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 .
1. Claims 1-16 are pending and under consideration.
Priority
2. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
It is noted that the Examiner has established a priority date of May 24, 2022 for claims 1-16 of the instant application because the priority of the instantly claimed invention is based on the prior filed application KR10-2021-0067276 which is written Korean. The prior filed applications have not been translated and the Examiner is unable to determine the information in the document.
If Applicant disagrees with any rejection set forth in this action based on examiner's establishment of a priority date of May 24, 2022 for claims 1-16, then Applicant is invited to submit a proper translation of the priority document and to point to page and line where support can be found establishing an earlier priority date. If Applicant choses to file a translation, then the translation must be filed together with a statement that the translation of the certified copy is accurate. See 35 U.S.C. 119 (b)(3), 37 C.F.R. 1.55(g)(3)(4), 37 C.F.R. 1.78(d)(7), and MPEP 1895.01.
Improper Markush Grouping Rejection
3. Claim 2 is 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 a monobody of the chimeric antigen receptor that specifically bind the various proteins of claim 2 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: Each of the proteins of claim 2 are structurally distinct proteins with distinct primary, secondary and tertiary structures. Thus, a monobody of the chimeric antigen receptor that binds a particular protein would have a distinct structure to allow it to specifically bind a particular protein and not bind to other proteins. Thus, the structure of the monobodies of the chimeric antigen receptor would not be similar to each other and they would not have a common use as each monobody is specific for a distinct protein.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
4. Claim 2 is 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 2 recites the protein GPR56 ECR. Although GPR56 is known G-protein coupled receptor (see Liu et al. (Genomics 1999 55: 296-305), abstract), the specification does not define what GPR56 ECR is. Thus scope of the term GPR56 ECR is unclear and indefinite.
Claim 2 also recites the proteins Fluc family and Fluc homologues. The specification and claims do not define what proteins are encompassed by Fluc family and Fluc homologues. Thus scope of the term by Fluc family and Fluc homologues is unclear and indefinite.
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.
5. Claims 1-3 and 5-16 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.
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, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. “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).
On 22 February 2018, the USPTO provided a Memorandum clarifying the Written Description Guidelines for claims drawn to antibodies, which can be found at www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. That Memorandum indicates that, in compliance with recent legal decisions, the disclosure of a fully characterized antigen no longer is sufficient written description of an antibody to that antigen. Accordingly, the instant claims have been evaluated in view of that guidance.
Scope of the claimed genus
The claims are drawn broadly drawn to a monobody based chimeric antigen receptor comprising an extracellular ligand binding domain comprising a monobody. Thus the claims are broadly drawn to a very large genus of any monobody based chimeric antigen receptor targeting any antigen, some of which are listed in claim 2, with any extracellular ligand binding domain comprising any monobody.
State of the Relevant Art
The general structure of chimeric antigen receptors is well known in the art at the time the invention was filed. See Jena et al. (Blood 19 Aug. 2010, 116 (7): 1035-1044), e.g., abstract and Fig. 1 and June and Sadelain (N Engl. J. Med 2018: 379: 647-73), e.g., Figs. 1 and 2. Additionally, art at the time the invention was filed, one of skill in the could have screened for monobodies to a particular antigen. See Koide and Koide (Methods in molecular biology (Clifton, N.J.), (2007) Vol. 352, pp. 95-109).
Thus overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those monobodies with desired functional properties for use in a chimeric antigen receptor was high. However, even if a selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify monobodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”). Absent the structure of a particular monobody to a particular antigen, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what a monobody with a particular set of functional properties would look like structurally.
Summary of Species disclosed in the original specification
The specification teaches the a chimeric antigen receptor directed to EphA2 with an anti-EphA2 monobody binding domain. See Example 1 and Fig. 1. The anti-EphA2 monobody binding domain has the sequence of SEQ ID NO: 8, encoded by SEQ IN NO: 2.
Are the disclosed species representative of the claimed genus?
MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
The specification discloses the reduction to practice one chimeric antigen receptor directed to EphA2 with an anti-EphA2 monobody binding domain. The specification does not actually produce any other chimeric antigen receptors with monobody binding domains or produce other monobodies for use in a chimeric antigen receptor. Monobodies produced by different methods to different antigens or epitopes would have been generally expected to be highly structurally diverse to allow for the specific binding to different antigens or epitopes Thus, while applicant has described one chimeric antigen receptor directed to EphA2 with an anti-EphA2 monobody binding domain, the genus of a monobody based chimeric antigen receptor comprising an extracellular ligand binding domain comprising a monobody is very large and there is only one described species for the genus. The described species therefore cannot be considered representative of the genus of a monobody based chimeric antigen receptor comprising an extracellular ligand binding domain comprising a monobody . See e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (Fed. Cir. 2014).
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied 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. To meet this requirement in the instant case, the specification must describe structural features that convey the claimed binding activity, a prerequisite for utility in the recited methods of treating.
The specification does not describe what residues within the monobody confer the binding activity claimed. Accordingly, the skilled artisan would not be able to discern a structure/function correlation for monobodies for the large genus of monobodies to be used in the claimed chimeric antigen receptor
For all of the reasons presented above, one of skill in the art would not know which of the countless other monobodies encompassed by the independent claims that meet the highly general structural requirements of the claims would also be able to specifically bind proteins to be targeted by the monobody chimeric antigen receptor. Neither the specification nor the dependent claims provide sufficient additional structure or a structure/function correlation to provide an adequate written description of the genus claimed. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of a monobody based chimeric antigen receptor comprising an extracellular ligand binding domain comprising a monobody as broadly claimed. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as broadly claimed.
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.
6. Claim(s) 1-2 and 5-16 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by WO 2020/146706-A2 (Liu et al. July 16, 2020, filed Jan. 10, 2020), “Liu.
Liu teaches in claims 1-5 and 14:
1. A chimeric antigen receptor (CAR) comprising: (a) an extracellular tumor antigen binding moiety comprising a first binding domain and a second binding domain; (b) a CD8a hinge; (c) a CD8a transmembrane domain; (d) an intracellular cytoplasmic domain comprising a CD3 zeta signaling domain and a co-stimulatory domain from CD28.
2. The chimeric antigen receptor of claim 1, wherein the first binding domain binds a first epitope of a first tumor antigen, and the second binding domain binds a second epitope of the first tumor antigen.
3 . The chimeric antigen receptor of claim 2, wherein the first tumor antigen is EGFR or HER-2.
4. The chimeric antigen receptor of claim 2, wherein the first binding domain comprises a single domain antibody mimic that binds to a first epitope of EGFR, and the second binding domain comprises a single domain antibody mimic that binds to a second epitope of EGFR.
5. The chimeric antigen receptor of claim 4, wherein the single domain antibody mimic is a monobody comprising an FN3 domain or an affibody comprising a three helix bundle Z domain, or a DARPin.
14. The chimeric antigen receptor of claim 13, wherein the first binding domain comprises a monobody that binds to an epitope of EGFR and the second binding domain comprises a DARPin that binds to an epitope of HER-2.
See also the abstract and ¶¶ 0006, 0024, and 0033-0047.
Liu teaches expressing the EGFR monobody chimeric receptors with retroviral expression vectors in T cells. See ¶¶ 0008-0011, Example 1 and Figs. 2-5.
Liu teaches T cells comprising the bispecific EGFR monobody chimeric receptors had antitumor activity against lymphoma cells and pancreatic cancers. See Example 2, ¶¶ 0053 and 0066, and Figs. 3 and 4.
Regarding claims 14-16, a pharmaceutical composition for preventing or treating cancer is/are intended use(s) of the immune cell according to claim 12, which does not result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art and thus is not given weight for comparison of the claims with the prior art.
6. Claim(s) 1-3 and 5-16 are rejected under 35 U.S.C. 102(a)(1) and 102(a)(2) as being anticipated by WO 2019/099440 A1 (Hilbert et al. May 23, 2019), “Hilbert”.
Hilbert teaches a multi-functional chimeric antigen receptor (CAR)-based compositions and their use in directing immune responses to target cells. The compositions have uses that include treating hyperproliferative disorders such as cancer. The provided methods generally include the use of a CAR cell in combination with an Adapter. The Adapter confers the ability to modulate, alter, and/or redirect CAR cell-mediated immune response in vitro and in vivo. See Abstract and ¶¶ 0004.
