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TitleRapidly acquired HIV-1 neutralization breadth in a rhesus V2 apex knockin mouse model after a single bolus immunization.
Journal, issue, pagesSci Immunol, Vol. 11, Issue 116, Page eadz5064, Year 2026
Publish dateFeb 13, 2026
AuthorsAmrit Raj Ghosh / Rumi Habib / Nitesh Mishra / Ryan S Roark / Madhav Akauliya / Ali A Albowaidey / Joel D Allen / Khaled Amereh / Gabriel Avillion / Maria Bottermann / Bo Liang / Namit Chaudhary / Sean Callaghan / Jonathan Dye / Xuduo Li / Jordan R Ellis-Pugh / Rohan Roy Chowdhury / Nicole E James / Xiaotie Liu / Laura Maiorino / Paula M Villavicencio / Rebecca Nedellec / Prabhgun Oberoi / Kirsten J Sowers / Younghoon Park / Thavaleak Prum / Linette Rodriguez / Maria Ssozi / Jonathan L Torres / Agnes A Walsh / John E Warner / Stephanie R Weldon / Liling Xu / Kevin Wiehe / Max Crispin / Andrew B Ward / Usha Nair / Beatrice H Hahn / Dennis R Burton / Lawrence Shapiro / Peter D Kwong / Darrell J Irvine / Raiees Andrabi / George M Shaw / Facundo D Batista /
PubMed AbstractCurrent immunization strategies to elicit broadly neutralizing antibodies (bnAbs) against HIV-1 generally propose complex, multiboost regimens. In rhesus macaques, simian-human immunodeficiency virus ...Current immunization strategies to elicit broadly neutralizing antibodies (bnAbs) against HIV-1 generally propose complex, multiboost regimens. In rhesus macaques, simian-human immunodeficiency virus (SHIV) infection rapidly drives the development of some bnAb classes sharing structural similarities with those in humans. Here, we generated a knockin (KI) mouse model with B cells bearing the unmutated common ancestor of a V2 apex-targeted bnAb lineage, V033-a. A single immunization with a germline-targeting native-like trimer, Q23-APEX-GT1, recapitulated the ontogeny of the mature rhesus bnAb in KI mice, including rare, disfavored somatic mutations. Resulting antibodies exhibited potent neutralization against a broad panel of heterologous HIV-1 strains. Boosting with Env escape mutant trimers further improved breadth and potency, and cryo-electron microscopy analysis revealed the structural basis for heterologous neutralization breadth. Nonhuman primate and mouse models combined with structure can serve as a platform for identifying and validating immunogens that streamline HIV vaccination regimens.
External linksSci Immunol / PubMed:41686913
MethodsEM (single particle)
Resolution3.1 - 3.8 Å
Structure data

70663

9oog

EMDB-70663, PDB-9oog:
Cryo-EM structure of vaccine-elicited antibody T3_NB_G05 in complex with HIV Env trimer Q23-APEX-GT1.N187S
Method: EM (single particle) / Resolution: 3.1 Å

70664

9ook

EMDB-70664, PDB-9ook:
Cryo-EM structure of vaccine-elicited antibody T3_QB_G12 in complex with HIV Env trimer Q23-APEX-GT1
Method: EM (single particle) / Resolution: 3.8 Å

70666

9oom

EMDB-70666, PDB-9oom:
Cryo-EM structure of vaccine-elicited antibody T6_P_H03 in complex with HIV Env trimer Q23-APEX-GT1
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

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

Source
  • Macaca mulatta (Rhesus monkey)
  • mus musculus (house mouse)
  • homo sapiens (human)
  • Human immunodeficiency virus 1
  • human immunodeficiency virus type 1
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / immune complex / neutralizing antibody / V2 apex / mouse model / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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