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
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.