ArticlePloS one2015
Interdomain Contacts and the Stability of Serralysin Protease from Serratia marcescens.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 28 citations in OpenAlex.
- Rare Earth Element-Induced Condensation of the Block V of the Repeats-in-Toxin Domain from CyaA fromLangmuir : the ACS journal of surfaces and colloids · 2025Article
- Review
- Evaluation of Immunostimulatory Effects of Bacterial Lysate Proteins on THP-1 Macrophages: Pro-inflammatory Cytokine Response and Proteomic Profiling.Journal of immunology research · 2025Article
- How do Gram-negative bacteria escape predation by Bdellovibrio bacteriovorus?npj antimicrobials and resistance · 2024Review
- An up-to-date review of biomedical applications of serratiopeptidase and its biobetter derivatives as a multi-potential metalloprotease.Archives of microbiology · 2024Review
- Serratia marcescens DUF1471-Containing Protein SrfN Is Needed for Adaptation to Acid and Oxidative Stresses.mSphere · 2022Article
- A serralysin-like protein ofFrontiers in microbiology · 2022Article
- Design, expression and functional assessment of novel engineered serratiopeptidase analogs with enhanced protease activity and thermal stability.World journal of microbiology & biotechnology · 2021Article
- Protein Surface Interactions-Theoretical and Experimental Studies.Frontiers in molecular biosciences · 2021Review
- Assessing the Genomic Variability of Gardnerella vaginalis through Comparative Genomic Analyses: Evolutionary and Ecological Implications.Applied and environmental microbiology · 2020Article
- Calcium-Dependent RTX Domains in the Development of Protein Hydrogels.Gels (Basel, Switzerland) · 2019Review
- Serralysin family metalloproteases protects Serratia marcescens from predation by the predatory bacteria Micavibrio aeruginosavorus.Scientific reports · 2018Article
- CpxR-Dependent Thermoregulation of Serratia marcescens PrtA Metalloprotease Expression and Its Contribution to Bacterial Biofilm Formation.Journal of bacteriology · 2018Article
- Draft Genome Sequence ofGenome announcements · 2017Article
- The Inhibitory Effect of C-phycocyanin Containing Protein Extract (C-PC Extract) on Human Matrix Metalloproteinases (MMP-2 and MMP-9) in Hepatocellular Cancer Cell Line (HepG2).The protein journal · 2017Article
- Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.Scientific reports · 2016Article
- Structure of a thermostable serralysin from Serratia sp. FS14 at 1.1 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2016Article
- SlpE is a calcium-dependent cytotoxic metalloprotease associated with clinical isolates of Serratia marcescens.Research in microbiologyArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The serralysin family of bacterial metalloproteases is associated with virulence in multiple modes of infection. These extracellular proteases are members of the Repeats-in-ToXin (RTX) family of toxins and virulence factors, which mediated virulence in E. coli, B. pertussis, and P. aeruginosa, as well as other animal and plant pathogens. The serralysin proteases are structurally dynamic and their folding is regulated by calcium binding to a C-terminal domain that defines the RTX family of proteins. Previous studies have suggested that interactions between N-terminal sequences and this C-terminal domain are important for the high thermal and chemical stabilities of the RTX proteases. Extending from this, stabilization of these interactions in the native structure may lead to hyperstabilization of the folded protein. To test this hypothesis, cysteine pairs were introduced into the N-terminal helix and the RTX domain and protease folding and activity were assessed. Under stringent pH and temperature conditions, the disulfide-bonded mutant showed increased protease activity and stability. This activity was dependent on the redox environment of the refolding reaction and could be blocked by selective modification of the cysteine residues before protease refolding. These data demonstrate that the thermal and chemical stability of these proteases is, in part, mediated by binding between the RTX domain and the N-terminal helix and demonstrate that stabilization of this interaction can further stabilize the active protease, leading to additional pH and thermal tolerance.
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