Disassembly of HIV envelope glycoprotein trimer immunogens is driven by antibodies elicited via immunization.

ABSTRACT: Rationally designed protein subunit vaccines are being developed for a variety of viruses including influenza, RSV, SARS-CoV-2, and HIV. These vaccines are based on stabilized versions of the primary targets of neutralizing antibodies on the viral surface, namely, viral fusion glycoproteins. While these immunogens display the epitopes of potent neutralizing antibodies, they also present epitopes recognized by non-neutralizing or weakly neutralizing ("off-target") antibodies. Using our recently developed electron microscopy polyclonal epitope mapping approach, we have uncovered a phenomenon wherein off-target antibodies elicited by HIV trimer subunit vaccines cause the otherwise highly stabilized trimeric proteins to degrade into cognate protomers. Further, we show that these protomers expo

SUBMITTER: Turner HL 

PROVIDER: S-EPMC8318364 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature