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SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall in Streptococcus pyogenes

Rebecca J Edgar1, Jing Chen1, Sashi Kant2

  • 1Department of Molecular and Cellular Biochemistry, University of Kentucky Lexington, KY, USA.

Frontiers in Cellular and Infection Microbiology
|October 30, 2016
PubMed

Insights

The study reveals that SpyB, a protein from Streptococcus pyogenes, influences bacterial aggregation and cell wall structure. Heme binding appears to regulate SpyB activity, impacting its function in Group A Streptococcus infections.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Molecular Biology

Background:

  • Streptococcus pyogenes (Group A Streptococcus, GAS) causes diverse infections.
  • GAS cell wall structure involves peptidoglycan and decorated carbohydrates.
  • The spyBA operon encodes membrane proteins SpyB and SpyA.

Purpose of the Study:

  • To investigate the function of the SpyB protein in GAS.
  • To understand SpyB's role in bacterial physiology and pathogenesis.

Main Methods:

  • Phenotypic analysis of a spyB deletion mutant.
  • Cell wall glycosyl composition analysis.
  • Biochemical assays for protein-heme interactions.

Main Results:

  • spyB deletion resulted in increased bacterial aggregation.
  • Mutant strains showed reduced susceptibility to cephalosporins and PlyC.
  • Altered cell wall carbohydrate structure was observed in the mutant.
  • SpyB was found to associate with heme and protoporphyrin IX.
  • Heme binding induced SpyB dimerization via disulfide bond formation.

Conclusions:

  • SpyB plays a role in GAS aggregation and cell wall integrity.
  • SpyB's activity may be regulated by heme binding and dimerization.
Keywords:
ADP-ribosyltransferaseGroup A carbohydrateSpyASpyBStreptococcus pyogenescell wallheme

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