A role for erythrocyte band 3 degradation by the parasite gp76 serine protease in the formation of the parasitophorous vacuole during invasion of erythrocytes by Plasmodium falciparum

Mol Biochem Parasitol. 1996 Nov 12;82(1):13-24. doi: 10.1016/0166-6851(96)02714-4.

Abstract

A purified Plasmodium falciparum serine protease (gp76) implicated in erythrocyte invasion, degrades human erythrocyte band 3 and glycophorin A. Inhibition studies using synthetic peptides derived from the presumed band 3 enzymatic cleavage sites and the observed uptake of fluorescent phospholipids following gp76 treatment, suggest that band 3 degradation by this serine protease participates in the formation of the parasitophorous vacuole by restructuring the red cell cytoskeleton. These results provide a rationale for the elaboration of specific inhibitors to block red cell invasion by malaria parasites.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anion Exchange Protein 1, Erythrocyte / metabolism*
  • Chymotrypsin / metabolism
  • Erythrocytes / parasitology*
  • Glycophorins / metabolism
  • Humans
  • Liposomes / metabolism
  • Microscopy, Confocal
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Peptides / pharmacology
  • Plasmodium falciparum / enzymology*
  • Plasmodium falciparum / physiology
  • Serine Endopeptidases / metabolism*
  • Serine Proteinase Inhibitors / pharmacology
  • Vacuoles / metabolism
  • Vacuoles / parasitology

Substances

  • Anion Exchange Protein 1, Erythrocyte
  • Glycophorins
  • Liposomes
  • Peptides
  • Serine Proteinase Inhibitors
  • Serine Endopeptidases
  • Chymotrypsin