Food vacuole plasmepsins are processed at a conserved site by an acidic convertase activity in Plasmodium falciparum.

Abstract:

:Intraerythrocytic Plasmodium falciparum digests vast amounts of hemoglobin within an acidic food vacuole (FV). Four homologous aspartic proteases participate in hemoglobin degradation within the FV. Plasmepsin (PM) I and II are thought to initiate degradation of the native hemoglobin molecule. PM IV and histo-aspartic protease (HAP) act on denatured globin further downstream in the pathway. PM I and II have been shown to be synthesized as zymogens and activated by proteolytic removal of a propiece. In this study, we have determined that the proteolytic processing of FV plasmepsins occurs immediately after a conserved Leu-Gly dipeptidyl motif with uniform kinetics and pH and inhibitor sensitivities. We have developed a cell-free in vitro processing assay that generates correctly processed plasmepsins. Our data suggest that proplasmepsin processing is not autocatalytic, but rather is mediated by a separate processing enzyme. This convertase requires acidic conditions and is blocked only by the calpain inhibitors, suggesting that it may be an atypical calpain-like protease.

journal_name

Mol Biochem Parasitol

authors

Banerjee R,Francis SE,Goldberg DE

doi

10.1016/s0166-6851(03)00119-1

subject

Has Abstract

pub_date

2003-07-01 00:00:00

pages

157-65

issue

2

eissn

0166-6851

issn

1872-9428

pii

S0166685103001191

journal_volume

129

pub_type

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