Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface

dc.contributor.authorJiang, Rays H. Y.
dc.contributor.authorStahelin, Robert V.
dc.contributor.authorBhattacharjee, Souvik
dc.contributor.authorHaldar, Kasturi
dc.contributor.departmentBiochemistry and Molecular Biology, School of Medicine
dc.date.accessioned2025-05-27T11:02:33Z
dc.date.available2025-05-27T11:02:33Z
dc.date.issued2013
dc.description.abstractSimilar to bacteria, eukaryotic pathogens may utilize common strategies of pathogenic secretion, because effector proteins from the oomycete Phytophthora infestans and virulence determinants from the human malaria parasite Plasmodium falciparum share a functionally equivalent host-cell-targeting motif (RxLR-dEER in P. infestans and RxLxE/D/Q in P. falciparum). Here we summarize recent studies that reveal that the malarial motif may function differently than previously envisioned. Binding of the lipid phosphatidylinositol 3-phosphate [PI(3)P] is a critical step in accessing the host for both pathogens, but occurs in different locations. Nanomolar affinity for PI(3)P by these short amino acid motifs suggests that a newly identified mechanism of phosphoinositide binding that unexpectedly occurs in secretory locations has been exploited for virulence by diverse eukaryotic pathogens.
dc.eprint.versionAuthor's manuscript
dc.identifier.citationJiang RH, Stahelin RV, Bhattacharjee S, Haldar K. Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface. Trends Microbiol. 2013;21(3):145-156. doi:10.1016/j.tim.2012.12.004
dc.identifier.urihttps://hdl.handle.net/1805/48375
dc.language.isoen_US
dc.publisherElsevier
dc.relation.isversionof10.1016/j.tim.2012.12.004
dc.relation.journalTrends in Microbiology
dc.rightsPublisher Policy
dc.sourcePMC
dc.subjectMalaria
dc.subjectOomycetes
dc.subjectHost-targeting
dc.subjectPhosphoinositides
dc.subjectSecretion
dc.subjectPathogenesis
dc.titleEukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface
dc.typeArticle
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