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

Souvik Bhattacharjee, Robert Stahelin, Kasturi Haldar

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)555-562
Number of pages8
JournalTrends in Parasitology
Volume28
Issue number12
DOIs
StatePublished - Dec 2012

Fingerprint

Phosphatidylinositols
Malaria
Virulence
Parasites
Endoplasmic Reticulum
Erythrocytes
Lipids
phosphatidylinositol 3-phosphate
Proteins

Keywords

  • Blood cells
  • Endoplasmic reticulum
  • Export
  • Host targeting
  • Malaria
  • Pathogenic secretion
  • Phosphoinositides

ASJC Scopus subject areas

  • Infectious Diseases
  • Parasitology

Cite this

Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites. / Bhattacharjee, Souvik; Stahelin, Robert; Haldar, Kasturi.

In: Trends in Parasitology, Vol. 28, No. 12, 12.2012, p. 555-562.

Research output: Contribution to journalArticle

@article{c37275c0ccc447efad1fbb9969d05fa0,
title = "Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites",
abstract = "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.",
keywords = "Blood cells, Endoplasmic reticulum, Export, Host targeting, Malaria, Pathogenic secretion, Phosphoinositides",
author = "Souvik Bhattacharjee and Robert Stahelin and Kasturi Haldar",
year = "2012",
month = "12",
doi = "10.1016/j.pt.2012.09.004",
language = "English",
volume = "28",
pages = "555--562",
journal = "Trends in Parasitology",
issn = "1471-4922",
publisher = "Elsevier Limited",
number = "12",

}

TY - JOUR

T1 - Host targeting of virulence determinants and phosphoinositides in blood stage malaria parasites

AU - Bhattacharjee, Souvik

AU - Stahelin, Robert

AU - Haldar, Kasturi

PY - 2012/12

Y1 - 2012/12

N2 - 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.

AB - 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.

KW - Blood cells

KW - Endoplasmic reticulum

KW - Export

KW - Host targeting

KW - Malaria

KW - Pathogenic secretion

KW - Phosphoinositides

UR - http://www.scopus.com/inward/record.url?scp=84869183087&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84869183087&partnerID=8YFLogxK

U2 - 10.1016/j.pt.2012.09.004

DO - 10.1016/j.pt.2012.09.004

M3 - Article

C2 - 23084821

AN - SCOPUS:84869183087

VL - 28

SP - 555

EP - 562

JO - Trends in Parasitology

JF - Trends in Parasitology

SN - 1471-4922

IS - 12

ER -