Human malaria parasite adenosine deaminase. Characterization in host enzyme-deficient erythrocyte culture

J Biol Chem. 1984 Feb 10;259(3):1472-5.

Abstract

Human malaria infected erythrocytes show a dramatic increase in adenosine deaminase activity in vitro. Using recently developed culture techniques, adenosine deaminase-deficient human erythrocytes were infected in vitro with the major human pathogen Plasmodium falciparum. Adenosine deaminase activity was undetectable in the uninfected host red cells, but increased by 2-fold over normal levels in these cells with an 8% parasitemia. The enzyme in these cells appeared unique in that its activity was markedly elevated over that of other parasite purine enzymes, was not cross-reactive with antibody against human erythrocyte adenosine deaminase, and though inhibited competitively by deoxycoformycin was relatively insensitive to erythro-9-(2-hydroxy-3-nonyl) adenine. The use of adenosine deaminase-deficient erythrocytes for the in vitro cultivation of Plasmodium provides a unique system for the study of parasite enzyme and allows further insight into the purine metabolism of the intraerythrocytic malaria parasite.

Publication types

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

MeSH terms

  • Adenosine Deaminase / deficiency
  • Adenosine Deaminase / isolation & purification
  • Adenosine Deaminase / metabolism*
  • Animals
  • Coformycin / analogs & derivatives
  • Coformycin / pharmacology
  • Erythrocytes / physiology*
  • Humans
  • Immunosuppressive Agents / pharmacology
  • Kinetics
  • Nucleoside Deaminases / metabolism*
  • Pentostatin
  • Plasmodium falciparum / enzymology*

Substances

  • Immunosuppressive Agents
  • Coformycin
  • Pentostatin
  • Nucleoside Deaminases
  • Adenosine Deaminase