Abstract
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.
MeSH terms
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ATP Binding Cassette Transporter, Subfamily B, Member 2
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ATP Binding Cassette Transporter, Subfamily B, Member 3
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ATP-Binding Cassette Transporters / metabolism
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Amino Acid Sequence
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Animals
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Antigen Presentation
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Antigens, Viral / chemistry*
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Antigens, Viral / immunology
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Antigens, Viral / metabolism
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Arginine
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Cattle / immunology*
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Chromatography, High Pressure Liquid
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Consensus Sequence
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Fibroblasts / immunology
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Fibroblasts / virology
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Histocompatibility Antigens Class I / chemistry*
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Histocompatibility Antigens Class I / immunology
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Histocompatibility Antigens Class I / isolation & purification
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Hybridomas / immunology
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Leukocytes / immunology
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Leukocytes / virology
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Mice
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Molecular Sequence Data
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Parainfluenza Virus 3, Human / immunology*
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Peptide Fragments / chemistry*
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Peptide Fragments / immunology
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Protein Binding
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Sequence Alignment
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Species Specificity
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Viral Proteins / chemistry*
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Viral Proteins / immunology
Substances
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ATP Binding Cassette Transporter, Subfamily B, Member 2
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ATP Binding Cassette Transporter, Subfamily B, Member 3
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ATP-Binding Cassette Transporters
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Antigens, Viral
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Histocompatibility Antigens Class I
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Peptide Fragments
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TAP1 protein, human
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Tap1 protein, mouse
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Tap2 protein, mouse
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Viral Proteins
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TAP2 protein, human
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Arginine