The glycosylation status of MHC class I molecules impacts their interactions with TAPBPR.
Mol Immunol
; 139: 168-176, 2021 11.
Article
em En
| MEDLINE
| ID: mdl-34543843
ABSTRACT
Glycosylation plays a crucial role in the folding, structure, quality control and trafficking of glycoproteins. Here, we explored whether the glycosylation status of MHC class I (MHC-I) molecules impacts their affinity for the peptide editor, TAPBPR. We demonstrate that the interaction between TAPBPR and MHC-I is stronger when MHC-I lacks a glycan. Subsequently, TAPBPR can dissociate peptides, even those of high affinity, more easily from non-glycosylated MHC-I compared to their glycosylated counterparts. In addition, TAPBPR is more resistant to peptide-mediated allosteric release from non-glycosylated MHC-I compared to species with a glycan attached. Consequently, we find the glycosylation status of HLA-A*6802, -A*0201 and -B*2705 influences their ability to undergo TAPBPR-mediated peptide exchange. The discovery that the glycan attached to MHC-I significantly influences the affinity of their interactions with TAPBPR has important implications, on both an experimental level and in a biological context.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Imunoglobulinas
/
Antígenos de Histocompatibilidade Classe I
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Revista:
Mol Immunol
Ano de publicação:
2021
Tipo de documento:
Article