IP Library › Granted Patent US 12,252,512
Granted Patent B2
US 12,252,512 · App. 18/358,358 · Granted Mar 18, 2025

Mutated polypeptides, compositions comprising the same, and uses thereof

Inventors: Bruce C. Schnepp (Havertown, PA); Philip R. Johnson (Bryn Mawr, PA)
Assignee: Interius Biotherapeutics, Inc.
C07K14/145C07K2319/03C07K2319/30
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Quick Facts
Patent No.
US 12,252,512
App. No.
18/358,358
Granted
Mar 18, 2025
Kind
B2
Abstract

Provided for herein are viral particles comprising a heterologous viral glycoprotein and a targeting moiety, wherein the targeting moiety comprises a polypeptide comprising a formula of T-S 1 , wherein T is a target binding domain and S 1 is a stalk portion. The stalk portion may comprise a variant Fe domain. The stalk portion may comprise a flexible polypeptide domain. The targeting moiety comprising the formula T-S 1 may be incorporated into a viral particle to assist with targeting such particles to a specific cell type. Also provided for herein are compositions comprising the same, and methods of using the same.

Claims (53)

1. A viral particle comprising a heterologous viral glycoprotein and a targeting moiety, wherein the targeting moiety comprises a polypeptide having the formula T-S 1 , wherein T is a target binding domain and Sis a stalk portion,

wherein the heterologous viral glycoprotein is a VSV-G polypeptide comprising an amino acid sequence having at least 95% identity to SEQ ID NO: 2;

wherein the target binding domain (T) comprises a scFv antibody that binds to CD7, wherein the scFv comprises a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises a heavy chain complementarity determining region 1 (HCDR1) comprising the amino acid sequence of SEQ ID NO: 30, a HCDR2 comprising the amino acid sequence of SEQ ID NO: 31, and a HCDR3 comprising the amino acid sequence of SEQ ID NO: 32; and wherein the light chain variable region comprises a light chain complementarity determining region 1 (LCDR1) comprising the amino acid sequence of SEQ ID NO: 33, a LCDR2 comprising the amino acid sequence of SEQ ID NO: 34, and a LCDR3 comprising the amino acid sequence of SEQ ID NO: 35; and

wherein the stalk portion S 1 comprises a Fc protein comprising an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO: 103, and wherein the S1 stalk portion is attached to the surface of the viral particle through a transmembrane domain.

2. The viral particle of claim 1 , wherein the heavy chain variable region comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO: 36; and the light chain variable region comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO: 37.

3. The viral particle of claim 1 , wherein the scFv comprises an amino acid sequence having at least 95% sequence identity to the amino acid sequence of SEQ ID NO: 38.

4. The viral particle 1, wherein the VSV-G polypeptide comprises a mutation at position 182 as compared to SEQ ID NO: 2.

5. The viral particle 1, wherein the VSV-G polypeptide comprises a I182E or I182D mutation as compared to SEQ ID NO: 2.

6. The viral particle of claim 4 , wherein the VSV-G polypeptide further comprises a mutation at position 214 and/or position 352 of SEQ ID NO: 2.

7. The viral particle of claim 6 , wherein the mutation at position 182 is I182D or I182E, the mutation at position 214 is T214N, and the mutation at position 352 is T352A.

8. A method of infecting a cell, the method comprising contacting the cell with the viral particle of claim 1 .

9. The viral particle of claim 1 , wherein the heavy chain variable region comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO: 36; and the light chain variable region comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO: 37.

10. The viral particle of claim 1 , wherein the heavy chain variable region comprises the amino acid sequence of SEQ ID NO: 36; and the light chain variable region comprises the amino acid sequence of SEQ ID NO: 37.

11. The viral particle of claim 1 , wherein the scFv comprises an amino acid sequence having at least 98% sequence identity to the amino acid sequence of SEQ ID NO: 38.

12. The viral particle of claim 1 , wherein the scFv comprises the amino acid sequence of SEQ ID NO: 38.

13. The viral particle of claim 1 , wherein the VSV-G polypeptide comprises the amino acid sequence of SEQ ID NO: 23.

14. The viral particle of claim 1 , wherein the Fc protein comprises one or more mutations that correspond to L19A, L20A, N82A, P114G, 138A, H95A, or H220A of SEQ ID NO: 103.

15. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 2 and an I182E or an I182D mutation as compared to SEQ ID NO: 2;

the target binding domain (T) comprises an scFv comprising an amino acid sequence that is at least 95% identical to SEQ ID NO: 38, wherein the scFv comprises a HCDR1 comprising the amino acid sequence of SEQ ID NO: 30; a HCDR2 comprising the amino acid sequence of SEQ ID NO: 31; a HCDR3 comprising the amino acid sequence of SEQ ID NO: 32; a LCDR1 comprising the amino acid sequence of SEQ ID NO: 33; a LCDR2 comprising the amino acid sequence of SEQ ID NO: 34; and a LCDR3 comprising the amino acid sequence of SEQ ID NO: 35; and

wherein the Fc protein comprises an amino acid sequence having at least 95% identity to the amino acid sequence of SEQ ID NO: 104, provided that the Fc protein comprises the mutations of L19A, L20A, N82A, P114G, I38A, H95A, and H220A.

16. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 98% identical to SEQ ID NO: 2 and an I182E or an I182D mutation as compared to SEQ ID NO: 2;

the target binding domain (T) comprises an scFv comprising an amino acid sequence that is at least 98% identical to SEQ ID NO: 38, wherein the scFv comprises a HCDR1 comprising the amino acid sequence of SEQ ID NO: 30; a HCDR2 comprising the amino acid sequence of SEQ ID NO: 31; a HCDR3 comprising the amino acid sequence of SEQ ID NO: 32; a LCDR1 comprising the amino acid sequence of SEQ ID NO: 33; a LCDR2 comprising the amino acid sequence of SEQ ID NO: 34; and a LCDR3 comprising the amino acid sequence of SEQ ID NO: 35; and

wherein the Fc protein comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO: 104, provided that the Fc protein comprises the mutations of L19A, L20A, N82A, P114G, I38A, H95A, and H220A.

17. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 98% identical to SEQ ID NO: 2 and an I182E mutation as compared to SEQ ID NO: 2;

the target binding domain (T) comprises an scFv comprising an amino acid sequence that is at least 98% identical to SEQ ID NO: 38, wherein the scFv comprises a HCDR1 comprising the amino acid sequence of SEQ ID NO: 30; a HCDR2 comprising the amino acid sequence of SEQ ID NO: 31; a HCDR3 comprising the amino acid sequence of SEQ ID NO: 32; a LCDR1 comprising the amino acid sequence of SEQ ID NO: 33; a LCDR2 comprising the amino acid sequence of SEQ ID NO: 34; and a LCDR3 comprising the amino acid sequence of SEQ ID NO: 35; and

wherein the Fc protein comprises an amino acid sequence having at least 98% identity to the amino acid sequence of SEQ ID NO: 104, provided that the Fc protein comprises the mutations of L19A, L20A, N82A, P114G, I38A, H95A, and H220A.

18. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 95% identical to SEQ ID NO: 2 and an I182E or an I182D mutation as compared to SEQ ID NO: 2; and

the targeting moiety comprises an amino acid sequence having at least 95% identity to SEQ ID NO: 98.

19. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 98% identical to SEQ ID NO: 2 and an I182E or an I182D mutation as compared to SEQ ID NO: 2; and

the targeting moiety comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 98.

20. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises an amino acid sequence that is at least 98% identical to SEQ ID NO: 2 and an I182E mutation as compared to SEQ ID NO: 2; and

the targeting moiety comprises an amino acid sequence having at least 98% identity to SEQ ID NO: 98.

21. The viral particle of claim 1 , wherein the viral particle further comprises a nucleic acid molecule encoding a CAR.

22. The viral particle of claim 21 , wherein the CAR comprises an antigen binding domain that binds to CD20.

23. The viral particle of claim 22 , wherein the antigen binding domain that binds to CD20 comprises a polypeptide comprising a light chain and a heavy chain comprising: a heavy chain variable region of the heavy chain having at least 95% identity to an amino acid sequence of SEQ ID NO: 89; and a light chain variable region of the light chain having at least 95% identity to an amino acid sequence of SEQ ID NO: 90.

24. The viral particle of claim 22 , wherein the CAR comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 99.

25. The viral particle of claim 22 , wherein the CAR comprises an amino acid sequence having at least 98% identity to an amino acid sequence of SEQ ID NO: 99.

