2022
Epitope convergence of broadly HIV-1 neutralizing IgA and IgG antibody lineages in a viremic controller
LORIN, Valerie; Ignacio FERNANDEZ; Guillemette MASSE-RANSON; Melanie BOUVIN-PLEY; Luis M MOLINOS-ALBERT et. al.Základní údaje
Originální název
Epitope convergence of broadly HIV-1 neutralizing IgA and IgG antibody lineages in a viremic controller
Autoři
LORIN, Valerie; Ignacio FERNANDEZ; Guillemette MASSE-RANSON; Melanie BOUVIN-PLEY; Luis M MOLINOS-ALBERT; Cyril PLANCHAIS; Thierry HIEU; Gerard PEHAU-ARNAUDET; Dominik HREBÍK; Giulia GIRELLI-ZUBANI; Oriane FIQUET; Florence GUIVEL-BENHASSINE; Rogier W SANDERS; Bruce D WALKER; Olivier SCHWARTZ; Johannes F SCHEID; Jordan D DIMITROV; Pavel PLEVKA; Martine BRAIBANT; Michael S SEAMAN; Francois BONTEMS; James p DI SANTO; Felix A REY a Hugo MOUQUET
Vydání
JOURNAL OF EXPERIMENTAL MEDICINE, UNITED STATES, ROCKEFELLER UNIV PRESS, 2022, 0022-1007
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
30102 Immunology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 15.300
Kód RIV
RIV/00216224:14740/22:00127891
Organizační jednotka
Středoevropský technologický institut
UT WoS
000867703500001
EID Scopus
2-s2.0-85126474984
Klíčová slova anglicky
B-CELLSSTANDARDIZED ASSESSMENTSENVELOPE GLYCOPROTEINEFFICIENT GENERATIONMONOCLONAL-ANTIBODYCRYSTAL-STRUCTUREPOTENTGLYCANGP120MATURATION
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 11. 1. 2023 15:45, Mgr. Pavla Foltynová, Ph.D.
Anotace
V originále
Decrypting the B cell ontogeny of HIV-1 broadly neutralizing antibodies (bNAbs) is paramount for vaccine design. Here, we characterized IgA and IgG bNAbs of three distinct B cell lineages in a viremic controller, two of which comprised only IgG(+) or IgA(+) blood memory B cells; the third combined both IgG and IgA clonal variants. 7-269 bNAb in the IgA-only lineage displayed the highest neutralizing capacity despite limited somatic mutation, and delayed viral rebound in humanized mice. bNAbs in all three lineages targeted the N332 glycan supersite. The 2.8-angstrom resolution cryo-EM structure of 7-269-BG505 SOSIP.664 complex showed a similar pose as 2G12, on an epitope mainly composed of sugar residues comprising the N332 and N295 glycans. Binding and cryo-EM structural analyses showed that antibodies from the two other lineages interact mostly with glycans N332 and N386. Hence, multiple B cell lineages of IgG and IgA bNAbs focused on a unique HIV-1 site of vulnerability can codevelop in HIV-1 viremic controllers.