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

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  • dc.contributor.author Torralba, Johana
  • dc.contributor.author Arada, Igor de la
  • dc.contributor.author Partida-Hanon, Angélica
  • dc.contributor.author Rujas, Edurne
  • dc.contributor.author Arribas, Madalen
  • dc.contributor.author Insausti, Sara
  • dc.contributor.author Valotteau, Claire
  • dc.contributor.author Valle, Javier
  • dc.contributor.author Andreu Martínez, David
  • dc.contributor.author Caaveiro, José M. M.
  • dc.contributor.author Jiménez, María Ángeles
  • dc.contributor.author Apellániz, Beatriz
  • dc.contributor.author Redondo-Morata, Lorena
  • dc.contributor.author Nieva, José L.
  • dc.date.accessioned 2022-12-15T07:16:32Z
  • dc.date.available 2022-12-15T07:16:32Z
  • dc.date.issued 2022
  • dc.description.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.
  • dc.description.sponsorship This study was supported by MCIN/AEI/10.13039/501100011033 - “ERDF A way of making Europe” (Grant PID2021-126014OB-I00 to J.L.N. and B.A.), MCIN/AEI/10.13039/501100011033 (Grant PID2020-112821GB-I00 to M.A.J.), Basque Government (Grant: IT1449-22 to J.L.N. and B.A.) and Kiban-B grant 20H03228 from JSPS to J.M.M.C. L.R.-M. acknowledges funding from the Agence National de la Recherche (ANR), as part of the ‘Investments d′Avenir’ Program (I-SITE ULNE/ANR-16-IDEX-0004 ULNE). This project has received funding from the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie grant agreement No. 895819 (to C.V.). Work at Pompeu Fabra University was supported by the María de Maeztu network of Units of Excellence of the Spanish Ministry of Science and Innovation. Technical assistance from Miguel García-Porras is greatly acknowledged. The NMR experiments were performed in the “Manuel Rico” NMR laboratory, LMR, CSIC, a node of the Spanish Large-Scale National Facility ICTS R-LRB.
  • dc.format.mimetype application/pdf
  • dc.identifier.citation Torralba J, de la Arada I, Partida-Hanon A, Rujas E, Arribas M, Insausti S, Valotteau C, Valle J, Andreu D, Caaveiro JMM, Jiménez MA, Apellániz B, Redondo-Morata L, Nieva JL. Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope. Commun Biol. 2022 Nov 18;5(1):1265. DOI: 10.1038/s42003-022-04219-6
  • dc.identifier.doi http://dx.doi.org/10.1038/s42003-022-04219-6
  • dc.identifier.issn 2399-3642
  • dc.identifier.uri http://hdl.handle.net/10230/55144
  • dc.language.iso eng
  • dc.publisher Nature Research
  • dc.relation.ispartof Commun Biol. 2022 Nov 18;5(1):1265
  • dc.relation.projectID info:eu-repo/grantAgreement/EC/H2020/895819
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PE/PID2021-126014OB-I00
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/2PE/PID2020-112821GB-I00
  • dc.rights © The Author(s) 2022. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
  • dc.rights.accessRights info:eu-repo/semantics/openAccess
  • dc.rights.uri http://creativecommons.org/licenses/by/4.0/
  • dc.subject.keyword Immunology
  • dc.subject.keyword Membrane biophysics
  • dc.subject.keyword Nanoscale biophysics
  • dc.title Molecular recognition of a membrane-anchored HIV-1 pan-neutralizing epitope
  • dc.type info:eu-repo/semantics/article
  • dc.type.version info:eu-repo/semantics/publishedVersion

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