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© Charles Dauguet
Virus VIH-2, second virus du sida isolé en 1985 par l'équipe du Pr. Montagnier de l'Institut Pasteur.
Publication : Cell reports

Affinity for the Interface Underpins Potency of Antibodies Operating In Membrane Environments.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cell reports - 18 Aug 2020

Rujas E, Insausti S, Leaman DP, Carravilla P, González-Resines S, Monceaux V, Sánchez-Eugenia R, García-Porras M, Iloro I, Zhang L, Elortza F, Julien JP, Saéz-Cirión A, Zwick MB, Eggeling C, Ojida A, Domene C, Caaveiro JMM, Nieva JL,

Link to Pubmed [PMID] – 32814041

Link to DOI [DOI] – S2211-1247(20)31022-610.1016/j.celrep.2020.108037

Cell Rep 2020 Aug; 32(7): 108037

The contribution of membrane interfacial interactions to recognition of membrane-embedded antigens by antibodies is currently unclear. This report demonstrates the optimization of this type of antibodies via chemical modification of regions near the membrane but not directly involved in the recognition of the epitope. Using the HIV-1 antibody 10E8 as a model, linear and polycyclic synthetic aromatic compounds are introduced at selected sites. Molecular dynamics simulations predict the favorable interactions of these synthetic compounds with the viral lipid membrane, where the epitope of the HIV-1 glycoprotein Env is located. Chemical modification of 10E8 with aromatic acetamides facilitates the productive and specific recognition of the native antigen, partially buried in the crowded environment of the viral membrane, resulting in a dramatic increase of its capacity to block viral infection. These observations support the harnessing of interfacial affinity through site-selective chemical modification to optimize the function of antibodies that target membrane-proximal epitopes.

https://pubmed.ncbi.nlm.nih.gov/32814041