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

Publication Type:
Journal Article
Citation:
Journal of Biological Chemistry, 2011, 286 (44), pp. 38439 - 38447
Issue Date:
2011-11-04
Full metadata record
Files in This Item:
Filename Description Size
J. Biol. Chem.-2011-Krishna Kumar-38439-47.pdfPublished Version2.59 MB
Adobe PDF
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. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
Please use this identifier to cite or link to this item: