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J Biol Chem, Vol. 273, Issue 19, 11440-11447, May 8, 1998
From the Department of Medicine and Therapeutics, University of
Aberdeen, Foresterhill,
Aberdeen, AB25 2ZD, Scotland, United Kingdom
Class II molecules are believed to influence
immune responses by selectively binding antigen-derived peptides for
recognition by T cells. In Goodpasture's (anti-glomerular basement
membrane) disease, autoimmunity to the NC1 domain of the Three nested sets of naturally presented 
3-chain of
type IV collagen (3(IV)NC1) is strongly associated with HLA-DR15. We
have examined the influence of the peptide binding preferences of DR15
molecules on the selection of 3(IV)NC1-derived peptides displayed
bound to DR15 molecules on the surface of 3(IV)NC1-pulsed DR15-homozygous Epstein-Barr virus-transformed human B cells. The
preferences of DR15 molecules were investigated using a panel of 24 overlapping peptides spanning the sequence of 3(IV)NC1. The
3(IV)NC1-derived peptides selected for display to T cells were
determined by biochemical analysis as reported previously (Phelps,
R. G., Turner, A. N., and Rees, A. J. (1996)
J. Biol. Chem. 271, 18549-18553).
3(IV)NC1 peptides were
detectable bound to DR15 molecules. Peptides representative of each
nested set bound to DR15 molecules, but almost two-thirds of the
3(IV)NC1 peptides studied had as good or better DR15 affinity than
those identified as naturally processed. Thus 3(IV)NC1 presentation to T cells is determined more by "processing factors" than by the
preferences of relatively indiscriminate DR15 molecules. The results
have important implications for the use of class II peptide binding
data to aid identification of potential T cell epitopes, especially for
antigens which, like 3(IV)NC1, contain many sequences able to bind
class II molecules.
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