IP Library › Granted Patent US 12,398,177
Granted Patent B2
US 12,398,177 · App. 17/231,415 · Granted Aug 26, 2025

SIV envelope trimer

Inventors: Raiees Andrabi (La Jolla, CA); Dennis Burton (La Jolla, CA)
Assignee: THE SCRIPPS RESEARCH INSTITUTE
C07K5/08A61K9/127A61K9/51A61K39/21A61K39/39A61K47/08A61K47/10A61P31/18C12N7/00C12N15/86G01N33/56988A61K2039/545A61K2039/55505A61K2039/55555A61K2039/55566C12N2740/15022C12N2740/15034C12N2750/14143
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Quick Facts
Patent No.
US 12,398,177
App. No.
17/231,415
Granted
Aug 26, 2025
Kind
B2
Abstract

The present application relates to epitope-targeted SIV and HIV vaccines. The invention provides novel envelope glycoproteins which may be utilized as HIV-1 vaccine immunogens, antigens for crystallization, and for identification of broadly neutralizing antibodies. The invention encompasses preparation and purification of immunogenic compositions which are formulated into vaccines of the present invention.

Claims (27)

1. An engineered or non-naturally occurring molecule that binds to a Human Immunodeficiency Virus (HIV-1) broadly neutralizing antibody (bnAb),

wherein the molecule comprises the amino acid sequence of SEQ ID NO: 28.

2. The molecule of claim 1 ,

wherein the HIV-1 bnAb comprises three complementarity determining regions (CDRs) of a heavy chain variable domain, a first CDR of which comprising the amino acid sequence of SEQ ID NO: 33, a second CDR of which comprising the amino acid sequence of SEQ ID NO: 34, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 35,

and three CDRs of a light chain variable domain, a first CDR of which comprising the amino acid sequence of SEO ID NO: 42, a second CDR of which comprising the amino acid sequence of 43, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 44.

3. The molecule of claim 1 , wherein the HIV-1 bnAb comprises three complementarity determining regions (CDRs) of a heavy chain variable domain, a first CDR of which comprising the amino acid sequence of SEQ ID NO: 50, a second CDR of which comprising the amino acid sequence of SEQ ID NO: 51, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 52, and three CDRs of a light chain variable domain, a first CDR of which comprising the amino acid sequence of SEQ ID NO: 59, a second CDR of which comprising the amino acid sequence of SEQ ID NO: 60, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 61.

4. An engineered or non-naturally occurring molecule that binds to a Human Immunodeficiency Virus (HIV-1) broadly neutralizing antibody (bnAb), wherein the bnAb binds to the V2 apex region of HIV-1 envelope, wherein the molecule comprises an amino acid sequence comprising SEO ID NO: 28 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 28.

5. A nucleic acid encoding the molecule of claim 1 .

6. A vector comprising a regulatory element operable in a eukaryotic cell operably linked to the nucleic acid of claim 5 , wherein the vector comprises a viral vector.

7. A method of eliciting an immune response in a mammal or stimulating an HIV-1 broadly neutralizing antibody (bnAb) comprising administering the molecule of claim 1 .

8. The method of claim 7 , wherein the mammal is a mouse, non-human primate, or a human.

9. The engineered or non-naturally occurring molecule of claim 4 , wherein the HIV bnAb comprises (i) three complementarity determining regions (CDRs) of a heavy chain variable domain, a first CDR of which comprises an amino acid sequence comprising SEQ ID NO: 33 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 33, a second CDR of which comprises an amino acid sequence comprising SEQ ID NO: 34 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 34, and a third CDR of which comprises an amino acid sequence comprising SEQ ID NO: 35 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 35; and, (ii) three CDRs of a light chain variable domain, a first CDR of which comprises an amino acid sequence comprising SEQ ID NO: 42 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 42, a second CDR of which comprises an amino acid sequence comprising SEQ ID NO: 43 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 43, and a third of which comprises an amino acid sequence comprising SEQ ID NO: 44 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 44.

10. The molecule of claim 1 , wherein the HIV-1 bnAb comprises three complementarity determining regions (CDRs) of a heavy chain variable domain, a first CDR of which comprising the amino acid sequence of SEQ ID NO: 50 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 50, a second CDR of which comprising the amino acid sequence of SEQ ID NO: 51 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 51, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 52 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 52, and three CDRs of a light chain variable domain, a first CDR of which comprising the amino acid sequence of SEQ ID NO: 59 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 59, a second CDR of which comprising the amino acid sequence of SEQ ID NO: 60 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 60, and a third CDR of which comprising the amino acid sequence of SEQ ID NO: 61 or an amino acid sequence having at least 95% sequence identity to SEQ ID NO: 61.

11. The method of claim 7 , wherein the molecule is administered with an adjuvant.

12. The method of claim 11 ,

wherein the adjuvant comprises a lecithin or

wherein the adjuvant is an immune stimulating complex-forming adjuvant or a lipid-based vaccine adjuvant.

13. The method of claim 12 , wherein the lecithin is (a) combined with an acrylic polymer, (b) in a coated oil droplet in an oil-in-water emulsion or (c) in an acrylic polymer in an oil-in-water emulsion.

14. A method of eliciting an immune response in a mammal or stimulating an HIV-1 broadly neutralizing antibody (bnAb) comprising administering the molecule of claim 1 ,

wherein the molecule is administered in a liposome or in a nanoparticle or

wherein the molecule is fixed, wherein the molecule is fixed in glutaraldehyde, or

wherein the molecule is quenched with glycine.

