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© Research
Publication : Cell reports

Conformational Plasticity in Broadly Neutralizing HIV-1 Antibodies Triggers Polyreactivity

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cell reports - 29 May 2018

Prigent J, Jarossay A, Planchais C, Eden C, Dufloo J, Kök A, Lorin V, Vratskikh O, Couderc T, Bruel T, Schwartz O, Seaman MS, Ohlenschläger O, Dimitrov JD, Mouquet H

Link to Pubmed [PMID] – 29847789

Cell Rep 2018 May;23(9):2568-2581

Human high-affinity antibodies to pathogens often recognize unrelated ligands. The molecular origin and the role of this polyreactivity are largely unknown. Here, we report that HIV-1 broadly neutralizing antibodies (bNAbs) are frequently polyreactive, cross-reacting with non-HIV-1 molecules, including self-antigens. Mutating bNAb genes to increase HIV-1 binding and neutralization also results in de novo polyreactivity. Unliganded paratopes of polyreactive bNAbs with improved HIV-1 neutralization exhibit a conformational flexibility, which contributes to enhanced affinity of bNAbs to various HIV-1 envelope glycoproteins and non-HIV antigens. Binding adaptation of polyreactive bNAbs to the divergent ligands mainly involves hydrophophic interactions. Plasticity of bNAbs’ paratopes may, therefore, facilitate accommodating divergent viral variants, but it simultaneously triggers promiscuous binding to non-HIV-1 antigens. Thus, a certain level of polyreactivity can be a mark of adaptable antibodies displaying optimal pathogens’ recognition.

https://www.ncbi.nlm.nih.gov/pubmed/29847789