Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
18 11 2022
18 11 2022
Historique:
received:
04
08
2022
accepted:
03
11
2022
pubmed:
19
11
2022
medline:
23
11
2022
entrez:
18
11
2022
Statut:
epublish
Résumé
Antibodies against the carboxy-terminal section of the membrane-proximal external region (C-MPER) of the HIV-1 envelope glycoprotein (Env) are considered as nearly pan-neutralizing. Development of vaccines capable of producing analogous broadly neutralizing antibodies requires deep understanding of the mechanism that underlies C-MPER recognition in membranes. Here, we use the archetypic 10E8 antibody and a variety of biophysical techniques including single-molecule approaches to study the molecular recognition of C-MPER in membrane mimetics. In contrast to the assumption that an interfacial MPER helix embodies the entire C-MPER epitope recognized by 10E8, our data indicate that transmembrane domain (TMD) residues contribute to binding affinity and specificity. Moreover, anchoring to membrane the helical C-MPER epitope through the TMD augments antibody binding affinity and relieves the effects exerted by the interfacial MPER helix on the mechanical stability of the lipid bilayer. These observations support that addition of TMD residues may result in more efficient and stable anti-MPER vaccines.
Identifiants
pubmed: 36400835
doi: 10.1038/s42003-022-04219-6
pii: 10.1038/s42003-022-04219-6
pmc: PMC9674588
doi:
Substances chimiques
HIV Envelope Protein gp41
0
HIV Antibodies
0
Epitopes
0
Lipid Bilayers
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1265Informations de copyright
© 2022. The Author(s).
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