Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope - Archive ouverte HAL
Article Dans Une Revue Communications Biology Année : 2022

Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope

Claire Valotteau
José Caaveiro

Résumé

Abstract 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.

Dates et versions

hal-04100970 , version 1 (18-05-2023)

Identifiants

Citer

Johana Torralba, Igor de la Arada, Angélica Partida-Hanon, Edurne Rujas, Madalen Arribas, et al.. Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope. Communications Biology, 2022, 5 (1), pp.1265. ⟨10.1038/s42003-022-04219-6⟩. ⟨hal-04100970⟩
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