Malaria parasite proteins that remodel the host erythrocyte

Date

2009

Authors

Maier, Alex
Cooke, Brian M.
Cowman, A
Tilley, Leann

Journal Title

Journal ISSN

Volume Title

Publisher

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.

Description

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

Citation

Source

Nature Reviews Microbiology

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

Restricted until

2037-12-31