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Molecular Characterization of a Kinesin-Related Antigen of Leishmania chagasi that Detects Specific Antibody in African and American Visceral Leishmaniasis

We report the cloning of a Leishmania chagasi antigen gene and an evaluation of leishmaniasis patient antibody responses to the recombinant protein, rK39. rK39 contains a 39-amino acid repeat that is part of a 230-kDa protein predominant in L. chagasi tissue amastigotes. Sequence analyses showed thi...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1993-01, Vol.90 (2), p.775-779
Main Authors: Burns, James M., Shreffler, Wayne G., Benson, Darin R., Ghalib, Hashim W., Badaro, Roberto, Reed, Steven G.
Format: Article
Language:English
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Summary:We report the cloning of a Leishmania chagasi antigen gene and an evaluation of leishmaniasis patient antibody responses to the recombinant protein, rK39. rK39 contains a 39-amino acid repeat that is part of a 230-kDa protein predominant in L. chagasi tissue amastigotes. Sequence analyses showed this protein, LcKin, to be related to the kinesin superfamily of metor proteins. Southern blot analyses demonstrated LcKin-related sequences in seven species of Leishmania, with conservation of the repeat between L. chagasi and Leishmania donovani. Serological evaluation revealed that 98% (56 of 57) of Brazilian and 100% (52 of 52) of Sudanese visceral leishmaniasis patients have high antibody levels to the rK39 repeat. Detectable anti-K39 antibody was virtually absent in cutaneous and mucosal leishmaniasis patients and in individuals infected with Trypanosoma cruzi. The data show that rK39 may replace crude parasite antigens as a basis for serological diagnosis of visceral leishmaniasis.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.90.2.775