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Infection and Immunity, June 2004, p. 3161-3170, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3161-3170.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Comparative Analysis of B- and T-Cell Epitopes of Mycobacterium leprae and Mycobacterium tuberculosis Culture Filtrate Protein 10

John S. Spencer,1* Hee Jin Kim,1 Angela M. Marques,1 Mercedes Gonzalez-Juarerro,1 Monica C. B. S. Lima,2 Varalakshmi D. Vissa,1 Richard W. Truman,3 Maria Laura Gennaro,4 Sang-Nae Cho,5 Stewart T. Cole,6 and Patrick J. Brennan1

Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, Colorado,1 Laboratory of Immunopathology, State University of Rio de Janeiro, Rio de Janeiro, Brazil,2 National Hansen's Disease Center, Louisiana State University, Baton Rouge, Louisiana,3 Public Health Research Institute, Newark, New Jersey,4 Yonsei University College of Medicine, Seoul, Republic of Korea,5 Institut Pasteur, Paris, France6

Received 18 November 2003/ Returned for modification 2 January 2004/ Accepted 27 February 2004

Culture filtrate protein 10 (CFP-10) from Mycobacterium tuberculosis is a well-characterized immunodominant 10-kDa protein antigen known to elicit a very potent early gamma interferon response in T cells from M. tuberculosis-infected mice and humans. The sequence of the Mycobacterium leprae homologue of CFP-10 shows only 40% identity (60% homology) at the protein level with M. tuberculosis CFP-10 and thus has the potential for development as a T- or B-cell reactive antigen for specific diagnosis of leprosy. Antisera raised in mice or rabbits against recombinant M. leprae and M. tuberculosis CFP-10 proteins reacted only with homologous peptides from arrays of overlapping synthetic peptides, indicating that there was no detectable cross-reactivity at the antibody level. Sera from leprosy and tuberculosis patients were also specific for the homologous protein or peptides and showed distinct patterns of recognition for either M. leprae or M. tuberculosis CFP-10 peptides. At the cellular level, only 2 of 45 mouse T-cell hybridomas raised against either M. leprae or M. tuberculosis CFP-10 displayed a cross-reactive response against the N-terminal heterologous CFP-10 peptide, the region that exhibits the highest level of identity in the two proteins; however, the majority of peptide epitopes recognized by mouse T-cell hybridomas specific for each protein did not cross-react with heterologous peptides. Coupled with the human serology data, these results raise the possibility that peptides that could be used to differentiate infections caused by these two related microorganisms could be developed. Immunohistochemical staining of sections of M. leprae-infected nude mouse footpads resulted in strongly positive staining in macrophages and dendritic cells, as well as weaker staining in extracellular areas, suggesting that M. leprae CFP-10, like its homologue in M. tuberculosis, is a secreted protein.

* Corresponding author. Mailing address: Department of Microbiology, Immunology and Pathology, Colorado State University, Campus Delivery 1682, Fort Collins, CO 80523. Phone: (970) 491-2432. Fax: (970) 491-1815. E-mail: John.Spencer{at}colostate.edu.

Editor: F. C. Fang

Infection and Immunity, June 2004, p. 3161-3170, Vol. 72, No. 6
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.6.3161-3170.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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