Format

Send to

Choose Destination

Links from Structure

J Biol Chem. 2011 Nov 4;286(44):38439-47. doi: 10.1074/jbc.M111.287300. Epub 2011 Sep 14.

Structural basis for hemoglobin capture by Staphylococcus aureus cell-surface protein, IsdH.

Author information

1
School of Molecular Bioscience, University of Sydney, New South Wales 2006, Australia.

Abstract

Pathogens must steal iron from their hosts to establish infection. In mammals, hemoglobin (Hb) represents the largest reservoir of iron, and pathogens express Hb-binding proteins to access this source. Here, we show how one of the commonest and most significant human pathogens, Staphylococcus aureus, captures Hb as the first step of an iron-scavenging pathway. The x-ray crystal structure of Hb bound to a domain from the Isd (iron-regulated surface determinant) protein, IsdH, is the first structure of a Hb capture complex to be determined. Surface mutations in Hb that reduce binding to the Hb-receptor limit the capacity of S. aureus to utilize Hb as an iron source, suggesting that Hb sequence is a factor in host susceptibility to infection. The demonstration that pathogens make highly specific recognition complexes with Hb raises the possibility of developing inhibitors of Hb binding as antibacterial agents.

PMID:
21917915
PMCID:
PMC3207429
DOI:
10.1074/jbc.M111.287300
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center