Malaria parasite proteins that remodel the host erythrocyte
Date
2009
Authors
Maier, Alex
Cooke, Brian M.
Cowman, A
Tilley, Leann
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Nature Publishing Group
Abstract
Exported proteins of the malaria parasite Plasmodium falciparum interact with proteins of the erythrocyte membrane and induce substantial changes in the morphology, physiology and function of the host cell. These changes underlie the pathology that is responsible for the deaths of 1-2 million children every year due to malaria infections. The advent of molecular transfection technology, including the ability to generate deletion mutants and to introduce fluorescent reporter proteins that track the locations and dynamics of parasite proteins, has increased our understanding of the processes and machinery for export of proteins in P. falciparum-infected erythrocytes and has provided us with insights into the functions of the parasite protein exportome. We review these developments, focusing on parasite proteins that interact with the erythrocyte membrane skeleton or that promote delivery of the major virulence protein, PfEMP1, to the erythrocyte membrane.
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Keywords
Keywords: ankyrin; CD36 antigen; erythrocyte membrane protein 1; glucose transporter 1; glycophorin A; glycophorin C; mature parasite infected erythrocyte surface antigen; membrane associated His rich protein 1; Plasmodium falcifarum antigen 332; Plasmodium falcifa
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Source
Nature Reviews Microbiology
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Journal article
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2037-12-31
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