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

Martins, Tiago M., Domingos, Ana, Berry, Colin ORCID: https://orcid.org/0000-0002-9943-548X and Wyatt, David 2006. The activity and inhibition of the food vacuole plasmepsin from the rodent malaria parasite Plasmodium chabaudi. Acta Tropica 97 (2) , pp. 212-218. 10.1016/j.actatropica.2005.11.001

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > Q Science (General)
Uncontrolled Keywords:	Rodent malaria model; Plasmodium chabaudi; Aspartic proteinase; New plasmepsin.
Publisher:	Elsevier
ISSN:	0001-706X
Last Modified:	27 Oct 2022 08:31
URI:	https://orca.cardiff.ac.uk/id/eprint/62585

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