title: Association of Ld-restricted peptides with the wild-derived mouse Lw16 MHC class I molecule.
abstract: Previous serological analysis of untreated splenocytes and L cell transfectants expressing the wild-derived mouse major histocompatibility complex (MHC) class I molecule, Lw16, demonstrated the presence of two forms of this molecule in the cell lysates, one reactive with both the alpha 2 domain-reactive monoclonal antibody (mAb) 30-5-7 and the alpha 3 domain-reactive mAb 28-14-8 (30-5-7+ 28-14-8+), and the other reactive with only the latter of the two (30-5-7- 28-14-8+). Furthermore, the analysis suggested the presence of both forms on the cell surface. Due to the similarity of Lw16 to the inbred mouse-derived Ld molecule, we tested a panel of Ld-restricted and control peptides for their ability to bind to Lw16 molecules. Here, we report that two Ld-restricted viral peptides, lymphocytic choriomeningitis virus nucleoprotein (LCMV NP) 118-126 and murine cytomegalovirus (MCMV) pp89 168-176, significantly increase the number of Lw16 molecules on the cell surface as measured by the mAb 28-14-8, and the proportion of those molecules that are recognized by the mAb 30-5-7. This was further supported by an increase in mAb 30-5-7-reactive molecules in L.Lw16 cell lysates following treatment with either of these peptides. Examination of the stability of the different forms on the cell surface suggested that the 30-5-7+ Lw16 molecules induced with these peptides were unstable and probably lost their Ld-restricted peptides to generate 30-5-7- 28-14-8+ molecules; these latter molecules were also unstable. In contrast, putative 30-5-7+ and 30-5-7- 28-14-8+ Lw16 molecules on untreated cells were stable. Together, these results suggest that two Ld-restricted, viral peptides can induce assembly of or stabilize 30-5-7+ 28-14-8+ Lw16 molecules, mimicking endogenous self peptides. However, the association of the Ld-restricted peptides with Lw16 is apparently not optimal, since it results in unstable Lw16 molecules.
authors.affiliation: Department of Molecular Microbiology and Immunology, University of Missouri, Columbia 65212.
authors.forename: B L
authors.initials: BL
authors.lastname: Talken
authors.forename: L G
authors.initials: LG
authors.lastname: Harrison
authors.forename: D R
authors.initials: DR
authors.lastname: Lee
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D001769:Blood; D020126:Brefeldin A; D002462:Cell Membrane / Q000187:drug effects / Q000276:immunology; D003517:Cyclopentanes / Q000494:pharmacology; D003587:Cytomegalovirus / Q000276:immunology; D006649:Histocompatibility Antigens / Q000276:immunology*; D015395:Histocompatibility Antigens Class I / Q000276:immunology*; D017874:Immediate-Early Proteins / Q000276:immunology; D007739:L Cells; D008217:Lymphocytic choriomeningitis virus / Q000276:immunology; D051379:Mice; D008969:Molecular Sequence Data; D009698:Nucleoproteins / Q000276:immunology; D010455:Peptides / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology*
chemical_list: D000911:Antibodies, Monoclonal; D003517:Cyclopentanes; D006649:Histocompatibility Antigens; D015395:Histocompatibility Antigens Class I; D017874:Immediate-Early Proteins; D009698:Nucleoproteins; D010455:Peptides; D014764:Viral Proteins; C052612:cytomegalovirus immediate early phosphoprotein pp89; D020126:Brefeldin A