Structural and dynamic features of HLA-B27 subtypes
B. Uchanska-Ziegler*; A. Ziegler; P. Schmieder
Curr. Opin. Rheumatol. 25, 411-418 (2013)
PURPOSE OF REVIEW: The
differential association of HLA-B27 subtypes with ankylosing spondylitis
provides the rationale for a comparative investigation of these proteins.
Results from the last 2 years of research on minimally distinct HLA-B27
subtypes, primarily using biochemical and biophysical techniques, are presented
and discussed.
RECENT FINDINGS: We summarize evidence that
micropolymorphisms within the molecules' peptide-binding groove influence
wide-ranging biochemical, biophysical and antigenic properties of HLA-B27
molecules, and suggest that distinct, subtype and peptide-dependent dynamics of
peptide - heavy chain - ?2-microglobulin heterotrimers could be instrumental
for an understanding of the initiation of disease processes that are connected
with certain HLA-B27 subtypes.
SUMMARY: The results indicate that
mAbs that bind only to structurally distinguishable subsets of HLA-B27
molecules as well as techniques that assess the flexibility of these antigens
may hold the key to comprehend molecular events contributing to the initial
stages of disease pathogenesis in spondyloarthropathies.