H. Direskeneli et al., RECOGNITION OF B-CELL EPITOPES OF THE 65 KDA HSP IN BEHCETS-DISEASE, Scandinavian journal of immunology, 43(4), 1996, pp. 464-471
B-cell epitopes of the mycobacterial 65 kDa heat shock protein (HSP) w
ere mapped in sera from patients with Behcet's (BD). A series of 47 ov
erlapping synthetic peptides (15(ers)) derived from the sequence of th
e Mycobacterium tuberculosis 65 kDa HSP was used in ELISA. Significant
increases in IgA and IgG antibody levels were observed with peptides
111-125, 154-172 and 311-326 in sera from BD, compared with those from
controls. Homologous peptides derived from the sequence of the human
mitochondrial 60 kDa HSP were then examined. Peptides 136-150 and 336-
351 showed comparable results to the homologous mycobacterial peptides
111-125 and 311-326, respectively. The B-cell epitopes defined in thi
s investigation overlap with the T-cell epitopes the authors have prev
iously reported in BD. Inhibition studies are consistent with the view
that antibodies to each of the three B-cell epitope peptides represen
t a small proportion of the total B-cell epitope repertoire elicited b
y the 65 or 60 kD HSP. Sequential antibody studies suggest that IgA an
d IgG antibody titres to one or all three peptides tested map increase
during exacerbations of ocular disease. The functional role of these
antibodies needs to be determined, but the peptides may be involved in
the immunopathogenesis of BD as they can induce experimental uveitis
in Lewis rats, which is a principal manifestation of BD.