%A Hussain R
%A Dockrell HM
%A Kifayet A
%A Daud A
%A Watson JD
%A Chiang TJ


%T Recognition of <em>Mycobacterium leprae</em> recombinant 18-KDa proteins in leprosy

%0 Journal Article

%D 1992

%J International Journal of Leprosy and other Mycobacterial Diseases

%P 0148-916X

%V 60

%N 3

%X Three different, purified, <em>Escherichia coli</em> derived, recombinant preparations of the <em>Mycobacterium leprae</em> 18K protein were compared for their immunological recognition in leprosy. The preparations tested were 18K fusion proteins containing 70% (amino acids 38-148) of the full 18K protein fused to either a short leader sequence containing six asparagine residues or to <em> &#946;</em>-galactosidase, and the full length 18K protein. All three recombinant antigens were recognized by IgG antibodies which were restricted mostly to lepromatous leprosy patients. The 18K antigen with the asparagine leader sequence showed better reactivity with IgG antibodies compared with the other two 18K preparations. In lymphocyte proliferation assays, the truncated 18Kand the full-length 18K showed equivalent responses in the same donors with strongest recognition in donors who were also strongly responsive to the <em>M. leprae</em> soluble sonicate. These results indicate that the major human B- and T-cell epitopes are located within the segment 38-148, although some individuals may recognize additional epitopes at the NH<sub>2</sub>-terminal end.