ArticleJournal of bacteriology2022
The Protease SplB of Staphylococcus aureus Targets Host Complement Components and Inhibits Complement-Mediated Bacterial Opsonophagocytosis.
Article in Journal of bacteriology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 44 citations in OpenAlex.
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- Staphylococcal SplA and SplB Serine Protease Allelic Variants Exhibit Different Substrate Specificities.Chembiochem : a European journal of chemical biology · 2026Article
- Metal nanozyme sensors with different modes: biomedical applications and research advances.Frontiers in bioengineering and biotechnology · 2026Review
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- Genome-wide association analysis provides insights into the genomics and extracellular expression ofVirulence · 2025Article
- The grand escape - how pathogens outsmart the human complement system.Immunobiology · 2025Review
- Halogenated quinoline kill agent rapidly induces iron starvation ofMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2025Article
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- Linking Virulence and Iron Limitation Response inJournal of proteome research · 2025Article
- pTripleTREP - A vector for tightly controlled expression and purification of virulence factors in Staphylococcus aureus.Microbial cell factories · 2025Article
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- Identification of NovelInternational journal of molecular sciences · 2025Article
- Staphylococcal SplA and SplB serine proteases target ubiquitin(-like) specific proteases.AMB Express · 2025Article
- Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus aureus is an opportunistic pathogen that can cause life-threatening infections, particularly in immunocompromised individuals. The high-level virulence of S. aureus largely relies on its diverse and variable collection of virulence factors and immune evasion proteins, including the six serine protease-like proteins SplA to SplF. Spl proteins are expressed by most clinical isolates of S. aureus, but little is known about the molecular mechanisms by which these proteins modify the host's immune response for the benefit of the bacteria. Here, we identify SplB as a protease that inactivates central human complement proteins, i.e., C3, C4, and the activation fragments C3b and C4b, by preferentially cleaving their α-chains. SplB maintained its proteolytic activity in human serum, degrading C3 and C4. SplB further cleaved the components of the terminal complement pathway, C5, C6, C7, C8, and C9. In contrast, the important soluble human complement regulators factor H and C4b-binding protein (C4BP), as well as C1q, were left intact. Thereby, SplB reduced C3b-mediated opsonophagocytosis by human neutrophils as well as C5b-9 deposition on the bacterial surface. In conclusion, we identified the first physiological substrates of the S. aureus extracellular protease SplB. This enzyme inhibits all three complement pathways and blocks opsonophagocytosis. Thus, SplB can be considered a novel staphylococcal complement evasion protein.
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