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

Staphylococcus aureus Growth using Human Hemoglobin as an Iron Source

Published on: February 7, 2013

Heme coordination by Staphylococcus aureus IsdE.

Jason C Grigg1, Christie L Vermeiren2, David E Heinrichs2

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

The Journal of Biological Chemistry
|August 2, 2007
PubMed
Summary

Staphylococcus aureus acquires iron from heme using the Isd system. Researchers determined the crystal structure of IsdE bound to heme, revealing its unique iron binding mechanism essential for bacterial growth.

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Staphylococcus aureus is a major cause of hospital-acquired infections.
  • S. aureus requires host iron for growth, with heme iron being a primary source.
  • The iron-regulated surface determinant (Isd) system facilitates heme uptake in S. aureus.

Purpose of the Study:

  • To elucidate the structural basis of heme binding and transport by the IsdE lipoprotein.
  • To understand the role of specific residues in heme interaction and bacterial iron acquisition.

Main Methods:

  • X-ray crystallography to determine the structure of soluble IsdE in complex with heme.
  • Biochemical assays measuring S. aureus growth on heme as an iron source.
  • Multiple sequence alignments of IsdE homologues.

Main Results:

  • The crystal structure of IsdE revealed a bi-lobed structure with heme bound at the domain interface.
  • Heme iron is coordinated by methionine and histidine residues in a novel manner for heme transporters.
  • Histidine 229 was identified as crucial for heme uptake and bacterial growth.

Conclusions:

  • IsdE belongs to the helical backbone metal receptor superfamily.
  • The determined structure provides insights into the mechanism of heme transport by Gram-positive bacteria.
  • Conserved residues suggest similar heme binding and transport mechanisms in related pathogens.