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TitleThe asymmetric opening of HIV-1 Env by a potent CD4 mimetic enables anti-coreceptor binding site antibodies to mediate ADCC.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateAug 27, 2024
AuthorsJonathan Richard / Michael W Grunst / Ling Niu / Marco A Díaz-Salinas / William D Tolbert / Lorie Marchitto / Fei Zhou / Catherine Bourassa / Derek Yang / Ta Jung Chiu / Hung-Ching Chen / Mehdi Benlarbi / / Suneetha Gottumukkala / Wenwei Li / Katrina Dionne / Étienne Bélanger / Debashree Chatterjee / Halima Medjahed / Wayne A Hendrickson / Joseph Sodroski / Zabrina C Lang / Abraham J Morton / Rick K Huang / Doreen Matthies / Amos B Smith / Walther Mothes / James B Munro / Marzena Pazgier / Andrés Finzi /
PubMed AbstractHIV-1 envelope glycoproteins (Env) from primary HIV-1 isolates typically adopt a pretriggered "closed" conformation that resists to CD4-induced (CD4i) non-neutralizing antibodies (nnAbs) mediating ...HIV-1 envelope glycoproteins (Env) from primary HIV-1 isolates typically adopt a pretriggered "closed" conformation that resists to CD4-induced (CD4i) non-neutralizing antibodies (nnAbs) mediating antibody-dependent cellular cytotoxicity (ADCC). CD4-mimetic compounds (CD4mcs) "open-up" Env allowing binding of CD4i nnAbs, thereby sensitizing HIV-1-infected cells to ADCC. Two families of CD4i nnAbs, the anti-cluster A and anti-coreceptor binding site (CoRBS) Abs, are required to mediate ADCC in combination with the indane CD4mc BNM-III-170. Recently, new indoline CD4mcs with improved potency and breadth have been described. Here, we show that the lead indoline CD4mc, CJF-III-288, sensitizes HIV-1-infected cells to ADCC mediated by anti-CoRBS Abs alone, contributing to improved ADCC activity. Structural and conformational analyses reveal that CJF-III-288, in combination with anti-CoRBS Abs, potently stabilizes an asymmetric "open" State-3 Env conformation, This Env conformation orients the anti-CoRBS Ab to improve ADCC activity and therapeutic potential.
External linksbioRxiv / PubMed:39253431 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution3.5 - 21.5 Å
Structure data

45530

9cf5

EMDB-45530, PDB-9cf5:
STRUCTURE OF CD4 MIMETIC CJF-III-288 IN COMPLEX WITH BG505 SOSIP.664 HIV-1ENV TRIMER AND 17B FAB
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-46646: HIV-1 BaL Env in complex with CD4 mimetic CJF-III-288 and 17b IgG
Method: EM (subtomogram averaging) / Resolution: 21.5 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-Y26:
propyl (2R,3S)-2-(carbamimidamidomethyl)-3-[2-(4-chloro-3-fluoroanilino)(oxo)acetamido]-6-[(methylamino)methyl]-2,3-dihydro-1H-indole-1-carboxylate

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 / FUSION / ENTRY / MEMBRANE / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX

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