ArticleScientific reports2019
Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial toxin action.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Immune evasion of multidrug-resistant bacteria: insights from lung innate immune cells and targeted therapies.Frontiers in cellular and infection microbiology · 2026Review
- Taming Bacterial Toxins into an Anticancer Platform.Biochemical and biophysical research communications · 2025Article
- Bacterial single-cell RNA sequencing captures biofilm transcriptional heterogeneity and differential responses to immune pressure.Nature communications · 2024Article
- Article
- Article
- Adaptive laboratory evolution and independent component analysis disentangle complex vancomycin adaptation trajectories.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- StaphylococcalInternational journal of molecular sciences · 2022Article
- Multiple Domains of Staphylococcal Superantigen-like Protein 11 (SSL11) Contribute to Neutrophil Inhibition.Biochemistry · 2022Article
- Mitofusin-2 regulates leukocyte adhesion and β2 integrin activation.Journal of leukocyte biology · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Methicillin resistant Staphylococcus aureus (MRSA) is a major human pathogen, which causes superficial to lethal clinical infections. Neutrophils are the most abundant leukocytes in the blood and are the first defense mechanism against S. aureus infections. Here we show Staphylococcal Superantigen-Like protein 11 (SSL11) from MRSA USA300_FPR3757 mediated differentiated human neutrophil-like cells (dHL60) motility arrest by inducing cell adhesion and "locking" cells in adhesion stage, without inducing oxidative burst. Pre-incubation of SSL11 with the glycan Sialyl Lewis X blocked SSL11 function and de-glycosylation of dHL60 cells by PNGase F abolished SSL11 binding, suggesting that SSL11 functions via interacting with glycans. This is the first description of a bacterial toxin inhibiting neutrophil motility by inducing adhesion and "locking" cells in an adhesion stage. Therefore, this study might provide a new target against S. aureus infections.
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