Open AccessMolecular characterization of a Leishmania donovani infantum antigen identified as histone H2A
Author(s) -
SOTO Manuel,
REQUENA Jose María,
GOMEZ Luis Carlos,
NAVARRETE Ignacio,
ALONSO Carlos
Publication year - 1992
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1992.tb16770.x
Subject(s) - biology , leishmania infantum , microbiology and biotechnology , complementary dna , histone h2a , histone , gene , histone h1 , genomic dna , cdna library , nucleic acid sequence , histone h4 , genetics , visceral leishmaniasis , leishmaniasis
A Leishmania donovani infantum promastigote cDNA expression library was screened with a serum obtained from a dog naturally infected with this parasite. One of the positive clones obtained revealed nucleotide sequence similarities with the histone H2A genes from various organisms. Northern blot analyses and sequence data of three independently isolated cDNA clones indicated that the Leishmania H2A mRNAs are polyadenylated, as are the basal histone mRNAs of higher eukaryotes and the histone mRNAs of yeast. The analysis of the genomic distribution of the DNA coding for histone H2A suggested that, in L. d. infantum , there are at least four genes coding for the H2A protein. It is likely that there is a simultaneous expression of at least two of the H2A genes since differences in nucleotide sequence between two of the sequenced cDNAs were observed. Affinity‐purified antibodies against the β‐galactosidase‐fused H2A protein recognize specifically a Leishmania protein band with a molecular mass of 14 kDa.