Different modes of peptide interaction enable HLA-DQ and HLA-DR molecules to bind diverse peptide repertoires.
The role of HLA-DQ molecules in Ag presentation has, thus far, remained elusive. Here we report that two DQ allotypes, DQ7 (DQA1*0501/B1*0301) and DQ9 (DQA1*0201/B1*0303), are capable of binding peptide repertoires in complementarity with DR molecules. The results reflect fundamental differences in the binding modes of these two HLA class II isotypes, in that DQ7 and DQ9 but not DR molecules appear to have the capacity to bind peptide structures without type 1-like anchor residues. Consistent with this is our observation that none of the amino acid side chains of the class II-associated invariant chain peptides (CLIP) are required for association with DQ7 and DQ9, even though many of them are essential for CLIP-DR interaction. Together, these data reveal a functional complementarity of HLA-DR and -DQ molecules in Ag presentation.
Raddrizzani
L
L
Roche Milano Ricerche, Milan, Italy.
Sturniolo
T
T
Guenot
J
J
Bono
E
E
Gallazzi
F
F
Nagy
Z A
ZA
Sinigaglia
F
F
Hammer
J
J
D000595:Amino Acid Sequence; D017951:Antigen Presentation; D006683:HLA-DQ Antigens / Q000737:chemistry / Q000276:immunology*; D006684:HLA-DR Antigens / Q000737:chemistry / Q000276:immunology*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000276:immunology*; D011485:Protein Binding / Q000276:immunology
D006683:HLA-DQ Antigens; D006684:HLA-DR Antigens; D010455:Peptides