Targeting malaria virulence and remodeling proteins to the host erythrocyte

Marti, M. , Good, R. T., Rug, M., Knueppfer, E. and Cowman, A. F. (2004) Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science, 306(5703), pp. 1930-1933. (doi: 10.1126/science.1102452) (PMID:15591202)

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To establish infection in the host, malaria parasites export remodeling and virulence proteins into the erythrocyte. These proteins can traverse a series of membranes, including the parasite membrane, the parasitophorous vacuole membrane, and the erythrocyte membrane. We show that a conserved pentameric sequence plays a central role in protein export into the host cell and predict the exported proteome in Plasmodium falciparum. We identified 400 putative erythrocyte-targeted proteins corresponding to ∼8% of all predicted genes, with 225 virulence proteins and a further 160 proteins likely to be involved in remodeling of the host erythrocyte. The conservation of this signal across Plasmodium species has implications for the development of new antimalarials.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Marti, Professor Matthias
Authors: Marti, M., Good, R. T., Rug, M., Knueppfer, E., and Cowman, A. F.
College/School:College of Medical Veterinary and Life Sciences > School of Infection & Immunity
Journal Name:Science
Publisher:American Association for the Advancement of Science
ISSN (Online):1095-9203

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