Localisation of hypoxanthine phosphoribosyl transferase in the malaria parasite Plasmodium falciparum

Exp Parasitol. 1992 Feb;74(1):11-9. doi: 10.1016/0014-4894(92)90134-v.


The enzyme hypoxanthine phosphoribosyl transferase of the human malaria parasite Plasmodium falciparum has been located in parasites and parasite-infected erythrocytes by antibody probing. The probe was a polyclonal rabbit antiserum made against the parasite enzyme made in Escherichia coli. The enzyme is associated with membrane-bound compartments in merozoites and asexual blood parasites. In particular, indirect immunofluorescence studies reveal the enzyme localized in vesicle-like structures within the cytoplasm of the infected erythrocyte. This is the first time a P. falciparum protein of defined metabolic function has been tracked to a site outside the parasite cytosol. Studies on the targeting of the enzyme using a cell-free system suggests that the protein reaches its destination via a route different from the normal secretory pathway.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Transport
  • Blotting, Western
  • DNA
  • Erythrocytes / enzymology
  • Erythrocytes / parasitology
  • Humans
  • Hypoxanthine Phosphoribosyltransferase / analysis*
  • Hypoxanthine Phosphoribosyltransferase / blood
  • Hypoxanthine Phosphoribosyltransferase / genetics
  • Malaria, Falciparum / enzymology
  • Microscopy, Fluorescence
  • Microscopy, Immunoelectron
  • Molecular Sequence Data
  • Plasmodium falciparum / enzymology*


  • DNA
  • Hypoxanthine Phosphoribosyltransferase