Year: 2026
Type: article
Abstract: -linked glycosylation sites are indicative of native-like glycoprotein structure. Despite the presence of features of native-like glycosylation, both electron microscopy and glycopeptide analysis indicated the presence of a sub-population of non-native material. We also investigated the glycosylation of material derived from cell-types that likely produce immunogens near the site of intramuscular RNA injection. We show that replicon-transformed dendritic and muscle cell lines generate immunogens displaying similar oligomannose-type glycan content, whereas sites presenting complex-type glycosylation differed substantially in the levels of glycan processing. Overall, the control of the immunogen assembly by protein engineering is sufficient to drive native-like glycosylation at the majority of glycosylation sites independent of producer cells. Furthermore, we explored the engineering of RNA immunogens to improve glycan site occupancy. Controlling immunogen assembly at the nucleotide level offers a route to enhanced RNA-based immunogens.
Source: RSC Chemical Biology
DOI: 10.1039/d5cb00165j
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,962
Awards: International AIDS Vaccine Initiative - to advance the CAVD-supported projects through the translational stage and into clinical evaluation, ultimately resulting in successful new HIV/AID..., G1585882487, G1597505487, The University of Southampton - To provide a facility to characterize critical sugar components on HIV vaccine candidates for the Collaboration for AIDS Vaccine Discovery (CAVD), International AIDS Vaccine Initiative - to develop and test vaccination strategies that are practical, deployable and have the potential to reduce HIV incidence, G4103933137, G5287318678, G753129689, G7876585708, G8889668879, G9000291502
OpenAlex ID: W7122508235