A. Kaliyaperumal et al., FUNCTIONAL EXPRESSION AND RECOGNITION OF NONCLASSICAL MHC CLASS-I T10(B) IS NOT PEPTIDE-DEPENDENT, The Journal of immunology, 155(5), 1995, pp. 2379-2386
Studies of classical and nonclassical MHC class I molecules have shown
that unique peptides are associated and functionally recognized by al
loreactive T cells. We have recently shown that an alloreactive TCR-ga
mma delta cell recognizes a nonclassical MHC molecule, T10(b). However
, T cell recognition of this glycoprotein did not appear to require ty
pical peptide recognition based on studies using transporter-defective
mutant cell lines. In the current study, we have analyzed in detail,
the role of peptide in T10(b) expression and recognition. The findings
reveal that the recognition of the nonclassical MHC molecule by TCR-g
amma delta cells is independent of species, tissue type, both the clas
s I and class II Ag processing and presentation pathways, or the prese
nce of peptides. In fact, biochemical analysis of the T10(b) chimeric
molecule, T10(b)/L(d), transfected into CHO cells using radiolabeled [
H-3]leucine, HPLC, and mass spectrometry suggest that peptides are not
associated with this nonclassical class I molecule. Therefore, some c
lass I molecules, e.g., T10(b), do not associate with polymorphic pept
ides typical of classical MHC class I molecules and can be expressed i
n the absence of peptides on the cell surface in a functionally active
form.