Hilbert teaches the disclosure provides a composition comprising: (a) a cell expressing a CAR, wherein the CAR comprises an (i) an ADBD that binds to a first AD on a target cell, (ii) a transmembrane domain, and (iii) an intracellular domain; and (b) an Adapter which comprises (i) said first AD and (ii) an ADBD that binds to a second AD on said target cell. See ¶¶ 0006.
Hilbert teaches the disclosure provides a composition comprising: (a) a cell expressing a CAR, wherein the CAR comprises (i) an ADBD that is an alternative scaffold binding domain (ASBD) that binds to a first AD, (ii) a transmembrane domain, and (iii) an intracellular domain; and (b) an Adapter which comprises (i) said first AD and (ii) an ADBD that binds to a second AD on a target cell. See ¶¶ 0008.
Hilbert teaches that the ASBD is an adnectin-based AD binding domain, i.e. a monobody. The adnectin-based binding domain is derived from the tenth domain of fibronectin type III (l0Fn3). See ¶¶ 0220-0221.
Hilbert teaches that the CAR can target tumor antigens like the ephrin receptor, EphA2 and VEGFR2 See ¶¶ 0148.
Hilbert teaches the transmembrane can be from the alpha, beta or zeta chain of the T cell receptor; CD28, CD3 epsilon, CD45, CD4, CDS, CD8, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD137, and CD154. See ¶¶ 0380-0382.
Hilbert teaches the CAR can comprise a CD3z intracellular signaling domain and a CD28, 41BB, CD27 or CD134/OX40 co-stimulatory domain. See p. 18-¶¶ 16-21 and ¶¶ 0384-0397.
Hilbert teaches the CAR can comprise a linker/hinge. See ¶¶ 0122, 0372, and 0375-0377. See ¶¶
Hilbert teaches the CARs can be expression from polynucleotide expression vectors in T cells. See ¶¶ 0136-0137 and 0398-407.
Hilbert teaches the cells expressing CARs can be pharmaceutically acceptable compositions for treatment See ¶¶ 0507, 0512, 0513, 0553-0559.
Hilbert teaches treat cancer, including pancreatic, ovarian and prostate. . See abstract, 0045-0062, 0146-0147, and 0454.
Regarding claims 14-16, a pharmaceutical composition for preventing or treating cancer is/are intended use(s) of the immune cell according to claim 12, which does not result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art and thus is not given weight for comparison of the claims with the prior art.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
7. Claim(s) 4 is rejected under 35 U.S.C. 103 as being unpatentable over WO 2019/099440 A1 (Hilbert et al. May 23, 2019), “Hilbert” as applied to claims 1-3 and 5-16 above, and further in view of WO 2019/094669 A2 (Butterfield et al. May 16, 2019), “Butterfield”.
Hilbert teaches as set forth above, but does not teach the monobody of SEQ ID NO: 8.
Butterfield teaches EphA2 targeted-monobody of SEQ ID NO: 24 as a targeting domain, which comprises SEQ ID NO: 8. See p. 25-lines 4-20 and Appendix.
It would have been prima facie obvious at the time the invention was filed given that the level of skill in the art was high to combine the teachings of Hilbert and Butterfield and use the EphA2 targeted-monobody of SEQ ID NO: 24 of Butterfield in the CARs of Hilbert because Hilbert teaches targeting CARs to EphA2 and using adnectin/monobody binding domains in the CARs and Butterfield teaches using the EphA2, SEQ ID NO: 24 monobody as a targeting domain. One would have been motivated to use the EphA2, SEQ ID NO: 24 monobody for the EphA2 CARs of Hilbert because it was known in the art to target EphA2.
Conclusion
8. No claims allowed.
9. Any inquiry concerning this communication or earlier communications from the examiner should be directed to PETER J REDDIG whose telephone number is (571)272-9031. The examiner can normally be reached M-F 8:30-5:30 Eastern Time.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Greg Emch can be reached at 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/PETER J REDDIG/ Primary Examiner, Art Unit 1646
APPENDIX
Alignment of SEQ ID NO: 8 with SEQ ID NO: 24 of Butterfield
ID BGJ19250 standard; protein; 90 AA.
XX
AC BGJ19250;
XX
DT 11-JUL-2019 (first entry)
XX
DE EphA2 targeted-monobody (polypeptide targeting domain), SEQ ID 24.
