enough information about the actual makeup of the claimed products — “a precise definition, such as structure, formula, chemic name, physical properties of other properties, of species falling with the genus sufficient to distinguish the gene from other materials”, which may be present in “functional terminology when the art has established a correlation between structure and function” (Amgen page 1361).
Adequate written description requires more than a mere statement that is part of the invention. See Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993) and Amgen Inc. v. Chungai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. In Fiddes v. Baird, 30 USPQ2d 1481, 1483, claims directed to mammalian FGF's were found unpatentable due to lack of written description for the broad class. The specification provided only the bovine sequence.
The University of California v. Eli Lilly and Co., 43 USPQ2d 1398, 1404, 1405 held that: ...To fulfill the written description requirement, a patent specification must describe an invention and does so in sufficient detail that one skilled in the art can clearly conclude that “the inventor invented the claimed invention.” Lockwood v. American Airlines Inc. 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) ("[T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus an Applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2dat1966.
MPEP § 2163.02 states, “[a]n objective standard for determining compliance with the written description requirement is, ‘does the description clearly allow person of ordinary skill in the art to recognize that he or she invented what is claimed’”. The courts have decided: the purpose of the “written description" requirement is broader than to merely explain how to "make and use"; the Applicant must convey with reasonable clarity to those skilled in the art, that as of the filing date sought, he or she was in possession of the invention. The invention is for purposes of the “written description” inquiry, whatever is now claimed. See 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 from its enablement provision; and adequate written description requires more than a mere statement that it is part of the invention and reference to a potential method for isolating it. Fiers v. Revel, 25 USPQ2d 1601, 1606 (CAFC 1993). And Amgen Inc. v. Chugai Pharmaceutical Co. Ltd., 18 USPQ2d 1016. Moreover, 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 the Applicant described distinguishing identifying characteristics sufficient to show that Applicant were in possession of the claimed invention at the time the application was filed.
Therefore, for all these reasons the specification lacks adequate written description, and one of skill in the art cannot reasonably conclude that Applicant had possession of the claimed invention at the time the instant application was filed.
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 24-30 and 42 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.
Claim 24 recites the limitation "the core polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 24 depends from claim 18, and there is no recitation of a core polypeptide in claim 18.
Claim 25 recites the limitation "the repeating core polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 25 depends from claim 18, and there is no recitation of a repeating core polypeptide in claim 18.
Claim 26 recites the limitation "the corona polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 26 depends from claim 18, and there is no recitation of a corona polypeptide in claim 18.
Claim 27 recites the limitation "the core polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 27 depends from claim 18, and there is no recitation of a core polypeptide in claim 18.
Claim 28 recites the limitation "the corona polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 28 depends from claim 18, and there is no recitation of a corona polypeptide in claim 18.
Claim 29 recites the limitation "the di-block”. There is insufficient antecedent basis for this limitation in the claim. Claim 27 depends from claim 18, and there is no recitation of a diblock in claim 18.
Claim 30 recites the limitation "the targeting polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 30 depends from claim 18, and there is no recitation of a targeting polypeptide in claim 18.
Claim 42 recites the limitation "the core polypeptide”. There is insufficient antecedent basis for this limitation in the claim. Claim 42 depends from claim 18, and there is no recitation of a core polypeptide in claim 18.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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) 18, 21, 22, 24, 26,27, 43 and 44 is/are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by Chilkoti et al. (US Patent Application 20180037609 A1, published February 8, 2018).
The instant claims are drawn to a protein nanoparticle comprising a fusion protein comprising at least one binding polypeptide and at least one unstructured polypeptide.
Chilkoti et al. teach a protein nanoparticle comprising a fusion protein formed from an environmentally responsive polypeptide which may encapsulate a therapeutic for delivery to a biological site fused to a polypeptide of interest, such as a therapeutics, carbohydrates, synthetic polymers, polynucleotides and oligonucleotides, including DNA, RNA, as well chemically synthesized small molecules (See paragraphs 0013 and 0073-0075). Chilkoti et al. teach that the polypeptide may be used for drug and therapeutic delivery (See paragraph 0073). Chilkoti et al. teach that targeted delivery is achieved by recognition, binding, or affinity of a particular receptor or other molecule that is associated with a tumor, wound, or disease by the nanoparticle (See paragraph 0073). Chilkoit et al. teach that the polypeptides may be formed which are block polymers and block polymers may include deblocks of the motifs (See paragraph 0063). Chilkoti et al. teach the environmentally responsive polypeptide comprises ten or more sequences selected from VPTGVG (SEQ ID NO: 34), VHPGVG (SEQ ID NO: 37), GRGDSPV (SEQ ID NO: 43), GRGDSPYQ (SEQ ID NO: 48) (See paragraph 0009). It should be noted that SEQ ID NO: 43 represents a corona polypeptide and SEQ ID NO: 48 represents a core polypeptide. SEQ ID NO: 43 is 100% identical to SEQ ID NO: 17 and SEQ ID NO: 48 is 100% identical to SEQ ID NO: 3 of the instant claims. Thus, Chilkoti et al. anticipate the claims.
Claim Status
No claims are allowed.
Conclusion
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/SANDRA CARTER/Examiner, Art Unit 1674
/VANESSA L. FORD/Supervisory Patent Examiner, Art Unit 1674