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TitleAcquisition of quaternary trimer interaction as a key step in the lineage maturation of a broad and potent HIV-1 neutralizing antibody.
Journal, issue, pagesStructure, Vol. 33, Issue 8, Page 1325-11336.e5, Year 2025
Publish dateAug 7, 2025
AuthorsQingbo Liu / Ruth J Parsons / Kevin Wiehe / Robert J Edwards / Kevin O Saunders / Peng Zhang / Huiyi Miao / Kedamawit Tilahun / Julia Jones / Yue Chen / Bhavna Hora / Wilton B Williams / David Easterhoff / Xiao Huang / Katarzyna Janowska / Katayoun Mansouri / Barton F Haynes / Priyamvada Acharya / Paolo Lusso /
PubMed AbstractAlthough most broadly neutralizing antibodies (bNAbs) specific for the CD4-binding site (CD4-BS) of HIV-1 interact with a single gp120 protomer, a few mimic the quaternary binding mode of CD4, making ...Although most broadly neutralizing antibodies (bNAbs) specific for the CD4-binding site (CD4-BS) of HIV-1 interact with a single gp120 protomer, a few mimic the quaternary binding mode of CD4, making contact with a second protomer through elongated heavy chain framework 3 (FRH3) or complementarity-determining region 1 (CDRH1) loops. Here, we show that a CDRH3-dominated anti-CD4-BS bNAb, CH103, establishes quaternary interaction despite regular-length FRH3 and CDRH1. This quaternary interaction is critical for neutralization and is primarily mediated by two FRH3 acidic residues that were sequentially acquired and subjected to strong positive selection during CH103 maturation. Cryoelectron microscopy (cryo-EM) structures confirmed the role of the two FRH3 acidic residues in mediating quaternary contact and demonstrated that CH103 reaches the adjacent gp120 protomer by virtue of its unique angle of approach. Thus, the acquisition of quaternary interaction may constitute a key step in the lineage maturation of a broad and potent HIV-1 neutralizing antibody.
External linksStructure / PubMed:40412376 / PubMed Central
MethodsEM (single particle)
Resolution3.37 - 13.0 Å
Structure data

EMDB-44736: HIV Envelope trimer BG505 SOSIP.664 in complex with wild type CH103 antibody
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-44738: HIV Envelope BG505 SOSIP.664 in complex with one Fab of CH103 E75K/D76N mutant
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-44739: HIV Envelope trimer CH505 SOSIP.664 in complex with wild type CH103 antibody
Method: EM (single particle) / Resolution: 12.0 Å

EMDB-44740: HIV Envelope trimer CH505 SOSIP.664 in complex with three CH103 E75K/D76N mutant antibody Fabs
Method: EM (single particle) / Resolution: 10.0 Å

46604

9d7g

EMDB-46604, PDB-9d7g:
BG505 DS-SOSIP.664 apo structure from the CH103 KN cryo-EM dataset
Method: EM (single particle) / Resolution: 3.58 Å

46605

9d7h

EMDB-46605, PDB-9d7h:
Cryo-EM structure of BG505 DS-SOSIP.664 with 1 CH103 KN Fab bound
Method: EM (single particle) / Resolution: 3.59 Å

46606

9d7i

EMDB-46606, PDB-9d7i:
Cryo-EM structure of BG505 DS-SOSIP.664 with 2 CH103 KN Fabs bound
Method: EM (single particle) / Resolution: 3.68 Å

46613

9d7o

EMDB-46613, PDB-9d7o:
Cryo-EM structure of BG505 DS-SOSIP.664 with 1 CH103 Fab bound
Method: EM (single particle) / Resolution: 3.56 Å

46614

9d7p

EMDB-46614, PDB-9d7p:
Cryo-EM structure of BG505 DS-SOSIP.664 with 2 CH103 Fabs bound
Method: EM (single particle) / Resolution: 3.37 Å

Chemicals

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

Source
  • Human immunodeficiency virus 2
  • homo sapiens (human)
  • human immunodeficiency virus 1
KeywordsVIRAL PROTEIN / Trimer / Env / BG505 / CH103 / VIRAL PROTEIN/IMMUNE SYSTEM / VIRAL PROTEIN-IMMUNE SYSTEM complex

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