XX
KW Epha2 tyrosine kinase receptor; drug delivery; monobody; nanotechnology;
KW protein engineering; protein production.
XX
OS Unidentified.
XX
FH Key Location/Qualifiers
FT Region 23..29
FT /note= "These residues can be changed depending on the
FT desired binding specificity to a particular target"
FT Region 51..54
FT /note= "These residues can be changed depending on the
FT desired binding specificity to a particular target"
FT Region 76..82
FT /note= "These residues can be changed depending on the
FT desired binding specificity to a particular target"
XX
CC PN WO2019094669-A2.
XX
CC PD 16-MAY-2019.
XX
CC PF 09-NOV-2018; 2018WO-US059943.
XX
PR 09-NOV-2017; 2017US-0583937P.
PR 18-JUN-2018; 2018US-0686576P.
XX
CC PA (UNIW ) UNIV WASHINGTON.
XX
CC PI Butterfield G, Lajoie MJ, King NP, Baker D, Ellis D;
XX
DR WPI; 2019-43525D/39.
XX
CC PT Isolated polypeptide for preparing nanostructure used for targeting
CC PT delivery of therapeutic in vitro or in vivo, includes specified amino
CC PT acid sequence.
XX
CC PS Claim 43; SEQ ID NO 24; 195pp; English.
XX
CC The present invention relates to a novel isolated polypeptide comprising
CC an amino acid sequence or its variant, useful for preparing a
CC nanostructure for targeting a delivery of therapeutic in vitro or in
CC vivo. The polypeptide further comprises a targeting domain linked to the
CC polypeptide and a polypeptide stabilization domain having sequences of
CC SEQ ID NOs: 58-518 (see BGJ19284-BGJ19744) and SEQ ID NOs: 593-595 (see
CC BGJ19819-BGJ19821). The invention further provides: (1) a nanostructure,
CC comprises (a) a plurality of first assemblies, each first assembly
CC comprising a plurality of identical first poly peptides, wherein the
CC first polypeptides comprise the polypeptide; and (b) a plurality of
CC second assemblies, each second assembly comprising a plurality of
CC identical second polypeptides, wherein the second polypeptides comprise
CC the polypeptide; (2) a polynucleotide encoding the polypeptide; (3) a
CC recombinant expression vector comprising the polynucleotide operably
CC linked to a control sequence; (4) a recombinant host cell comprising the
CC recombinant expression vector; (5) a composition comprising a synthetic
CC nucleocapsid composed of a computationally-designed capsid derived from
CC proteins that are of non-viral and/or non-container origin and designed
CC to contact each other, wherein the capsid contacts a nucleic acid
CC encoding its own genetic information; (6) a method for generating
CC polypeptides that self-assemble and package nucleic acid that encodes the
CC polypeptides; (7) a method for generating the polypeptides or
CC nanostructures; and (8) a synthetic nucleocapsid comprising a plurality
CC of first oligomeric polypeptides, each first oligomeric polypeptide
CC comprising a plurality of identical first synthetic polypeptides, a
CC plurality of second oligomeric polypeptides, each second oligomeric
CC polypeptide comprising a plurality of identical second synthetic
CC polypeptides, where the first oligomeric polypeptides and the second
CC oligomeric polypeptides interact non-covalently and assemble into an
CC icosahedral geometry with an interior cavity (a synthetic capsid) that
CC contacts a nucleic acid encoding the polypeptide components of the
CC synthetic nucleocapsid, where the synthetic nucleocapsid does not require
CC viral proteins or naturally-occurring non-viral container proteins, and
CC the first oligomeric polypeptides and second oligomeric polypeptides are
CC selected to provide a positive net charge on the interior surface.
XX
SQ Sequence 90 AA;
Query Match 100.0%; Score 479; Length 90;
Best Local Similarity 100.0%;
Matches 90; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 VSDVPRDLEVVAATPTSLLISWYYPFCAFYYRITYGETGGNSPVQEFTVPRPSDTATISG 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 VSDVPRDLEVVAATPTSLLISWYYPFCAFYYRITYGETGGNSPVQEFTVPRPSDTATISG 60
Qy 61 LKPGVDYTITVYAVTCLGSYSRPISINYRT 90
||||||||||||||||||||||||||||||
Db 61 LKPGVDYTITVYAVTCLGSYSRPISINYRT 90
Prosecution Insights