Cloning and characterization of the Leishmania (Viannia) braziliensis Hsp70 gene. Diagnostic use of the C-terminal fragment rLb70(513-663)

The Journal of Parasitology
Ada I ZuritaBasilio Valladares

Abstract

Cross-reactions between Leishmania braziliensis and Trypanosoma cruzi caused by common antigenic determinants hinder the specific diagnosis of cutaneous and mucocutaneous leishmaniasis (CL and MCL). Therefore, the usefulness of the 70-kDa heat shock protein (Hsp70) from L. braziliensis for differential serodiagnosis was investigated. The single-copy gene encoding Hsp70, consisting of 663 amino acids, was isolated from a genomic DNA library. The antigenicity data show that Hsp70 is an immunodominant antigen highly recognized (84%) by sera of patients with CL and MCL and to a lesser extent by chagasic patients (18.75%). Antigenic mapping of the 5 overlapping fragments into which the protein was split showed that the main antigenic determinants are located in the carboxy-terminal end. The linear antigenic determinants that show cross-reactions with chagasic sera are located in the fragment rLb70(352-518). The carboxy-terminal fragment rLb70(513-663) presents 70% sensitivity and 100% specificity, so it could be a potential candidate for specific serodiagnosis of CL and MCL caused by L. braziliensis.

References

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Citations

Jul 28, 2019·Proteomics. Clinical Applications·Janaína Capelli-PeixotoBeatriz Simonsen Stolf
Nov 4, 2020·Infection and Immunity·Pragya Prasanna, Arun Upadhyay

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Datasets Mentioned

BETA
AF291716

Methods Mentioned

BETA
enzyme-linked immunosorbent assay
biopsy
ELISA
PCR
electrophoresis

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