{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Chawla H"],"pubmed_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 <i>N</i>-linked glyc"],"journal":["RSC chemical biology"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12853648"],"repository":["biostudies-literature"],"pubmed_title":["Signatures of native-like glycosylation in RNA replicon-derived HIV-1 immunogens."],"pmcid":["PMC12853648"],"pubmed_authors":["Mckay PF","Irvine DJ","Ozorowski G","Chawla H","Silva M","Hayes GM","Butler J","Willcox JT","Lee WH","Ward AB","Shattock RJ","Crispin M"],"additional_accession":[]},"is_claimable":false,"name":"Signatures of native-like glycosylation in RNA replicon-derived HIV-1 immunogens.","description":"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 <i>N</i>-linked glyc","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-18T05:51:47.303Z","creation":"2026-06-18T03:07:12.735Z"},"accession":"S-EPMC12853648","cross_references":{"pubmed":["41623524"],"doi":["10.1039/d5cb00165j"]}}