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  • member
  • team
  • department
  • center
  • program_project
  • nrc
  • whocc
  • project
  • software
  • tool
  • patent
  • Administrative Staff
  • Assistant Professor
  • Associate Professor
  • Clinical Research Assistant
  • Clinical Research Nurse
  • Clinician Researcher
  • Department Manager
  • Dual-education Student
  • Full Professor
  • Honorary Professor
  • Lab assistant
  • Master Student
  • Non-permanent Researcher
  • Nursing Staff
  • Permanent Researcher
  • Pharmacist
  • PhD Student
  • Physician
  • Post-doc
  • Prize
  • Project Manager
  • Research Associate
  • Research Engineer
  • Retired scientist
  • Technician
  • Undergraduate Student
  • Veterinary
  • Visiting Scientist
  • Deputy Director of Center
  • Deputy Director of Department
  • Deputy Director of National Reference Center
  • Deputy Head of Facility
  • Director of Center
  • Director of Department
  • Director of Institute
  • Director of National Reference Center
  • Group Leader
  • Head of Facility
  • Head of Operations
  • Head of Structure
  • Honorary President of the Departement
  • Labex Coordinator
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Broadly neutralizing antibodies (bNAbs) develop in rare HIV-1 infected humans, and neutralize a large panel of viral quasi-species. Over the past decade, hundreds of bNAbs have been isolated, some of which can protect non-human primates from infection. Hence, bNAbs hold great promises for HIV-1 treatment and prevention by vaccination or passive immunoprophylaxis. Indeed, decrypting the B cell ontogeny of HIV-1 bNAbs is paramount for vaccine design. In this study, we describe the detailed characterization of IgA and IgG bNAbs from 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 Å-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. Thus, 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. Also, potent IgA bNAbs to the N332 supersite are elicited in response to HIV-1 infection, with an affinity maturation signature compatible with the one induced by vaccines, which could be essential for blocking HIV-1 mucosal transmission.

Source

Epitope convergence of broadly HIV-1 neutralizing IgA and IgG antibody lineages in a viremic controller, Journal of Experimental Medicine, March 1, 2022