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Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source
06:37

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Published on: February 7, 2013

Haem recognition by a Staphylococcus aureus NEAT domain.

Jason C Grigg1, Christie L Vermeiren, David E Heinrichs

  • 1Department of Microbiology and Immunology, Life Sciences Institute, The University of British Columbia, Vancouver, BC, Canada V6T 1Z3.

Molecular Microbiology
|January 19, 2007
PubMed
Summary

Staphylococcus aureus uses the NEAT domain protein IsdA to bind and utilize host haem-iron for growth. Structural analysis reveals IsdA

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Pathogenic bacteria require iron, often sourced from host haem-iron under iron-restricted conditions.
  • NEAT (NEAr Transporter) domains are cell surface proteins in Gram-positive bacteria involved in nutrient acquisition.
  • IsdA is a NEAT domain protein in Staphylococcus aureus implicated in haem binding.

Purpose of the Study:

  • To investigate the role of IsdA in Staphylococcus aureus growth using haem as an iron source.
  • To characterize the structural basis of haem binding by the IsdA NEAT domain.

Main Methods:

  • Overexpression and mutation of IsdA in Staphylococcus aureus.
  • Growth assays in media with haem as the sole iron source.
  • X-ray crystallography to determine the structure of the IsdA NEAT domain with and without haem.

Main Results:

  • IsdA overexpression enhanced S. aureus growth on haem, while its inactivation caused a growth defect.
  • The NEAT domain alone possesses haem-binding capability.
  • Structural data revealed a beta-sandwich fold with a hydrophobic pocket; haem iron is coordinated by Tyr166.
  • Conserved Tyr166 is a key residue for NEAT domain haem binding.

Conclusions:

  • IsdA is crucial for Staphylococcus aureus to utilize haem-iron for growth.
  • The IsdA NEAT domain employs a specific structural mechanism for haem binding and iron acquisition.
  • Understanding NEAT domain function provides insights into bacterial iron scavenging strategies.