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Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial

Chen Chen1, Chen Yang2, Joseph T Barbieri2

  • 1Department of Microbiology and Immunology, Medical College of Wisconsin, Milwaukee, WI, 53226, USA. cchen0@mcw.edu.

Scientific Reports
|March 14, 2019
PubMed

Insights

Methicillin-resistant Staphylococcus aureus (MRSA) produces a toxin, SSL11, that stops neutrophils from moving by making them stick. This discovery offers a potential new way to fight MRSA infections.

Area of Science:

  • Microbiology
  • Immunology
  • Pathogen-Host Interactions

Background:

  • Methicillin-resistant Staphylococcus aureus (MRSA) is a significant pathogen causing diverse human infections.
  • Neutrophils are critical immune cells, acting as the primary defense against Staphylococcus aureus.
  • Understanding bacterial virulence factors that evade neutrophil responses is crucial for developing new therapies.

Purpose of the Study:

  • To investigate the effect of Staphylococcal Superantigen-Like protein 11 (SSL11) from MRSA on neutrophil function.
  • To elucidate the mechanism by which SSL11 impacts neutrophil motility and adhesion.
  • To identify potential therapeutic targets against MRSA infections based on SSL11's action.

Main Methods:

  • Utilized differentiated human neutrophil-like cells (dHL60) to study MRSA USA300_FPR3757.
  • Assessed the impact of SSL11 on neutrophil motility, adhesion, and oxidative burst.
  • Investigated the role of the glycan Sialyl Lewis X and glycosylation in SSL11 binding and function using pre-incubation and PNGase F treatment.

Main Results:

  • SSL11 induced motility arrest in dHL60 cells by promoting cell adhesion, effectively 'locking' them in an adhered state.
  • SSL11 did not trigger an oxidative burst in neutrophils.
  • SSL11 function was inhibited by Sialyl Lewis X, and its binding to dHL60 cells was abolished by de-glycosylation, indicating a glycan-mediated interaction.

Conclusions:

  • This study reveals SSL11 as a novel bacterial toxin that inhibits neutrophil motility by inducing adhesion.
  • The mechanism involves SSL11 interacting with specific glycans on the neutrophil surface, such as Sialyl Lewis X.
  • This finding presents a new potential target for therapeutic strategies against MRSA infections by interfering with SSL11's immune-evasive function.

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