ASSOCIATION OF L(D)-RESTRICTED PEPTIDES WITH THE WILD-DERIVED MOUSE L(W16) MHC CLASS-I MOLECULE

Citation
Bl. Talken et al., ASSOCIATION OF L(D)-RESTRICTED PEPTIDES WITH THE WILD-DERIVED MOUSE L(W16) MHC CLASS-I MOLECULE, Molecular immunology, 31(12), 1994, pp. 943-954
Citations number
50
Categorie Soggetti
Immunology,Biology
Journal title
ISSN journal
01615890
Volume
31
Issue
12
Year of publication
1994
Pages
943 - 954
Database
ISI
SICI code
0161-5890(1994)31:12<943:AOLPWT>2.0.ZU;2-2
Abstract
Previous serological analysis of untreated splenocytes and L cell tran sfectants expressing the wild-derived mouse major histocompatibility c omplex (MHC) class I molecule, L(w16), demonstrated the presence of tw o forms of this molecule in the cell lysates, one reactive with both t he alpha 2 domain-reactive monoclonal antibody (mAb) 30-5-7 and the al pha 3 domain-reactive mAb 28-14-8 (30-5-7(+) 28-14-8(+)), and the othe r reactive with only the latter of the two (30-5-7(-) 28-14-8(+)). Fur thermore, the analysis suggested the presence of both forms on the cel l surface. Due to the similarity of L(w16) to the inbred mouse-derived L(d) molecule, we tested a panel of L(d)-restricted and control pepti des for their ability to bind to L(w16) molecules. Here, we report tha t two L(d)-restricted viral peptides, lymphocytic choriomeningitis vir us nucleoprotein (LCMV NP) 118-126 and murine cytomegalovirus (MCMV) p p89 168-176, significantly increase the number of L(w16) 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 furth er supported by an increase in mAb 30-5-7-reactive molecules in L.L(w1 6) cell lysates following treatment with either of these peptides. Exa mination of the stability of the different forms on the cell surface s uggested that the 30-5-7(+) L(w16) molecules induced with these peptid es were unstable and probably lost their L(d)-restricted peptides to g enerate 30-5-7(-) 28-14-8(+) molecules; these latter molecules were al so unstable. In contrast, putative 30-5-7(+) and 30-5-7(-) 28-14-8(+) L(w16) molecules on untreated cells were stable. Together, these resul ts suggest that two L(d)-restricted, viral peptides can induce assembl y of or stabilize 30-5-7(+) 28-14-8(+) L(w16) molecules, mimicking end ogenous self peptides. However, the association of the L(d)-restricted peptides with L(W16) is apparently not optimal, since it results in u nstable L(w16) molecules.