ArticleNucleic acids research2012
The structural characterization of a prophage-encoded extracellular DNase from Streptococcus pyogenes.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular determinants of pathogenicity in a Streptococcus equi subsp. zooepidemicus strain from wild boar in Russia.Molecular genetics and genomics : MGG · 2026Article
- Review
- Nosocomial Transmission of Necrotizing Fasciitis: A Molecular Characterization of Group A Streptococcal DNases in Clinical Virulence.Microorganisms · 2024Article
- Article
- Pathogen-Derived Nucleases: An Effective Weapon for Escaping Extracellular Traps.Frontiers in immunology · 2022Review
- Virulence factors ofFrontiers in microbiology · 2022Review
- Article
- Interactions of Bacteriophages with Animal and Human Organisms-Safety Issues in the Light of Phage Therapy.International journal of molecular sciences · 2021Review
- Prophage exotoxins enhance colonization fitness in epidemic scarlet fever-causing Streptococcus pyogenes.Nature communications · 2020Article
- Crystal structure of NucB, a biofilm-degrading endonuclease.Nucleic acids research · 2018Article
- Systematic classification of the His-Me finger superfamily.Nucleic acids research · 2017Article
- Structural characterization of the virulence factor Sda1 nuclease from Streptococcus pyogenes.Nucleic acids research · 2016Article
- Structural characterization of the virulence factor nuclease A from Streptococcus agalactiae.Acta crystallographica. Section D, Biological crystallography · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The pathogenic bacterium Group A Streptococcus pyogenes produces several extracellular DNases that have been shown to facilitate invasive infection by evading the human host immune system. DNases degrade the chromatin in neutrophil extracellular traps, enabling the bacterium to evade neutrophil capture. Spd1 is a type I, nonspecific ββα/metal-dependent nuclease from Streptococcus pyogenes, which is encoded by the SF370.1 prophage and is likely to be expressed as a result of prophage induction. We present here the X-ray structure of this DNase in the wild-type and Asn145Ala mutant form. Through structural and sequence alignments as well as mutagenesis studies, we have identified the key residues His121, Asn145 and Glu164, which are crucial for Spd1 nucleolytic activity and shown the active site constellation. Our wild-type structure alludes to the possibility of a catalytically blocked dimeric form of the protein. We have investigated the multimeric nature of Spd1 using size-exclusion chromatography with multi-angle light scattering (SEC-MALLS) in the presence and absence of the divalent metal ion Mg(2+), which suggests that Spd1 exists in a monomeric form in solution.
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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.