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

Rays H Y Jiang, Robert Stahelin, Souvik Bhattacharjee, Kasturi Haldar

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Similar 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.

Original languageEnglish
Pages (from-to)145-156
Number of pages12
JournalTrends in Microbiology
Volume21
Issue number3
DOIs
StatePublished - Mar 2013

Fingerprint

Phytophthora infestans
Phosphatidylinositols
Virulence
Oomycetes
Amino Acid Motifs
Falciparum Malaria
Plasmodium falciparum
Parasites
Bacteria
Lipids
Proteins
phosphatidylinositol 3-phosphate

Keywords

  • Host-targeting
  • Malaria
  • Oomycetes
  • Pathogenesis
  • Phosphoinositides
  • Secretion

ASJC Scopus subject areas

  • Infectious Diseases
  • Microbiology (medical)
  • Microbiology
  • Virology

Cite this

Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface. / Jiang, Rays H Y; Stahelin, Robert; Bhattacharjee, Souvik; Haldar, Kasturi.

In: Trends in Microbiology, Vol. 21, No. 3, 03.2013, p. 145-156.

Research output: Contribution to journalArticle

Jiang, Rays H Y ; Stahelin, Robert ; Bhattacharjee, Souvik ; Haldar, Kasturi. / Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface. In: Trends in Microbiology. 2013 ; Vol. 21, No. 3. pp. 145-156.
@article{59debbe50735495ba4273596b1ca192e,
title = "Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface",
abstract = "Similar 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.",
keywords = "Host-targeting, Malaria, Oomycetes, Pathogenesis, Phosphoinositides, Secretion",
author = "Jiang, {Rays H Y} and Robert Stahelin and Souvik Bhattacharjee and Kasturi Haldar",
year = "2013",
month = "3",
doi = "10.1016/j.tim.2012.12.004",
language = "English",
volume = "21",
pages = "145--156",
journal = "Trends in Microbiology",
issn = "0966-842X",
publisher = "Elsevier Limited",
number = "3",

}

TY - JOUR

T1 - Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface

AU - Jiang, Rays H Y

AU - Stahelin, Robert

AU - Bhattacharjee, Souvik

AU - Haldar, Kasturi

PY - 2013/3

Y1 - 2013/3

N2 - Similar 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.

AB - Similar 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.

KW - Host-targeting

KW - Malaria

KW - Oomycetes

KW - Pathogenesis

KW - Phosphoinositides

KW - Secretion

UR - http://www.scopus.com/inward/record.url?scp=84875254752&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84875254752&partnerID=8YFLogxK

U2 - 10.1016/j.tim.2012.12.004

DO - 10.1016/j.tim.2012.12.004

M3 - Article

C2 - 23375057

AN - SCOPUS:84875254752

VL - 21

SP - 145

EP - 156

JO - Trends in Microbiology

JF - Trends in Microbiology

SN - 0966-842X

IS - 3

ER -