functional evaluation of plasmodium export signals in plasmodium berghei suggests multiple modes of protein export功能评价鼠疟原虫出口信号表明多个蛋白出口模式.pdfVIP

Functional Evaluation of Plasmodium Export Signals in Plasmodium berghei Suggests Multiple Modes of Protein Export 1 2 Puran Singh Sijwali *, Philip J. Rosenthal * 1 Centre for Cellular and Molecular Biology, Hyderabad, India, 2 Department of Medicine, San Francisco General Hospital, University of California San Francisco, San Francisco, California, United States of America Abstract The erythrocytic stage development of malaria parasites occurs within the parasitophorous vacuole inside the infected- erythrocytes, and requires transport of several parasite-encoded proteins across the parasitophorous vacuole to several locations, including the cytosol and membrane of the infected cell. These proteins are called exported proteins; and a large number of such proteins have been predicted for Plasmodium falciparum based on the presence of an N-terminal motif known as the Plasmodium export element (PEXEL) or vacuolar transport signal (VTS), which has been shown to mediate export. The majority of exported proteins contain one or more transmembrane domains at the C-terminus and one of three types of N-terminus domain architectures. (1) The majority, including the knob-associated histidine rich protein (KAHRP), contain a signal/hydrophobic sequence preceding the PEXEL/VTS motif. (2) Other exported proteins, including the P. berghei variant antigen family bir and the P. falciparum skeleton binding protein-1, do not appear to contain a PEXEL/VTS motif. (3) The P. falciparum erythrocyte membrane protein-1 (PfEMP1) family lacks a signal/hydrophobic sequence before the motif. These different domain architectures suggest the presence of multiple export pathways in malaria parasites. To determine if export pathways are conserved in plasmodia and to develop an experimental syste