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Streptococcus mutans Collagen-Binding Protein Cnm Is a Multifunctional Adhesin: A Structural Investigation.

Joshua L Mieher1, Norbert Schormann1, Ren Wu1

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Streptococcus mutans collagen-binding adhesin Cnm binds to both collagen and glycoprotein 340. Key residues Y176 and F192 are crucial for this dual binding, impacting virulence.

Keywords:
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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Collagen-binding adhesin (Cnm) is a virulence factor in Streptococcus mutans.
  • Cnm is found in specific S. mutans serotypes and is a cell wall-anchored surface adhesin.
  • It belongs to the LPXTG family of adhesins.

Purpose of the Study:

  • To determine the crystal structure of the N2 domain of S. mutans Cnm.
  • To model collagen binding to S. mutans Cnm.
  • To investigate the multifunctional binding properties of Cnm.

Main Methods:

  • Crystal structure determination of the Cnm N2 domain.
  • Homology modeling using Staphylococcus aureus Cna.
  • Protein-protein docking and competition assays.
  • Alanine substitution mutagenesis.

Main Results:

  • The crystal structure of the S. mutans Cnm N2 domain was determined.
  • Modeling identified conserved and divergent residues involved in collagen binding compared to Cna.
  • Cnm binds with high affinity to scavenger receptor cysteine-rich (SRCR) domains of glycoprotein 340 (Gp340).
  • Collagen and SRCR domains share a common binding site on Cnm.
  • Residues Y176 and F192 were confirmed as critical for binding to both collagen and Gp340.

Conclusions:

  • S. mutans Cnm exhibits multifunctional binding capabilities.
  • Collagen and Gp340 binding sites overlap on the Cnm N2 domain.
  • Key residues Y176 and F192 are essential for Cnm's interaction with both collagen and Gp340, highlighting their importance in S. mutans virulence.