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Crystal structure of the mucin-binding domain of Spr1345 from Streptococcus pneumoniae

Yang Du1, Yong-Xing He, Zhen-Yi Zhang

  • 1School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.

Journal of Structural Biology
|November 9, 2010
PubMed

Insights

Streptococcus pneumoniae

Area of Science:

  • Microbiology
  • Structural Biology
  • Pathogen-Host Interactions

Background:

  • Streptococcus pneumoniae surface protein Spr1345 (Mucin-Binding Protein, MucBP) mediates adherence and colonization.
  • MucBP comprises a mucin-binding domain (MucBD) and a proline-rich domain (PRD).
  • A sortase-cleaved mature form (MF171) anchors the protein to the bacterial cell wall.

Purpose of the Study:

  • To determine the crystal structure of the MucBP's mucin-binding domain (MucBD).
  • To investigate the mucin-binding capabilities of the MucBD.
  • To provide structural insights into pneumococcal adherence to host mucins.

Main Methods:

  • Purification and enrichment of MucBD on A549 lung carcinoma cells.
  • Crystallization of MucBD.
  • Structure determination using single-wavelength anomalous dispersion (SAD) phasing with iodine signals at 2.0Å resolution.

Main Results:

  • The MucBD alone exhibits significant in vitro mucin-binding affinity.
  • The crystal structure of MucBD reveals an immunoglobulin-like fold with a rod-like shape.
  • A conserved C-terminal region within MucBD is implicated in mucin recognition.

Conclusions:

  • The study provides the first structural characterization of a bacterial MucBD.
  • Structural insights elucidate mechanisms of pneumococcal-mucin interactions.
  • Findings may inform the development of novel vaccines and therapeutics against pneumococcal infections.

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