26. The viral particle of claim 22 , wherein the CAR comprises the amino acid sequence of SEQ ID NO: 99.

27. The viral particle of claim 1 , wherein:

the VSV-G polypeptide comprises the amino acid sequence of SEQ ID NO: 23; and

the targeting moiety comprises the amino acid sequence of SEQ ID NO: 98.

28. The viral particle of claim 27 , wherein the viral particle further comprises a nucleic acid molecule encoding a CAR.

29. The viral particle of claim 28 , wherein the CAR comprises an antigen binding domain that binds to CD20.

30. The viral particle of claim 29 , wherein the antigen binding domain that binds to CD20 comprises a polypeptide comprising a light chain and a heavy chain comprising: a heavy chain variable region of the heavy chain having at least 95% identity to an amino acid sequence of SEQ ID NO: 89; and a light chain variable region of the light chain having at least 95% identity to an amino acid sequence of SEQ ID NO: 90.

31. The viral particle of claim 29 , wherein the CAR comprises an amino acid sequence having at least 95% identity to an amino acid sequence of SEQ ID NO: 99.

32. The viral particle of claim 29 , wherein the CAR comprises an amino acid sequence having at least 98% identity to an amino acid sequence of SEQ ID NO: 99.

33. The viral particle of claim 29 , wherein the CAR comprises the amino acid sequence of SEQ ID NO: 99.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 12, 2023
From: SCHNEPP, BRUCE C.; JOHNSON, PHILIP R.; ANDORKO, JAMES I.
To: INTERIUS BIOTHERAPEUTICS, INC.
Reel/Frame 065202/0799 →
Continuity (5)
Provisional Application 63507783 · Jun 13, 2023
Provisional Application 63503815 · May 23, 2023
Provisional Application 63391939 · Jul 25, 2022
Provisional Application 63391930 · Jul 25, 2022
Related Publication 20240059744A1 · Feb 22, 2024
References Cited (121)
US 4439196A · Higuchi · 1984 [cited by applicant]
US 4447224A · DeCant, Jr. et al. · 1984 [cited by applicant]
US 4447233A · Mayfield · 1984 [cited by applicant]
US 4487603A · Harris · 1984 [cited by applicant]
US 4596556A · Morrow et al. · 1986 [cited by applicant]
US 4790824A · Morrow et al. · 1988 [cited by applicant]
US 4816567A · Cabilly et al. · 1989 [cited by applicant]
US 4941880A · Burns · 1990 [cited by applicant]
US 4946778A · Ladner et al. · 1990 [cited by applicant]
US 5064413A · Mckinnon et al. · 1991 [cited by applicant]
US 5260203A · Ladner et al. · 1993 [cited by applicant]
US 5312335A · Mckinnon et al. · 1994 [cited by applicant]
US 5383851A · Mckinnon, Jr. et al. · 1995 [cited by applicant]
US 5399163A · Peterson et al. · 1995 [cited by applicant]
US 6005079A · Casterman et al. · 1999 [cited by applicant]
US 6096002A · Landau · 2000 [cited by applicant]
US 6261567B1 · Hart et al. · 2001 [cited by applicant]
US 6620135B1 · Weston et al. · 2003 [cited by applicant]
US 11767366B1 · Russell et al. · 2023 [cited by applicant]
US 20070042368A1 · Zehentner-Wilkinson et al. · 2007 [cited by applicant]
US 20080227736A1 · Chen et al. · 2008 [cited by applicant]
US 20090324604A1 · Liu et al. · 2009 [cited by applicant]
US 20100196419A1 · Compans et al. · 2010 [cited by applicant]
US 20180036429A1 · Acharjee · 2018 [cited by applicant]
US 20180044425A1 · Ågerstam et al. · 2018 [cited by applicant]
US 20180371064A1 · Fusil et al. · 2018 [cited by applicant]
US 20190055568A1 · Puléet al. · 2019 [cited by applicant]
US 20190241655A1 · Cua et al. · 2019 [cited by applicant]
US 20200216502A1 · Albertini et al. · 2020 [cited by applicant]
US 20200371088A1 · Birnbaum et al. · 2020 [cited by applicant]
