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The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor

Christian Linke1, Tom T Caradoc-Davies, Paul G Young

  • 1School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand.

Journal of Bacteriology
|July 21, 2009
PubMed

Insights

Streptococcus pyogenes uses the laminin-binding protein (Lbp) for adhesion. This study reveals Lbp is a zinc-binding protein, suggesting zinc mediates its interaction with host laminin.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • * Streptococcus pyogenes is a common pathogen that colonizes human skin and tonsils.
  • * Pathogenicity involves adhesion to host receptors via adhesins, such as the proposed laminin-binding protein (Lbp).
  • * Lbp's sequence suggests a link to bacterial metal-binding receptors.

Purpose of the Study:

  • * To elucidate the structural role of Lbp in Streptococcus pyogenes.
  • * To investigate Lbp's interaction with human laminin and its potential role in pathogenicity.
  • * To determine if Lbp functions as a metal-binding receptor.

Main Methods:

  • * Crystallization of Lbp and X-ray crystallography to determine its 3D structure.
  • * In vitro binding assays to assess Lbp's interaction with laminin.
  • * Localization studies using Lbp-specific antibodies.

Main Results:

  • * The crystal structure of Lbp was solved at 2.45 A resolution, revealing a typical metal-binding receptor fold.
  • * Lbp possesses a metal-binding site containing a zinc ion.
  • * In vitro studies confirmed a specific interaction between Lbp and laminin.
  • * Localization studies indicated Lbp is membrane-associated.

Conclusions:

  • * Lbp is primarily a zinc-binding protein, not solely a laminin adhesin.
  • * The interaction between Lbp and laminin in vivo may be facilitated by zinc bound to laminin.
  • * Understanding Lbp's function provides insights into Streptococcus pyogenes pathogenicity.

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