Peptide motif of a cattle MHC class I molecule
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A I Bamford1, A Douglas, T Friede
1DKFZ, Department of Tumour Virus Immunology, Heidelberg I, Germany.
A consensus motif for a bovine major histocompatibility complex (MHC) class I molecule, A20, was derived from parainfluenza type-3 (PI-3) virus-infected muscle-derived fibroblast cells and peripheral blood leukocytes by extraction of the naturally processed peptides from MHC class I molecules by treatment with TFA and peptide sequencing of the complex mixture. The results showed that the majority of peptides were 9 amino acids long with position 2 occupied by lysine and position 9 occupied by arginine. The arginine at position 9 suggests that cattle, like humans, but unlike the mouse have permissive TAP transporter molecules accepting peptides with positively charged amino acids at their C-terminus. This is the first report of a MHC ligand motif in cattle.
A consensus motif for a bovine major histocompatibility complex (MHC) class I molecule, A20, was derived from parainfluenza type-3 (PI-3) virus-infected muscle-derived fibroblast cells and peripheral blood leukocytes by extraction of the naturally processed peptides from MHC class I molecules by treatment with TFA and peptide sequencing of the complex mixture. The results showed that the majority of peptides were 9 amino acids long with position 2 occupied by lysine and position 9 occupied by arginine. The arginine at position 9 suggests that cattle, like humans, but unlike the mouse have permissive TAP transporter molecules accepting peptides with positively charged amino acids at their C-terminus. This is the first report of a MHC ligand motif in cattle.