Purification of two Leishmania donovani membrane proteins recognized by sera from patients with visceral leishmaniasis

Charles L. Jaffe*, Mariano Zalis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Two Leishmania donovani membrane proteins recognized by sera from patients with visceral leishmaniasis were purified using species-specific monoclonal antibodies and characterized. The molecular weights of the proteins, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were ∼ 70 000 and ∼ 72 000, respectively. The 70 kDa protein, which appears as a diffuse band on silver staining, was resolved into a doublet by Western blotting with monoclonal antibody. Though of similar molecular weight and amino acid composition, the two proteins were shown to be distinct by peptide mapping and Western blotting of the purified material. The two proteins are recognized specifically by human visceral leishmaniasis serum and not by serum from cutaneous leishmaniasis or Chagas' disease. These proteins will be useful in developing a direct serodiagnostic assay for visceral leishmaniasis.

Original languageEnglish
Pages (from-to)53-62
Number of pages10
JournalMolecular and Biochemical Parasitology
Volume27
Issue number1
DOIs
StatePublished - 1 Jan 1988
Externally publishedYes

Keywords

  • Immunodiagnosis
  • Leishmania donovani
  • Membrane protein purification
  • Patient sera

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