PhytophthoraV1, Main, Exploration, bibRecord, 001330

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

Identifieur interne : 001330 ( Main/Exploration ); précédent : 001329; suivant : 001331

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

Auteurs : Rays H Y. Jiang [États-Unis] ; Robert V. Stahelin ; Souvik Bhattacharjee ; Kasturi Haldar

Source :

Trends in microbiology [ 1878-4380 ] ; 2013.

RBID : pubmed:23375057

Descripteurs français

KwdFr :
- Facteurs de virulence (métabolisme), Humains (MeSH), Interactions hôte-pathogène (MeSH), Liaison aux protéines (MeSH), Membrane cellulaire (composition chimique), Motifs d'acides aminés (MeSH), Phosphatidyl inositols (métabolisme), Phytophthora infestans (pathogénicité), Plantes (MeSH), Plasmodium falciparum (pathogénicité), Réticulum endoplasmique (composition chimique).
MESH :
- composition chimique : Membrane cellulaire, Réticulum endoplasmique.
- métabolisme : Facteurs de virulence, Phosphatidyl inositols.
- pathogénicité : Phytophthora infestans, Plasmodium falciparum.
- Humains, Interactions hôte-pathogène, Liaison aux protéines, Motifs d'acides aminés, Plantes.

English descriptors

KwdEn :
- Amino Acid Motifs (MeSH), Cell Membrane (chemistry), Endoplasmic Reticulum (chemistry), Host-Pathogen Interactions (MeSH), Humans (MeSH), Phosphatidylinositols (metabolism), Phytophthora infestans (pathogenicity), Plants (MeSH), Plasmodium falciparum (pathogenicity), Protein Binding (MeSH), Virulence Factors (metabolism).
MESH :
- chemical , metabolism : Phosphatidylinositols, Virulence Factors.
- chemistry : Cell Membrane, Endoplasmic Reticulum.
- pathogenicity : Phytophthora infestans, Plasmodium falciparum.
- Amino Acid Motifs, Host-Pathogen Interactions, Humans, Plants, Protein Binding.

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.

DOI: 10.1016/j.tim.2012.12.004
PubMed: 23375057
PubMed Central: PMC3595378

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001347
to stream Main, to step Curation: 001347

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface.

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

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