ArticleThe Journal of biological chemistry2016
The Salmonella Effector SpvD Is a Cysteine Hydrolase with a Serovar-specific Polymorphism Influencing Catalytic Activity, Suppression of Immune Responses, and Bacterial Virulence.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- The Manipulation of Host Cells byInternational journal of molecular sciences · 2026Review
- Salmonella multimutants enable efficient identification of SPI-2 effector protein function in gut inflammation and systemic colonization.Nature communications · 2025Article
- Single-cell analysis of genetically minimized Salmonella reveals effector gene cooperation in vivo.Nature microbiology · 2025Article
- Review
- Artesunate, EDTA, and colistin work synergistically against MCR-negative and -positive colistin-resistanteLife · 2025Article
- Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity.Cell host & microbe · 2024Article
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- Population structure and ongoing microevolution of the emerging multidrug-resistant Salmonella Typhimurium ST213.npj antimicrobials and resistance · 2024Article
- Transcriptomic analysis using RNA sequencing and phenotypic analysis ofFrontiers in microbiology · 2024Article
- A novel approach for detectingFrontiers in microbiology · 2024Article
- Article
- Review
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Genomic Characterization and Genetic Profiles ofGenes · 2023Article
- The LysR-Type Transcription Regulator YhjC Promotes the Systemic Infection of Salmonella Typhimurium in Mice.International journal of molecular sciences · 2023Article
- The emerging role and therapeutic implications of bacterial and parasitic deubiquitinating enzymes.Frontiers in immunology · 2023Review
- Host manipulation by bacterial type III and type IV secretion system effector proteases.Cellular microbiology · 2021Review
- Systematic reconstruction of an effector-gene network reveals determinants of Salmonella cellular and tissue tropism.Cell host & microbe · 2021Article
- Phylogeny ofMicrobial genomics · 2021Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Many bacterial pathogens secrete virulence (effector) proteins that interfere with immune signaling in their host. SpvD is a Salmonella enterica effector protein that we previously demonstrated to negatively regulate the NF-κB signaling pathway and promote virulence of S. enterica serovar Typhimurium in mice. To shed light on the mechanistic basis for these observations, we determined the crystal structure of SpvD and show that it adopts a papain-like fold with a characteristic cysteine-histidine-aspartate catalytic triad comprising Cys-73, His-162, and Asp-182. SpvD possessed an in vitro deconjugative activity on aminoluciferin-linked peptide and protein substrates in vitro A C73A mutation abolished SpvD activity, demonstrating that an intact catalytic triad is required for its function. Taken together, these results strongly suggest that SpvD is a cysteine protease. The amino acid sequence of SpvD is highly conserved across different S. enterica serovars, but residue 161, located close to the catalytic triad, is variable, with serovar Typhimurium SpvD having an arginine and serovar Enteritidis a glycine at this position. This variation affected hydrolytic activity of the enzyme on artificial substrates and can be explained by substrate accessibility to the active site. Interestingly, the SpvD
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