Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites

被引:16
作者
Bhattacharjee, Souvik [1 ,2 ]
Stahelin, Robert V. [1 ,3 ,4 ]
Haldar, Kasturi [1 ,2 ]
机构
[1] Univ Notre Dame, Ctr Rare & Neglected Dis, Notre Dame, IN 46556 USA
[2] Univ Notre Dame, Dept Biol Sci, Notre Dame, IN 46556 USA
[3] Indiana Univ Sch Med S Bend, Dept Biochem & Mol Biol, South Bend, IN 46617 USA
[4] Univ Notre Dame, Dept Chem & Biochem, Notre Dame, IN 46556 USA
关键词
malaria; phosphoinositides; host targeting; pathogenic secretion; export; blood cells; endoplasmic reticulum; PLASMODIUM; PROTEINS; MEMBRANE; EXPORT; TRAFFICKING; TRANSPORT; SIGNAL;
D O I
10.1016/j.pt.2012.09.004
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
Blood stage malaria parasites target a 'secretome' of hundreds of proteins including virulence determinants containing a host (cell) targeting (HT) signal, to human erythrocytes. Recent studies reveal that the export mechanism is due to the HT signal binding to the lipid phosphatidylinositol-3-phosphate [PI(3)P] in the parasite endoplasmic reticulum (ER). An aspartic protease plasmepsin V which cleaves a specialized form of the HT signal was previously thought to be the export mechanism, but is now recognized as a dedicated peptidase that cleaves the signal anchor subsequent to PI(3)P binding. We discuss a model of PI(3)P-dependent targeting and PI(3)P biology of a major human pathogen.
引用
收藏
页码:555 / 562
页数:8
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