Malaria parasite proteins that remodel the host erythrocyte
- Author(s)
- Maier, AG; Cooke, BM; Cowman, AF; Tilley, L;
- Details
- Publication Year 2009-05,Volume 7,Issue #5,Page 341-354
- Journal Title
- NATURE REVIEWS MICROBIOLOGY
- Publication Type
- Journal Article
- 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.
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- FALCIPARUM-INFECTED ERYTHROCYTES; RED-BLOOD-CELLS; HISTIDINE-RICH PROTEIN; PARASITOPHOROUS VACUOLE MEMBRANE; VESICLE-MEDIATED TRAFFICKING; MAURERS CLEFT ORGANELLES; RING-EXPORTED PROTEIN-1; PLASMODIUM-FALCIPARUM; SURFACE-ANTIGEN; BINDING DOMAIN
- Publisher's Version
- https://doi.org/10.1038/nrmicro2110
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2009-05-01 12:00:00