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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-\u00c5 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.<\/jats:p>","DOI":"10.1084\/jem.20212045","type":"journal-article","created":{"date-parts":[[2022,3,1]],"date-time":"2022-03-01T14:52:39Z","timestamp":1646146359000},"update-policy":"https:\/\/doi.org\/10.1084\/jem.crossmarkpolicy","source":"Crossref","is-referenced-by-count":31,"title":["Epitope convergence of broadly HIV-1 neutralizing IgA and IgG antibody lineages in a viremic controller"],"prefix":"10.1084","volume":"219","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1760-1585","authenticated-orcid":true,"given":"Val\u00e9rie","family":"Lorin","sequence":"first","affiliation":[{"name":"Laboratory of Humoral Immunology, Department of Immunology, Institut Pasteur, Paris, France 1"},{"name":"Institut national de la sant\u00e9 et de la recherche m\u00e9dicale U1222, Paris, France 2"},{"name":"Universit\u00e9 de Paris, Sorbonne Paris 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