The activity and inhibition of the food vacuole plasmepsin from the rodent malaria parasite Plasmodium chabaudi

Tiago M. Martins, Ana Domingos, Colin Berry, David M. Wyatt

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

The rodent malaria parasite Plasmodium chabaudi encodes one food vacuole plasmepsin - the aspartic proteinases important in haemoglobin degradation. A recombinant form of this enzyme was found to cleave a variety of peptide substrates and was susceptible to a selection of naturally occurring and synthetic inhibitors, displaying an inhibition profile distinct from that of aspartic proteinases from other malaria parasites. In addition, inhibitors of HIV proteinase that kill P. chabaudi in vivo were also inhibitors of this new plasmepsin. P. chabaudi is a widely used model for human malaria species and, therefore, the characterisation of this plasmepsin is an important contribution towards understanding its biology.

Original languageEnglish
Pages (from-to)212-218
Number of pages7
JournalActa Tropica
Volume97
Issue number2
DOIs
Publication statusPublished - Feb 2006

Keywords

  • Aspartic proteinase
  • New plasmepsin
  • Plasmodium chabaudi
  • Rodent malaria model

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