Open AccessIdentification and characterisation of a Leishmania donovani antigen belonging to the 70‐kDa heat‐shock protein family
Author(s) -
MacFARLANE Juan,
BLAXTER Mark L.,
BISHOP Richard P.,
MILES Michael A.,
KELLY John M.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb15586.x
Subject(s) - leishmania donovani , heat shock protein , biology , antigen , microbiology and biotechnology , visceral leishmaniasis , cdna library , gene , complementary dna , clone (java method) , genomic library , virology , peptide sequence , leishmaniasis , genetics
A Leishmania donovani promastigote cDNA library was screened with serum obtained from a patient infected with visceral leishmaniasis. Sequence analysis of a clone obtained from this library revealed that the 600‐bp insert corresponded to the carboxy‐terminal region of an antigen related to the 70‐kDa heat‐shock protein family. The full‐length sequence of the corresponding gene (1959 nucleotides) was determined after isolation of genomic clones. Genes encoding the antigen are present on a single chromosome as a series of approximately twelve 3.7‐kb direct tandem repeats. The antigen can be identified as a 70‐kDa heat‐shock cognate protein by virtue of its molecular mass, sequence and constitutive expression during heat shock. It is expressed at all stages of the parasite life‐cycle. Antibodies against the λgt11 fusion protein were detected in more than 50% of serum samples obtained from patients with visceral leishmaniasis, but were not detected in sera from patients with cutaneous leishmaniasis or Chagas' disease.