Antigen-specific antibody Fc glycosylation enhances humoral immunity via the recruitment of complement.

ABSTRACT: HIV-specific broadly neutralizing antibodies (bNAbs) confer protection after passive immunization, but the immunological mechanisms that drive their development are poorly understood. Structural features of bNAbs indicate that they originate from extensive germinal center (GC) selection, which relies on persistent GC activity. However, why a fraction of infected individuals are able to successfully drive more effective affinity maturation is unclear. Delivery of antigens in the form of antibody-immune complexes (ICs), which bind to complement receptors (CRs) or Fc receptors (FcRs) on follicular dendritic cells, represents an effective mechanism for antigen delivery to the GC. We sought to define whether IC-FcR or CR interactions differ among individuals who develop bNAb responses to HIV. E

SUBMITTER: Lofano G 

PROVIDER: S-EPMC6298214 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature