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J Biol Chem, Vol. 273, Issue 36, 23398-23409, September 4, 1998
From the In the vertebrate host, the malaria parasite
invades and replicates asexually within circulating erythrocytes.
Parasite proteolytic enzymes play an essential but poorly understood
role in erythrocyte invasion. We have identified a Plasmodium
falciparum gene, denoted pfsub-1, encoding a member
of the subtilisin-like serine protease family (subtilases). The
pfsub-1 gene is expressed in asexual blood stages of
P. falciparum, and the primary gene product (PfSUB-1) undergoes post-translational processing during secretory transport in a
manner consistent with its being converted to a mature, enzymatically active form, as documented for other subtilases. In the invasive merozoite, the putative mature protease (p47) is concentrated in dense
granules, which are secretory organelles located toward the apical end
of the merozoite. At some point following merozoite release and
completion of erythrocyte invasion, p47 is secreted from the parasite
in a truncated, soluble form. The subcellular location and timing of
secretion of p47 suggest that it is likely to play a role in
erythrocyte invasion. PfSUB-1 is a new potential target for
antimalarial drug development.
A Subtilisin-like Protein in Secretory Organelles of
Plasmodium falciparum Merozoites
,
,
,
,
,
,
, and
Division of Parasitology, National Institute
for Medical Research, Mill Hill, London NW7 1AA, United Kingdom, the
¶ Institute of Pathology, Case Western Reserve University,
Cleveland, Ohio 44106, and the 
Institute of
Medical Sciences, Tokai University, Boseidai, Isehara,
Kanagawa 259-11, Japan
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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