Mapping of SARS-CoV-2 spike glycoprotein-derived antigens presented by HLA class II on dendritic cells: how glycosylation is different from the original

Mapping of SARS-CoV-2 spike glycoprotein-derived antigens presented by HLA class II on dendritic cells: how glycosylation is different from the original

A group from University of Oxford, UK, etc. has reported on mapping of SARS-CoV-2 spike glycoprotein-derived antigens presented by HLA class II on dendritic cells.
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8116342/

It is very curious for blog admin whether HLA-II bound glycopeptides presented as SARS-CoV-2-specific antigens on dendritic cells have the same glycosylation as phagocytized SARS-CoV-2 by dendritic cells.

HLA-II-bound glycopeptides were identified from 14 N-linked glycosylation sites in Spike from total 22 glycosylation sites. HLA-II-bound peptides carried predominantly short paucimannosidic-type N-glycans while original Spike carried oligomannosidic- and GlcNAc-capped complex-type N-glycan structures at these sites. The paucimannosylation of the HLA-II-bound peptides comprised both core-fucosylated and fucosylated species. This reveals there is substantial trimming of glycan residues on the glycopeptides during antigen processing in dendritic cells.


The heatmap colors in a figure above indicate the relative frequency of each glycan composition present, and the total number of peptide spectral matches (PSM) is also shown (blue bars).

Mx

Pioneer in Glycan Profiling Technology Environmentally Regenerative Agriculture

Comments are closed.

Powered by WordPress |Copyright © 2020 Emukk. All rights reserved