US 20210087271A1 · Pejchal et al. · 2021 [cited by applicant]
US 20210106632A1 · Kim et al. · 2021 [cited by applicant]
US 20210317209A1 · Chu et al. · 2021 [cited by applicant]
US 20210347913A1 · Sagert et al. · 2021 [cited by applicant]
US 20220098271A1 · Gill et al. · 2022 [cited by applicant]
US 20220133790A1 · Gehrke et al. · 2022 [cited by applicant]
US 20230279363A1 · Russell et al. · 2023 [cited by applicant]
EP 0404097A2 · 1990 [cited by applicant]
WO WO1988001649A1 · 1988 [cited by applicant]
WO WO1993011161A1 · 1993 [cited by applicant]
WO WO1994004678A1 · 1994 [cited by applicant]
WO WO1994025591A1 · 1994 [cited by applicant]
WO WO1997009433A1 · 1997 [cited by applicant]
WO WO2004041862A2 · 2004 [cited by applicant]
WO WO2013153391A1 · 2013 [cited by applicant]
WO WO2015015489A1 · 2015 [cited by applicant]
WO WO2016065323A2 · 2016 [cited by applicant]
WO WO2018014039A1 · 2018 [cited by applicant]
WO WO2019200007A1 · 2019 [cited by applicant]
WO WO2020223240A1 · 2020 [cited by applicant]
WO WO2021000530A1 · 2021 [cited by applicant]
WO WO2022013872A1 · 2022 [cited by applicant]
WO WO2022023529A1 · 2022 [cited by applicant]
WO WO2022067262A1 · 2022 [cited by applicant]
WO WO2022140556A1 · 2022 [cited by applicant]
WO WO2022183072A1 · 2022 [cited by applicant]
WO WO2023107593A2 · 2023 [cited by applicant]
WO WO2023114884A2 · 2023 [cited by applicant]
WO WO2023170681A1 · 2023 [cited by applicant]
Vajdos, F. et al., 2002, JMB, pp. 415-428. [cited by examiner]
Bedouelle, H. et al., Febs J., 2006, pp. 34-46. [cited by examiner]
50YL Albertini, A.A et al., “50YL, VSV G CR2”, RCSB PDB, Mar. 21, 2018, last revised Apr. 18, 2018, available at https://www.rcsb.org/structure/50YL (last accessed Jan. 3, 2024), 6 pages. [cited by applicant]
50Y9—Albertini, A.A. et al., “50Y9, VSV G CR3”, RCSB PDB, Mar. 21, 2018, last revised Apr. 18, 2018, available at https://www.rcsb.org/structure/50Y9 (last accessed Jan. 3, 2024), 6 pages. [cited by applicant]
Albertini et al., “Molecular and Cellular Aspects of Rhabdovirus Entry,” Viruses (2012) 4:117-129. [cited by applicant]
Baert et al., “Influence of Immunogenicity on the Long-Term Efficacy of Infliximab in Crohn's Disease,” (2003) New Engl. J. Med. 348:601-608. [cited by applicant]
Beniaminovitz et al., “Prevention of Rejection in Cardiac Transplantation by Blockade of the Interleukin-2 Receptor with a Monoclonal Antibody,” (2000) New Engl. J. Med. 342(9):613-619. [cited by applicant]
C. Dunbar et al, “Gene therapy comes of age”, 359 Science 1 (2018). [cited by applicant]
Chothia et al., “Canonical Structures for the Hypervariable Regions of Immunoglobulins,” (1987) J. Mol. Biol. 196:901-917. [cited by applicant]
Chothia et al., “Conformations of Immunoglobulin Hypervariable Regions,” (1989) Nature 342: 877-883. [cited by applicant]
Clackson et al., “Making Antibody Fragments Using Phage Display Libraries,” (1991) Nature 352:624-628. (Abstract Only). [cited by applicant]
Dobson CS, Reich AN, Gaglione S, Smith BE, Kim EJ, Dong J, Ronsard L, Okonkwo V, Lingwood D, Dougan M, Dougan SK, Birnbaum ME. Antigen identification and high-throughput interaction mapping by reprogramming viral entry.… [cited by applicant]
Donald J. Voet et al., “Fundamentals of biochemistry” (2008), chapters 3 and 4, 39-82. [cited by applicant]
Duverge and M. Negroni, “Pseudotyping lentiviral vectors: when the clothes make the virus”, 12 VIRUSES 1311 (2020). [cited by applicant]
E. Pettersen et al., “UCSF Chimera—A visualization system for exploratory research and analysis”, 25 J. Comp. Chem. 1605 (2004). [cited by applicant]
