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Review
. 2008 Feb;20(1):105-10.
doi: 10.1016/j.coi.2007.10.007. Epub 2007 Dec 21.

Do the Peptide-Binding Properties of Diabetogenic Class II Molecules Explain Autoreactivity?

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Free PMC article
Review

Do the Peptide-Binding Properties of Diabetogenic Class II Molecules Explain Autoreactivity?

Anish Suri et al. Curr Opin Immunol. .
Free PMC article

Abstract

One seminal aspect in autoimmune diabetes is antigen presentation of beta cell antigens by the diabetes-propensity class II histocompatibility molecules. The binding properties of I-Ag7 molecules are reviewed here and an emphasis is placed on their selection of peptides with a highly specific sequence motif, in which one or more acidic amino acids are found at the carboxy end interacting at the P9 anchoring site of I-Ag7. The reasons for the central role of I-Ag7 in the autoimmune response are analyzed. The insulin B chain segment 9-23 is a hot spot for T cell selection and a striking example of a weak MHC binding peptide that triggers autoreactivity.

Figures

Figure 1
Figure 1
I-Ag7 binding motif as determined by the alignment results from the expectation-maximization alignment algorithm of Chang et al [27] and shown by WebLogo. Preferred amino acids from positions P1 to P9 are indicated by their one letter code.
Figure 2
Figure 2
Examples of two natural T cell clones from NOD mice that recognize different registers of the insulin peptide. The optimal register encompassed the entire 9-23 segment.

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