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Structural insights into SraP-mediated Staphylococcus aureus adhesion to host cells.

Yi-Hu Yang1, Yong-Liang Jiang1, Juan Zhang1

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Staphylococcus aureus uses its SraP protein to bind host cells. Structural and functional studies reveal how SraP

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Area of Science:

  • Microbiology
  • Structural Biology
  • Host-Pathogen Interactions

Background:

  • Staphylococcus aureus causes severe human diseases.
  • SraP, a surface glycoprotein, is crucial for S. aureus pathogenesis, particularly in infective endocarditis.
  • The precise mechanism of SraP-host interaction remains largely unknown.

Purpose of the Study:

  • To determine the structure of the SraP binding region (BR).
  • To elucidate the functional role of SraP in S. aureus adhesion and invasion.
  • To provide insights into S. aureus host-pathogen interactions.

Main Methods:

  • X-ray crystallography (2.05 Å resolution) of SraP BR.
  • Small-angle X-ray scattering (SAXS).
  • Molecular dynamics (MD) simulations.
  • Structure-guided mutagenesis.

Main Results:

  • The SraP BR exhibits a four-module, rod-like structure.
  • The N-terminal module binds N-acetylneuraminic acid.
  • The C-terminal modules form a rigid stem, extending the N-terminal module.
  • SraP binding to sialylated receptors promotes bacterial adhesion and invasion.

Conclusions:

  • SraP possesses a unique modular structure enabling host cell interaction.
  • SraP-mediated binding to sialylated host receptors is a key mechanism for S. aureus pathogenesis.
  • This study provides critical structural and functional insights into S. aureus host-pathogen interactions.