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The Rat cim Effect: TAP Allele-Dependent Changes in a Class I MHC Anchor Motif and Evidence Against C-Terminal Trimming of Peptides in the ER

1996; Cell Press; Volume: 4; Issue: 2 Linguagem: Inglês

10.1016/s1074-7613(00)80680-9

1097-4180

Simon J. Powis, Lesley Young, Etienne Joly, Patrick J. Barker, Louise Richardson, Remco P Brandt, Cornelis J.M. Melief, Jonathan C. Howard, Geoffrey W Butcher,

Monoclonal and Polyclonal Antibodies Research

Functional polymorphism in the rat peptide transporter associated with antigen processing (TAP) changes the peptide pool available for binding and presentation by a class I MHC allele, RT1.Aa. The peptide binding motif for RT1.Aa, determined by stabilization with synthetic peptides, included a strong preference for arginine at the peptide C terminus. Analysis of natural peptides bound to RT1.Aa by both pool sequencing and anhydrotrypsin chromatography revealed that TAP polymorphism determined the presence or absence of arginine as the peptide C-terminal residue. This result highlights the in vivo impact of TAP–peptide selectivity, and provides evidence against a high rate of generation of new C termini by protease activity in the endoplasmic reticulum.