15. A method of identifying an HIV-1 binder which comprises contacting a candidate binder with the molecule of claim 1 and identifying a candidate binder that binds to the molecule.

16. A method of identifying a broadly neutralizing antibody (bnAb) against HIV-1 which comprises contacting a candidate antibody with the molecule of claim 1 and identifying an antibody that binds to the molecule as a bnAb,

wherein the bnAb is a germline or germline reverted bnAb.

17. The vector of claim 6 , wherein the viral vector is selected from the group comprising adenoviruses, adeno-associated viruses (AAV), alphaviruses, herpesviruses, retroviruses, and poxviruses.

18. The vector of claim 17 , wherein the viral vector is AAV.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Apr 16, 2021
From: ANDRABI, RAIEES; BURTON, DENNIS
To: THE SCRIPPS RESEARCH INSTITUTE
Reel/Frame 055955/0424 →
Continuity (3)
Continuation In Part PCTUS2019056867 · Oct 18, 2019
Provisional Application 62747650 · Oct 18, 2018
Related Publication 20210324003A1 · Oct 21, 2021
References Cited (23)
US 10400015B2 · Kwong · 2019 [cited by examiner]
US 11555196B2 · Meyers · 2023 [cited by examiner]
US 20040191260A1 · Reiter et al. · 2004 [cited by applicant]
US 20210309753A1 · Munoz-Olaya · 2021 [cited by examiner]
US 20210363194A1 · Tokatlian · 2021 [cited by examiner]
US 20240261388A1 · Weiner · 2024 [cited by examiner]
Dondelinger, M., Filée, P., Sauvage, E., Quinting, B., Muyldermans, S., Galleni, M., and Vandevenne, M.S. (2018). Understanding the Significance and Implications of Antibody Numbering and Antigen-Binding Surface/Residue… [cited by examiner]
Bowie, J. U., Reidhaar-Olson, J. F., Lim, W. A., & Sauer, R. T. (1990). Deciphering the Message in Protein Sequences: Tolerance to Amino Acid Substitutions. Science (American Association for the Advancement of Science),… [cited by examiner]
Winkler, K., Kramer, A., Kuttner, G., Seifert, M., Scholz, C., Wessner, H., Schneider-Mergener, J., & Hohne, W. (2000). Changing the Antigen Binding Specificity by Single Point Mutations of an Anti-p24 (HIV-1) Antibody.… [cited by examiner]
Chen, Z., Wang, J., Bao, L., Guo, L., Zhang, W., Xue, Y., Zhou, H., Xiao, Y., Wang, J., Wu, F., Deng, Y., Qin, C., & Jin, Q. (2015). Human monoclonal antibodies targeting the haemagglutinin glycoprotein can neutralize H… [cited by examiner]
Sela-Culang, I., Kunik, V., & Ofran, Y. (2013). The Structural Basis of Antibody-Antigen Recognition. Frontiers in Immunology, 4, 302-302. (Year: 2013). [cited by examiner]
Tsuchiya, Y., & Mizuguchi, K. (2016). The diversity of H3 loops determines the antigen-binding tendencies of antibody CDR loops. Protein science : a publication of the Protein Society, 25(4), 815-825. (Year: 2016). [cited by examiner]
Collis, A. V., Brouwer, A. P., & Martin, A. C. (2003). Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen. Journal of mo… [cited by examiner]
Dondelinger, M., Filée, P., Sauvage, E., Quinting, B., Muyldermans, S., Galleni, M., & Vandevenne, M. S. (2018). Understanding the Significance and Implications of Antibody Numbering and Antigen-Binding Surface/Residue … [cited by examiner]
Griffith, S. A., & McCoy, L. E. (2021). To bnAb or Not to bnAb: Defining Broadly Neutralising Antibodies Against HIV-1. Frontiers in immunology, 12, 708227. (Year: 2021). [cited by examiner]
Andrabi, R. et al. (2019). The Chimpanzee SIV Envelope Trimer: Structure and Deployment as an HIV Vaccine Template. Cell Reports, 27(8), 2426-2441.e6. (Year: 2019). [cited by examiner]
R. Andrabi, et al. Identification of Common Features in Prototype Broadly Neutralizing Antibodies to HIV Envelope V2 Apex to Facilitate Vaccine Design. Immunity (Nov. 17, 2015) vol. 43, No. 5, pp. 959-973. [cited by applicant]
P. Wang, Anti-HIV Passive Immunization in Animal Models, J. Hiv Retrovirus (Feb. 26, 2018) vol. 4, No. 1:4. [cited by applicant]
International Search Report and Written Opinion dated Apr. 14, 2020 issued in Int'l Application PCT/US2019/056867. [cited by applicant]
Brandon F. Keele, et al., Chimpanzee Reservoirs of Pandemic and Nonpandemic HIV-1, Science, Jul. 28, 2006) vol. 313 pp. 523-526. [cited by applicant]
Jason S. McLellan, et al., Structure of HIV-1 gp120 VI/V2 domain with broadly neutralizing antibody PG9, Nature (Dec. 15, 2011) vol. 480, pp. 336-343. [cited by applicant]
EMBL Accession No. DQ373066—Simian immunodeficiency virus isolate SIVcpzMT145, complete genome (Jun. 3, 2006). [cited by applicant]
Supplementary EP Search Report issued Jun. 2, 2022 in counterpart EP Application No. 19872424.7. [cited by applicant]