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TitleConformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7334, Year 2024
Publish dateAug 26, 2024
AuthorsDurgadevi Parthasarathy / Karunakar Reddy Pothula / Sneha Ratnapriya / Héctor Cervera Benet / Ruth Parsons / Xiao Huang / Salam Sammour / Katarzyna Janowska / Miranda Harris / Joseph Sodroski / Priyamvada Acharya / Alon Herschhorn /
PubMed AbstractHIV-1 envelope glycoproteins (Envs) of most primary HIV-1 strains exist in closed conformation and infrequently sample open states, limiting access to internal epitopes. Thus, immunogen design aims ...HIV-1 envelope glycoproteins (Envs) of most primary HIV-1 strains exist in closed conformation and infrequently sample open states, limiting access to internal epitopes. Thus, immunogen design aims to mimic the closed Env conformation as preferred target for eliciting broadly neutralizing antibodies (bnAbs). Here we identify incompletely closed Env conformations of 6 out of 13 transmitted/founder (T/F) strains that are sensitive to antibodies that recognize internal epitopes typically exposed on open Envs. A 3.6 Å cryo-electron microscopy structure of unliganded, incompletely closed T/F Envs (1059-SOSIP) reveals protomer motion that increased sampling of states with incompletely closed trimer apex. We reconstruct de novo the post-transmission evolutionary pathway of a second T/F. Evolved viruses exhibit increased Env resistance to cold, soluble CD4 and 19b, all of which correlate with closing of the adapted Env trimer. Lastly, we show that the ultra-broad N6 bnAb efficiently recognizes different Env conformations and exhibits improved antiviral breadth against VRC01-resistant Envs isolated during the first-in-humans antibody-mediated-prevention trial.
External linksNat Commun / PubMed:39187497 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 3.8 Å
Structure data

41244

8tgu

EMDB-41244, PDB-8tgu:
Cryo-EM structure of BG505 SOSIP trimer purified via Galanthus nivalis lectin chromatography
Method: EM (single particle) / Resolution: 3.8 Å

41246

8tgw

EMDB-41246, PDB-8tgw:
Cryo-EM structure of 1059 SOSIP trimer purified via Galanthus nivalis lectin chromatography
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

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

Source
  • human immunodeficiency virus 1
KeywordsVIRAL PROTEIN / HIV-1 / Glycoprotein / Lectin / Trimer

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