ArticleScientific reports2016
Staphylokinase has distinct modes of interaction with antimicrobial peptides, modulating its plasminogen-activation properties.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- Whole genome investigation of multi-drug resistant Staphylococcus aureus strain.World journal of microbiology & biotechnology · 2026Article
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- Overview of Venous Thromboembolism and Emerging Therapeutic Technologies Based on Nanocarriers-Mediated Drug Delivery Systems.Molecules (Basel, Switzerland) · 2024Review
- The effects of stress on gut virome: Implications on infectious disease and systemic disorders.MicrobiologyOpen · 2024Review
- Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review.Microorganisms · 2024Review
- Fibrin and Fibrinolytic Enzyme Cascade in Thrombosis: Unravelling the Role.Life (Basel, Switzerland) · 2023Review
- Gut Virome: Role and Distribution in Health and Gastrointestinal Diseases.Frontiers in cellular and infection microbiology · 2022Review
- Prophages encoding human immune evasion cluster genes are enriched inMicrobial genomics · 2021Article
- Genomic epidemiology of methicillin-resistant and -susceptible Staphylococcus aureus from bloodstream infections.BMC infectious diseases · 2021Article
- Interplay between ESKAPE Pathogens and Immunity in Skin Infections: An Overview of the Major Determinants of Virulence and Antibiotic Resistance.Pathogens (Basel, Switzerland) · 2021Review
- Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen.Frontiers in cellular and infection microbiology · 2021Article
- Interaction of host and Staphylococcus aureus protease-system regulates virulence and pathogenicity.Medical microbiology and immunology · 2019Review
- Unstable chromosome rearrangements inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019Article
- After the deluge: mining Staphylococcus aureus genomic data for clinical associations and host-pathogen interactions.Current opinion in microbiology · 2018Review
- Structure-based antigenic epitope and PEGylation improve the efficacy of staphylokinase.Microbial cell factories · 2017Article
- Targeting and inactivation of bacterial toxins by human defensins.Biological chemistry · 2017Review
- Staphylococcus sciuri bacteriophages double-convert for staphylokinase and phospholipase, mediate interspecies plasmid transduction, and package mecA gene.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Staphylokinase (Sak) is a plasminogen activator protein that is secreted by many Staphylococcus aureus strains. Sak also offers protection by binding and inhibiting specific antimicrobial peptides (AMPs). Here, we evaluate Sak as a more general interaction partner for AMPs. Studies with melittin, mCRAMP, tritrpticin and bovine lactoferricin indicate that the truncation of the first ten residues of Sak (SakΔN10), which occurs in vivo and uncovers important residues in a bulge region, improves its affinity for AMPs. Melittin and mCRAMP have a lower affinity for SakΔN10, and in docking studies, they bind to the N-terminal segment and bulge region of SakΔN10. By comparison, lactoferricin and tritrpticin form moderately high affinity 1:1 complexes with SakΔN10 and their cationic residues form several electrostatic interactions with the protein's α-helix. Overall, our work identifies two distinct AMP binding surfaces on SakΔN10 whose occupation would lead to either inhibition or promotion of its plasminogen activating properties.
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