ArticleGut microbes2019
Caspase-3 cleavage of Salmonella type III secreted effector protein SifA is required for localization of functional domains and bacterial dissemination.
Article in Gut microbes, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 19 citations in OpenAlex.
- The Co-Evolutionary Arms Race BetweenMicroorganisms · 2026Review
- Salmonella effector kinase SteC is activated by phosphorylation at Serine 379.PLoS pathogens · 2026Article
- Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
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- Executioner caspases degrade essential mediators of pathogen-host interactions to inhibit growth of intracellular Listeria monocytogenes.Cell death & disease · 2025Article
- Unveiling the Potential Ways to Apply Citrus Oil to Control Causative Agents of Pullorum Disease and Fowl Typhoid in Floor Materials.Animals : an open access journal from MDPI · 2023Article
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
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- Evolutionary Diversity and Function of Metacaspases in Plants: Similar to but Not Caspases.International journal of molecular sciences · 2022Review
- Cross-Talk Between the Intestinal Epithelium andFrontiers in microbiology · 2022Review
- Manipulation of Host Cell Organelles by Intracellular Pathogens.International journal of molecular sciences · 2021Review
- The vacuole guard hypothesis: how intravacuolar pathogens fight to maintain the integrity of their beloved home.Current opinion in microbiology · 2020Review
- Article
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
SifA is a bi-functional Type III Secretion System (T3SS) effector protein that plays an important role in Salmonella virulence. The N-terminal domain of SifA binds SifA-Kinesin-Interacting-Protein (SKIP), and via an interaction with kinesin, forms tubular membrane extensions called Sif filaments (Sifs) that emanate from the Salmonella Containing Vacuole (SCV). The C-terminal domain of SifA harbors a WxxxE motif that functions to mimic active host cell GTPases. Taken together, SifA functions in inducing endosomal tubulation in order to maintain the integrity of the SCV and promote bacterial dissemination. Since SifA performs multiple, unrelated functions, the objective of this study was to determine how each functional domain of SifA becomes processed. Our work demonstrates that a linker region containing a caspase-3 cleavage motif separates the two functional domains of SifA. To test the hypothesis that processing of SifA by caspase-3 at this particular site is required for function and proper localization of the effector protein domains, we developed two tracking methods to analyze the intracellular localization of SifA. We first adapted a fluorescent tag called phiLOV that allowed for type-III secretion system (T3SS) mediated delivery of SifA and observation of its intracellular colocalization with caspase-3. Additionally, we created a dual-tagging strategy that permitted tracking of each of the SifA functional domains following caspase-3 cleavage to different subcellular locations. The results of this study reveal that caspase-3 cleavage of SifA is required for the proper localization of functional domains and bacterial dissemination. Considering the importance of these events in Salmonella pathogenesis, we conclude that caspase-3 cleavage of effector proteins is a more broadly applicable effector processing mechanism utilized by Salmonella to invade and persist during infection.
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Registered trials
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