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Infect Immun, June 1998, p. 2684-2690, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Molecular and Immunological Analyses of the Mycobacterium avium Homolog of the Immunodominant Mycobacterium leprae 35-Kilodalton Protein

James A. Triccas,1,dagger Nathalie Winter,1,dagger Paul W. Roche,1,Dagger Andrea Gilpin,2 Kathleen E. Kendrick,3 and Warwick J. Britton1,*

Centenary Institute of Cancer Medicine and Cell Biology, Newtown, New South Wales 2042, Australia1; Department of Plant Sciences, The University of Western Ontario, London, Ontario, Canada N6A 5B72; and Department of Microbiology, The Ohio State University, Columbus, Ohio 432103

Received 9 January 1998/Returned for modification 2 February 1998/Accepted 16 March 1998

The analysis of host immunity to mycobacteria and the development of discriminatory diagnostic reagents relies on the characterization of conserved and species-specific mycobacterial antigens. In this report, we have characterized the Mycobacterium avium homolog of the highly immunogenic M. leprae 35-kDa protein. The genes encoding these two proteins were well conserved, having 82% DNA identity and 90% identity at the amino acid level. Moreover both proteins, purified from the fast-growing host M. smegmatis, formed multimeric complexes of around 1000 kDa in size and were antigenically related as assessed through their recognition by antibodies and T cells from M. leprae-infected individuals. The 35-kDa protein exhibited significant sequence identity with proteins from Streptomyces griseus and the cyanobacterium Synechoccocus sp. strain PCC 7942 that are up-regulated under conditions of nutrient deprivation. The 67% amino acid identity between the M. avium 35-kDa protein and SrpI of Synechoccocus was spread across the sequences of both proteins, while the homologous regions of the 35-kDa protein and the P3 sporulation protein of S. griseus were interrupted in the P3 protein by a divergent central region. Assessment by PCR demonstrated that the gene encoding the M. avium 35-kDa protein was present in all 30 M. avium clinical isolates tested but absent from M. intracellulare, M. tuberculosis, or M. bovis BCG. Mice infected with M. avium, but not M. bovis BCG, developed specific immunoglobulin G antibodies to the 35-kDa protein, consistent with the observation that tuberculosis patients do not recognize the antigen. Strong delayed-type hypersensitivity was elicited by the protein in guinea pigs sensitized with M. avium.

* Corresponding author. Mailing address: Centenary Institute of Cancer Medicine and Cell Biology, Locked Bag no. 6, Newtown, NSW 2042, Australia. Phone: 61-2-9515-7098. Fax: 61-2-9565-6101. E-mail: wbritton{at}medicine.usyd.edu.au.

dagger Present address: Unité de Génétique Mycobactérienne, Institut Pasteur, 75724 Paris Cedex 15, France.

Dagger Present address: Mycobacterial Research Laboratories, Anandaban Leprosy Hospital, Kathmandu, Nepal.

Infect Immun, June 1998, p. 2684-2690, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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