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Infection and Immunity, October 1998, p. 4903-4909, Vol. 66, No. 10
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

T-Cell Recognition of Mycobacterial GroES Peptides in Thai Leprosy Patients and Contacts

Boosbun Chua-Intra,1,2 Somchai Peerapakorn,2 Nick Davey,3 Stipo Jurcevic,1 Marc Busson,4 H. Martin Vordermeier,1 Charoon Pirayavaraporn,2 and Juraj Ivanyi1,*

Tuberculosis and Related Infections Unit, MRC Clinical Sciences Centre,1 and Department of Immunology, Royal Postgraduate Medical School,3 Hammersmith Hospital, London W12, United Kingdom; Leprosy Division, Department of Communicable Disease Control, Ministry of Public Health, Bangkok, Thailand2; and INSERM U 396, Immunogénétique Humaine, Centre HAYEM, Hôpital Saint-Louis, 75010 Paris, France4

Received 23 March 1998/Returned for modification 25 May 1998/Accepted 23 July 1998

We report here the mapping of T-cell-stimulatory determinants of the GroES 10-kDa heat shock protein homologues from Mycobacterium leprae and Mycobacterium tuberculosis, which are known as major immunogens in mycobacterial infections. Peripheral blood mononuclear cells (PBMC) from treated tuberculoid leprosy or lepromatous leprosy patients and from healthy household or hospital staff contacts of the patients were cultured with 20 16-mer peptides covering the entire sequences of both M. leprae and M. tuberculosis GroES. The total number of recognized peptides was found to be the largest in family contacts, while responder frequencies to the individual tested peptides varied (5 to 80%) with specificity between the patient and contact groups. Proliferative responses to some peptides showed positive or negative associations of low statistical significance with DR and DQ alleles, though responses to most GroES peptides were genetically permissive. Notably, the sequence of the 25-40 peptide of M. leprae, but not that of M. tuberculosis, was more frequently stimulatory in tuberculoid leprosy patients than in either group of sensitized healthy contacts. This peptide bound to a number of HLA-DR molecules, of which HLA-DRB5*0101 had the strongest affinity. The epitope core binding to this allele was localized to the 29-to-37 sequence, and its key residue was localized to the M. leprae-specific glutamic acid at position 32. This epitope may be of interest for the development of a blood test- or skin test-based diagnostic reagent for tuberculoid leprosy, subject to further clinical evaluation in untreated patients.

* Corresponding author. Present address: Department of Oral Medicine and Pathology, UMDS at Guy's Hospital, Floor 28 Guy's Tower, London SE1 9RT, United Kingdom. Phone: 171-955 4568. Fax: 171-955 4455. E-mail: j.ivanyi{at}umds.ac.uk.

Infection and Immunity, October 1998, p. 4903-4909, Vol. 66, No. 10
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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