Signatures of native-like glycosylation in RNA replicon-derived HIV-1 immunogens.

ABSTRACT: RNA-based vaccines have emerged as a highly effective delivery platform. However, this approach eliminates the possibility for immunogen purification, common in manufacturing of recombinant immunogens. In HIV-1 vaccine design, this is of particular importance because non-native epitopes can compromise the desired immune response, and native immunogen assembly is important for presentation of glycan-based epitopes targeted by broadly neutralizing antibodies. Here, we investigate the assembly and glycosylation of the archetypal trimeric HIV-1 immunogen, BG505, in the soluble single-chain format (NFL.664) that bypasses the need of maturation by furin cleavage. We have investigated the presence of the trimer-associated mannose-patch as oligomannose-type structures at these N-linked glyc

SUBMITTER: Chawla H 

PROVIDER: S-EPMC12853648 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature