Jump to main content
Jump to site search

Issue 8, 2014
Previous Article Next Article

Proteomic analysis of putative heme-binding proteins in Streptococcus pyogenes

Author affiliations

Abstract

Streptococcus pyogenes is an important human bacterium with high pathogenicity. Heme is a major source of iron that plays a critical role in bacterial survival and virulence. In this study, heme-affinity chromatography, two-dimensional-electrophoresis and mass spectrometry were combined to identify putative heme-binding proteins and heme-regulatory proteins. In total, 68 heme-regulatory proteins and 284 putative heme-binding proteins were identified, among which 37 proteins showed expression alterations in response to heme deficiency. Bioinformatics analysis revealed that several key metabolic pathways had changed in the absence of heme, among which glycolysis was a major pathway impaired under heme-deficient conditions. New potential heme-binding proteins were successfully identified in this study providing novel clues for the study of the heme transport mechanism. Heme-binding proteins may play fundamental roles in many important biological pathways and thus contribute to bacterial pathogenicity.

Graphical abstract: Proteomic analysis of putative heme-binding proteins in Streptococcus pyogenes

Back to tab navigation

Supplementary files

Publication details

The article was received on 26 Jan 2014, accepted on 09 Apr 2014 and first published on 09 Apr 2014


Article type: Paper
DOI: 10.1039/C4MT00027G
Citation: Metallomics, 2014,6, 1451-1459
  •   Request permissions

    Proteomic analysis of putative heme-binding proteins in Streptococcus pyogenes

    N. Wang, J. Zhang, L. Zhang, X. Yang, N. Li, G. Yu, J. Han, K. Cao, Z. Guo, X. Sun and Q. He, Metallomics, 2014, 6, 1451
    DOI: 10.1039/C4MT00027G

Search articles by author

Spotlight

Advertisements