Edelman, G M et al. “The covalent structure of an entire gammaG immunoglobulin molecule.” [cited by applicant]
F. Amirache et al, “Mystery solved: VSV-G-LVs do not allow efficient gene transfer into unstimulated T cells, B cells, and HSCs cause they lack the LDL receptor”, 123 BLOOD 1422 (2014). [cited by applicant]
Finkelshtein et al., “LDL Receptor and its Family Members Serve as the Cellular Receptors for Vesicular Stomatitis Virus,” PNAS (2013) 110(18): 7306-7311. [cited by applicant]
Ghosh et al., “Natalizumab for Active Crohn's Disease,” (2003) New Engl. J. Med. 348:24-32. [cited by applicant]
Herold et al., “Anti-CD3 Monoclonal Antibody in New-Onset Type 1 Diabetes Mellitus,” (2002) New Engl. J. Med. 346(22): 1692-1698. [cited by applicant]
Holliger et al., “Diabodies: Small Bivalent and Bispecific Antibody Fragments,” (1993) Proc. Natl. Acad. Sci. USA 90: 6444-6448. [cited by applicant]
Holliger et al., “Engineered Antibody Fragments and the Rise of Single Domains,” (2005) Nat. Biotechnol. 23(9): 1126-1136. [cited by applicant]
Hwang et al., “Engineering a Serum-Resistant and Thermostable Vesicular Stomatitis Virus G Glycoprotein for Pseudotyping Retroviral and Lentiviral Vectors,” Gene Ther. (Aug. 2013) 20(8):807-815. [cited by applicant]
International Search Report and Written Opinion for PCT/US2022/081616, dated Jun. 15, 2023, 14 pages. [cited by applicant]
J. Rose and C. Gallione, “Nucleotide Sequences of the mRNAs Encoding the Vesicular Stomatitis Virus G and M Proteins Determined from cDNA Clones Containing the Complete Coding Regions”, 39 J. Virology 519 (1981). [cited by applicant]
Kabat et al., “Unusual Distributions of Amino Acids in Complementarity-Determining (Hypervariable) Segments of Heavy and Light Chains of Immunoglobulins and Their Possible Roles in Specificity of Antibody-Combining Site… [cited by applicant]
Kabat, “The Structural Basis for Antibody Complementary,” Adv. Prot. Chem. (1978) 32:1-75. (Abstract Only). [cited by applicant]
[cited by applicant]
[cited by applicant]
L. Naldini et al., “In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector”, 272 SCIENCE 263 (1996). [cited by applicant]
Lathe, “Synthetic Oligonucleotide Probes Deduced from Amino Acid Sequence Data,” J. Molec. Biol. (1985) 183:1-12. [cited by applicant]
Lee et al., “ASTCT Consensus Grading for Cytokine Release Syndrome and Neurologic Toxicity Associated with Immune Effector Cells,” Biol. Blood Marrow Transplant (2019) 25:625-638. [cited by applicant]
Lipsky et al., “Infliximab and Methotrexate in the Treatment of Rheumatoid Arthritis,” (2000) New Engl. J. Med. 343(22): 1594-1602. [cited by applicant]
Liu et al., “Chimeric Mouse-Human IgG1 Antibody that can Mediate Lysis of Cancer Cells,” Proc Natl. Acad. Sci., USA (1987) 84:3439-3443. [cited by applicant]
Liu et al., “Production of a Mouse-Human Chimeric Monoclonal Antibody to CD20 with Potent Fc-Dependent Biologic Activity,” J. Immunology (1987) 139(10):3521-3526. [cited by applicant]
Liu et al., “Randomised, Double Blind, Placebo Controlled Study of Interferon Beta-1a in Relapsing-Remitting Multiple Sclerosis Analysed by Area under Disability/Time Curves,” J. Neurol. Neurosurg. Psych. (1999) 67:451-… [cited by applicant]
Marks et al., “By-Passing Immunization,” J. Mol. Biol. (1991) 222: 581-597. [cited by applicant]
Michaels et al., “Preclinical proof of concept for VivoVec, a lentiviral-based platform for in vivo CAR T-cell engineering”, [cited by applicant]
Milgrom et al., “Treatment of Allergic Asthma with Monoclonal Anti-IgE Antibody,” New Engl. J. Med. (1999) 341:1966-1973. [cited by applicant]
