期刊
JOURNAL OF IMMUNOLOGY
卷 177, 期 4, 页码 2123-2130出版社
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.177.4.2123
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- NCI NIH HHS [1F32 CA 111041-01] Funding Source: Medline
- NIAID NIH HHS [2R01 AI 19624] Funding Source: Medline
The mouse multimember family of Qa-2 oligomorphic class I MHC genes is continuously undergoing duplications and deletions that alter the number of the two prototype Qa-2 sequences, Q8 and Q9. The frequent recombination events within the Q region lead to strain-specific modulation of the cumulative Qa-2 expression levels. Q9 protects C57BL/6 hosts from multiple disparate tumors and functions as a major CTL restriction element for shared tumor-associated Ags. We have now analyzed functional and structural properties of Q8, a class I MHC that differs significantly from Q9 in the peptide-binding, CTL-interacting alpha(1) and alpha(2) regions. Unexpectedly, we find that the extracellular domains of Q8 and Q9 act similarly during primary and secondary rejection of tumors, are recognized by cross-reactive antitumor CTL, have overlapping peptide-binding motifs, and are both assembled via the transporter associated with the Ag processing pathway. These findings suggest that shared Ag-presenting functions of the odd and even Qa-2 loci may contribute to the selective pressures shaping the haplotype-deperident quantitative variation of Qa-2 protein expression.
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