ReviewTrends in microbiology2013
Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface.
Review in Trends in microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Characterization of the First Secreted Sorting Nexin Identified in theInternational journal of molecular sciences · 2024Article
- In Silico Identification and Analysis of Proteins Containing the Phox Homology Phosphoinositide-Binding Domain in Kinetoplastea Protists: Evolutionary Conservation and Uniqueness of Phox-Homology-Domain-Containing Protein Architectures.International journal of molecular sciences · 2023Article
- The intracellular CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Key interplay between the co-opted sorting nexin-BAR proteins and PI3P phosphoinositide in the formation of the tombusvirus replicase.PLoS pathogens · 2020Article
- Recruitment of Vps34 PI3K and enrichment of PI3P phosphoinositide in the viral replication compartment is crucial for replication of a positive-strand RNA virus.PLoS pathogens · 2019Article
- Phylogenetic profiles of all membrane transport proteins of the malaria parasite highlight new drug targetsMicrobial cell (Graz, Austria) · 2016Article
- Protein export in malaria parasites: many membranes to cross.Current opinion in microbiology · 2013Review
Corrections and comments
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Authors and funding
4 authors.
Funding
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.
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Registered trials
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