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Type: Journal article
Title: Biochemical and functional analysis of two plasmodium falciparum blood-stage 6-cys proteins: P12 and P41
Author: Taechalertpaisarn, T.
Crosnier, C.
Bartholdson, S.
Hodder, A.
Thompson, J.
Bustamante, L.
Wilson, D.
Sanders, P.
Wright, G.
Rayner, J.
Cowman, A.
Gilson, P.
Crabb, B.
Citation: PLoS One, 2012; 7(7):e41937-1-e41937-15
Publisher: Public Library of Science
Issue Date: 2012
ISSN: 1932-6203
Statement of
Tana Taechalertpaisarn, Cecile Crosnier, S. Josefin Bartholdson, Anthony N. Hodder, Jenny Thompson, Leyla Y. Bustamante, Danny W. Wilson, Paul R. Sanders, Gavin J. Wright, Julian C. Rayner, Alan F. Cowman, Paul R. Gilson, Brendan S. Crabb.
Abstract: The genomes of Plasmodium parasites that cause malaria in humans, other primates, birds, and rodents all encode multiple 6-cys proteins. Distinct 6-cys protein family members reside on the surface at each extracellular life cycle stage and those on the surface of liver infective and sexual stages have been shown to play important roles in hepatocyte growth and fertilization respectively. However, 6-cys proteins associated with the blood-stage forms of the parasite have no known function. Here we investigate the biochemical nature and function of two blood-stage 6-cys proteins in Plasmodium falciparum, the most pathogenic species to afflict humans. We show that native P12 and P41 form a stable heterodimer on the infective merozoite surface and are secreted following invasion, but could find no evidence that this complex mediates erythrocyte-receptor binding. That P12 and P41 do not appear to have a major role as adhesins to erythrocyte receptors was supported by the observation that antisera to these proteins did not substantially inhibit erythrocyte invasion. To investigate other functional roles for these proteins their genes were successfully disrupted in P. falciparum, however P12 and P41 knockout parasites grew at normal rates in vitro and displayed no other obvious phenotypic changes. It now appears likely that these blood-stage 6-cys proteins operate as a pair and play redundant roles either in erythrocyte invasion or in host-immune interactions.
Keywords: Erythrocytes
Plasmodium falciparum
Escherichia coli
Protozoan Proteins
Recombinant Proteins
Antibodies, Protozoan
Culture Media, Conditioned
Protein Structure, Quaternary
Protein Transport
Protein Multimerization
HEK293 Cells
Rights: 2012 Taechalertpaisarn et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in anymedium, provided the original author and source are credited.
DOI: 10.1371/journal.pone.0041937
Appears in Collections:Aurora harvest 2
Molecular and Biomedical Science publications

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