The same major histocompatibility complex polymorphism involved in control of HIV influences peptide binding in the mouse H-2Ld system.

ABSTRACT: Single-site polymorphisms in human class I major histocompatibility complex (MHC) products (HLA-B) have recently been shown to correlate with HIV disease progression or control. An identical single-site polymorphism (at residue 97) in the mouse class I product H-2L(d) influences stability of the complex. To gain insight into the human polymorphisms, here we examined peptide binding, stability, and structures of the corresponding L(d) polymorphisms, Trp(97) and Arg(97). Expression of L(d)W97 and L(d)R97 genes in a cell line that is antigen-processing competent showed that L(d)R97 was expressed at higher levels than L(d)W97, consistent with enhanced stability of self-peptide·L(d)R97 complexes. To further examine peptide-binding capacities of these two allelic variants, we used a high affinit

SUBMITTER: Narayanan S 

PROVIDER: S-EPMC3814772 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature