Year: 2010
Type: article
Abstract: Glycosylation of immune proteins plays critical roles in the adaptive immune system.Complex asparagine (N)-linked glycans are involved in directing the proper protein folding and trafficking to the cell surface, protection from the proteolytic cleavage, and promoting the appropriate cell-cell adhesion and communication.Our study shows that elimination of complex N-linked glycans on MHC II reduced the presentation of a novel zwitterionic polysaccharide antigen PSA which expressed by B. fragilis but not conventional peptides in live antigen presenting cells (APCs).The binding assay demonstrated that full size complex N-glycans are necessary for PSA but not conventional peptide antigen binding to MHC II.T cell activation assay conducted in mouse bone marrow-derived dendritic cells (BMDCs) shows the in vitro evidence that PSA-mediated T cell activation is significantly reduced due to the blockade of complex N-glycans of MHC II in APCs.However, lacking N-glycans on MHC II does not affect OT-II T cell activation with OVA peptide.These results reveal that N-glycosylation of MHC II directly influences PSA but not conventional protein antigen presentation and downstream T cell activation.
Author: Fan Zhao
Institution: Case Western Reserve University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W2225112558