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TitleVaccination of nonhuman primates elicits a broadly neutralizing antibody lineage targeting a quaternary epitope on the HIV-1 Env trimer.
Journal, issue, pagesImmunity, Year 2025
Publish dateMay 5, 2025
AuthorsFabian-Alexander Schleich / Shridhar Bale / Javier Guenaga / Gabriel Ozorowski / Monika Àdori / Xiaohe Lin / Xaquin Castro Dopico / Richard Wilson / Mark Chernyshev / Alma Teresia Cotgreave / Marco Mandolesi / Jocelyn Cluff / Esmeralda D Doyle / Leigh M Sewall / Wen-Hsin Lee / Shiyu Zhang / Sijy O'Dell / Brandon S Healy / Deuk Lim / Vanessa R Lewis / Elana Ben-Akiva / Darrell J Irvine / Nicole A Doria-Rose / Martin Corcoran / Diane Carnathan / Guido Silvestri / Ian A Wilson / Andrew B Ward / Gunilla B Karlsson Hedestam / Richard T Wyatt /
PubMed AbstractThe elicitation of cross-neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) by vaccination remains a major challenge. Here, we immunized previously Env-immunized nonhuman primates with ...The elicitation of cross-neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) by vaccination remains a major challenge. Here, we immunized previously Env-immunized nonhuman primates with a series of near-native trimers that possessed N-glycan deletions proximal to the conserved CD4 binding site (CD4bs) to focus B cells to this region. Following heterologous boosting with fully glycosylated trimers, we detected tier 2 cross-neutralizing activity in the serum of several animals. Isolation of 185 matched heavy- and light-chain sequences from Env-binding memory B cells from an early responder identified a broadly neutralizing antibody lineage, LJF-0034, which neutralized nearly 70% of an 84-member HIV-1 global panel. High-resolution cryoelectron microscopy (cryo-EM) structures revealed a bifurcated binding mode that bridged the CD4bs to V3 across the gp120:120 interface on two adjacent protomers, evading the proximal N276 glycan impediment to the CD4bs, allowing neutralization breadth. This quaternary epitope defines a potential target for future HIV-1 vaccine development.
External linksImmunity / PubMed:40339576
MethodsEM (single particle)
Resolution3.3 - 8.2 Å
Structure data

45928

9cu5

EMDB-45928, PDB-9cu5:
LJF-085 Fab in complex with HIV Env JRFL NFL TD CC3+ trimer and 35O22 Fab
Method: EM (single particle) / Resolution: 3.4 Å

45929

9cu6

EMDB-45929, PDB-9cu6:
LJF-034 Fab in complex with HIV Env JRFL NFL TD CC3+ trimer and 35O22 Fab
Method: EM (single particle) / Resolution: 3.3 Å

45957

9cv7

EMDB-45957, PDB-9cv7:
LJF-085 Fab in complex with HIV Env ZM233 NFL TD CC3+ trimer
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-45978: LJF-085 Fab in complex with HIV Env ZM233 NFL TD CC3+ dimer and 35O22 Fab
Method: EM (single particle) / Resolution: 8.2 Å

Chemicals

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

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
  • macaca mulatta (Rhesus monkey)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / NHP / rhesus macaque / gp120 interface / HIV / NFL / neutralizing antibody / VIRAL PROTEIN-IMMUNE SYSTEM complex

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