ArticleJournal of bacteriology2010
Functional characterization of a phospholipase A(2) homolog from Rickettsia typhi.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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
39 citing papers in PubMed, 62 citations in OpenAlex.
- Innate immune responses to Rickettsia: emerging themes and contrasts between species.Current opinion in microbiology · 2026Review
- The host calcium system contributes to intracellularInfection and immunity · 2025Article
- Phosphatidylserine-binding receptor, CD300f, on macrophages mediates host invasion of pathogenic and non-pathogenic rickettsiae.Infection and immunity · 2025Article
- Pathogenic rickettsiae encode a secreted lipase that facilitates intracytosolic colonization in host cells.PloS one · 2025Article
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- Pathogenicity and virulence ofVirulence · 2023Review
- Metagenome diversity illuminates origins of pathogen effectors.bioRxiv : the preprint server for biology · 2023Article
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- Pathogenicity and virulence ofVirulence · 2022Review
- Involvement of Pore Formation and Osmotic Lysis in the Rapid Killing of Gamma Interferon-Pretreated C166 Endothelial Cells byTropical medicine and infectious disease · 2022Article
- A patatin-like phospholipase mediates Rickettsia parkeri escape from host membranes.Nature communications · 2022Article
- Widespread phages of endosymbionts: Phage WO genomics and the proposed taxonomic classification of Symbioviridae.PLoS genetics · 2022Article
- Rickettsia conorii survival in THP-1 macrophages involves host lipid droplet alterations and active rickettsial protein production.Cellular microbiology · 2021Article
- The enigmatic biology of rickettsiae: recent advances, open questions and outlook.Pathogens and disease · 2021Review
- Rickettsia-host interaction: strategies of intracytosolic host colonization.Pathogens and disease · 2021Review
- Pathogenic, but Not Nonpathogenic,mBio · 2021Article
- Modulation of Host Lipid Pathways by Pathogenic Intracellular Bacteria.Pathogens (Basel, Switzerland) · 2020Review
- Risk1, a Phosphatidylinositol 3-Kinase Effector, Promotes Rickettsia typhi Intracellular Survival.mBio · 2020Article
- Rv3091, An Extracellular Patatin-Like Phospholipase inFrontiers in microbiology · 2020Article
- Antimicrobial Resistance inMicrobiology spectrum · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Phospholipase A(2) (PLA(2)) has long been proposed to be involved in rickettsial entry into host cells, escape from the phagosome to evade destruction by lysosomal exposure, and lysis of the host cells. However, the corresponding rickettsial gene(s) encoding a protein with PLA(2) activity has not been identified or functionally characterized. Here, we report that the Rickettsia typhi genome possesses two genes encoding patatin-like PLA(2) proteins, RT0590 and RT0522. Sequence analysis of RT0522 and RT0590 reveals the presence of the conserved motifs essential for PLA(2) activity. Transcriptional analysis indicates that RT0522, but not RT0590, is transcribed at all stages of intracellular growth of R. typhi in Vero cells. The differential gene expression pattern of RT0522 at various stages of growth suggests its potential role during R. typhi infection of host cells. In silico, RT0522 is predicted to be noncytoplasmic and its gene does not encode a recognizable signal peptide sequence. However, our data indicate that RT0522 is secreted into the host cytoplasm. In addition, we observe that RT0522 protein expression is cytotoxic to both yeast and Vero cells. Importantly, we demonstrate that recombinant RT0522 possesses phospholipase A activity that requires a eukaryotic host cofactor for activation. Both cytotoxicity and phospholipase A activity associated with RT0522 were reduced by PLA(2) inhibitors. Site-directed mutagenesis of predicted catalytic Ser/Asp residues of RT0522 also eliminates cytotoxicity and phospholipase A activity. To our knowledge, RT0522 is the first protein identified from Rickettsia typhi with functional phospholipase A activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.