Muller, “[43] Determination of Affinity and Specificity of Anti-Hapten Antibodies by Competitive Radioimmunoassay,” Meth. Enzymol. (1983) 92:589-601. (Abstract Only). [cited by applicant]
Muyldermans et al., “Recognition of Antigens by Single-Domain Antibody Fragments: the Superfluous Luxury of Paired Domains,” (2001) Trends Biochem. Sci. 26(4):230-235. [cited by applicant]
N. Depolo et al, “VSV-G Pseudotyped lentiviral vector produced in human cells are inactivated by human serum”, 2 Molecular therapy 218 (2000). [cited by applicant]
Neelapu et al., “Chimeric Antigen Receptor T-Cell Therapy—Assessment and Management of Toxicities,” Nat. Rev. Clin. Oncology (Jan. 2018) 15(1): 47-62. [cited by applicant]
Nikolic et al., “Structural Basis for the Recognition of LDL-Receptor Family Members by VSV Glycoprotein,” Nature Comm. (2018) 9(1029): 1-12. [cited by applicant]
Notice of Allowance for U.S. Appl. No. 18/066,420 dated Jul. 26, 2023. [cited by applicant]
Notice of Allowance for U.S. Appl. No. 18/157,421 dated Aug. 25, 2023. [cited by applicant]
Notification Of Transmittal Of The International Search Report and The Written Opinion Of The International Searching Authority, dated Feb. 22, 2024, 139 pages. [cited by applicant]
Pluckthun, “Antibodies from [cited by applicant]
Portielji et al., “IL-12: A Promising Adjuvant for Cancer Vaccination,” Cancer Immunol. Immunother. (2003) 52:133-144. [cited by applicant]
Presta, “Selection, Design, and Engineering of Therapeutic Antibodies,” J. Allergy Clin. Immunol. (2005) 116(4):731-736. [cited by applicant]
R. Florkiewicz and J. Rose, “A Cell Line Expressing Vesicular Stomatitis Virus Glycoprotein fuses at low ph”, 225 SCIENCE 721 (1984). [cited by applicant]
Reichmann et al., “Reshaping Human Antibodies for Therapy,” Nature (1988) 332(6162):323-327. [cited by applicant]
Roche et al., “Crystal Structure of the Low-pH Form of the Vesicular Stomatitis Virus Glycoprotein G,” Science (Jul. 14, 2006) 313:187-191. [cited by applicant]
Roche et al., “Structure of the Prefusion Form of the Vesicular Stomatitis Virus Glycoprotein G,” Science (Feb. 9, 2007) 315:843-848. [cited by applicant]
S. P. J. Whelan, “Vesicular stomatis Virus”, Encyclopedia of virology 291 (Elsevier Itd) (2008). [cited by applicant]
S. Roche et al, “Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited”, 65 Cell Mol. Life Sci. 1716 (2008). [cited by applicant]
Slamon et al., “Use of Chemotherapy Plus a Monoclonal Antibody against HER2 for Metastatic Breast Cancer that Overexpresses HER2,” (2001) New Engl. J. Med. 344(11):783-792. [cited by applicant]
Teachey et al., “Identification of Predictive Biomarkers for Cytokine Release Syndrome after Chimeric Antigen Receptor T-cell Therapy for Acute Lymphoblastic Leukemia,” Cancer Discov. (Jun. 2016) 6(6):664-679. [cited by applicant]
Tsurushita et al., “Humanization of a Chicken Anti-IL-12 Monoclonal Antibody,” J. Immuno. Methods (2004) vol. 295, pp. 9-19. [cited by applicant]
Yang et al., “A Randomized Trial of Bevacizumab, an Anti-Vascular Endothelial Growth Factor Antibody, for Metastatic Renal Cancer,” (2003) New Engl. J. Med. 349(5): 427-434. [cited by applicant]
Zardecki et al., “RCSB Protein Data Bank: A Resource for Chemical, Biochemical, and Structural Explorations of large and small biomolecules”, 93 J. Chem. Educ. 569(2016). [cited by applicant]
Declaration of Proffesor John K. Rose, Phd in Support of Petition for Post-Grant Review of U.S. Appl. No. 11,767,366 Before the Patent Trial and Appeal Board [cited by applicant]