Diverse structural approaches to haem appropriation by pathogenic bacteria

Biochim Biophys Acta Proteins Proteom. 2017 Apr;1865(4):422-433. doi: 10.1016/j.bbapap.2017.01.006. Epub 2017 Jan 24.

Abstract

The critical need for iron presents a challenge for pathogenic bacteria that must survive in an environment bereft of accessible iron due to a natural low bioavailability and their host's nutritional immunity. Appropriating haem, either direct from host haemoproteins or by secreting haem-scavenging haemophores, is one way pathogenic bacteria can overcome this challenge. After capturing their target, haem appropriation systems must remove haem from a high-affinity binding site (on the host haemoprotein or bacterial haemophore) and transfer it to a binding site of lower affinity on a bacterial receptor. Structural information is now available to show how, using a combination of induced structural changes and steric clashes, bacteria are able to extract haem from haemophores, haemopexin and haemoglobin. This review focuses on structural descriptions of these bacterial haem acquisition systems, summarising how they bind haem and their target haemoproteins with particularly emphasis on the mechanism of haem extraction.

Keywords: Bacteria; Heme; Hemoprotein; Host-pathogen interaction; Iron; Nutritional immunity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Bacteria* / genetics
  • Bacteria* / metabolism
  • Bacteria* / pathogenicity
  • Bacterial Infections* / genetics
  • Bacterial Infections* / metabolism
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Heme / metabolism*
  • Humans

Substances

  • Bacterial Proteins
  • Heme