Molecular cloning and characterization of the pig MHC class Ⅰ-related MR1 gene
Major histocompatibility complex (MHC) class Ⅰ-related protein 1 (MR1), the most highly conserved MHC class Ⅰ molecule among mammals, is the restricting molecule for mucosal-associated invariant T (MAIT) cells. MAIT cells, a novel subset of T cells, play important roles in modulating the immune resp...
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Veröffentlicht in: | Developmental and comparative immunology 2019-07, Vol.96, p.58-67 |
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Sprache: | eng |
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Zusammenfassung: | Major histocompatibility complex (MHC) class Ⅰ-related protein 1 (MR1), the most highly conserved MHC class Ⅰ molecule among mammals, is the restricting molecule for mucosal-associated invariant T (MAIT) cells. MAIT cells, a novel subset of T cells, play important roles in modulating the immune responses to infectious and non-infectious diseases, and recognize antigens in the context of MR1. MR1 has been identified in many species, including human, mouse, sheep, and cow. Here, we cloned and characterized pig (Sus scrofa) MR1 (pMR1) transcripts, including five unique splice variants, from pig peripheral blood mononuclear cell cDNA. We also examined the tissue distribution of pMR1 and confirmed reactivity of pMR1 using a MR1 specific monoclonal antibody 26.5, demonstrating that the pMR1 gene was expressed in all tested tissues. Finally, we predicted the pMR1 3D structure and analyzed the docking mode of the MR1-5-OP-RU complex, finding that the docking mode of pMR1 with 5-OP-RU is similar to human MR1 docking. Collectively, this description of pMR1 adds to our understanding of the evolution of MHC molecules, and provides a theoretical basis for the subsequent study of pig MAIT cells.
•Six MR1 transcripts were cloned from tested pigs.•Pig MR1 mRNA was expressed in different tissues.•MR1 expression was detected in porcine cell lines and primary cells using a MR1 specific monoclonal antibody 26.5.•Pig MR1 shows a high degree sequence identity and structure similarity with human MR1.•Pig MR1 adopts a docking structure similar to human MR1 when binding the 5-OP-RU ligand. |
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ISSN: | 0145-305X 1879-0089 |
DOI: | 10.1016/j.dci.2019.02.020 |