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. 1990 Jan;58(1):80–87. doi: 10.1128/iai.58.1.80-87.1990

A major immunogenic 36,000-molecular-weight antigen from Mycobacterium leprae contains an immunoreactive region of proline-rich repeats.

J E Thole 1, L F Stabel 1, M E Suykerbuyk 1, M Y De Wit 1, P R Klatser 1, A H Kolk 1, R A Hartskeerl 1
PMCID: PMC258411  PMID: 1688422

Abstract

The 36,000-molecular-weight antigen (36K antigen) of Mycobacterium leprae is a major immunogenic protein carrying common and specific antigenic determinants recognized by antibodies and T cells in leprosy patients. Recombinant DNA clones containing the complete gene coding for the 36 K antigen, designated in this paper as PRA, were isolated from both lambda gt11 and cosmid libraries of the M. leprae genome. The DNA sequence of the pra gene coded for a polypeptide of 249 amino acids with a predicted molecular mass of 26,299 daltons. The deduced amino acid sequence revealed a proline-rich (42%) amino-terminal region containing a number of repeated sequences similar or identical to the sequence PGGSYPPPPP. The reactivity of four monoclonal antibodies (F47-9, F67-1, F67-5, and F126-5) was directed to this proline-rich region of the PRA protein. DNA sequence and immunological data indicated that the lambda gt11 recombinant Y3180, which was previously isolated by using antibody F47-9 (R. A. Young, V. Mehra, D. Sweetser, T. Buchanan, J. Clark-Curtiss, R. W. Davis, and B. R. Bloom, Nature (London) 316:450-452, 1985), specifies a fusion protein unrelated to PRA but containing a similar epitope recognized by F47-9.

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