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BMC microbiology2006; 6; 82; doi: 10.1186/1471-2180-6-82

Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi.

Abstract: Heme is a preferred iron source of bacterial pathogens. Streptococcus equi subspecies equi is a bacterial pathogen that causes strangles in horses. Whether S. equi has a heme acquisition transporter is unknown. Results: An S. equi genome database was blasted with the heme binding proteins Shp and HtsA of Streptococcus pyogenes, and found that S. equi has the homologue of Shp (designated SeShp) and HtsA (designated SeHtsA). Tag-free recombinant SeShp and SeHtsA and 6xHis-tagged SeHtsA (SeHtsAHis) were prepared and characterized. Purified holoSeShp and holoSeHtsA bind Fe(II)-protoporphyrin IX (heme) and Fe(III)-protoporphyrin IX (hemin) in a 1:1 stoichiometry, respectively, and are designated hemoSeShp and hemiSeHtsA. HemiSeShp and hemiSeHtsAHis can be reconstituted from apoSeShp and apoSeHtsAHis and hemin. HemoSeShp is stable in air and can be oxidized to hemiSeShp by ferricyanide. HemiSeHtsA can be reduced into hemoSeHtsA, which autoxidizes readily. HemoSeShp rapidly transfers its heme to apoSeHtsAHis. In addition, hemoSeShp can also transfer its heme to apoHtsA, and hemoShp is able to donate heme to apoSeHtsAHis. Conclusions: The primary structures, optical properties, oxidative stability, and in vitro heme transfer reaction of SeShp and SeHtsA are very similar to those of S. pyogenes Shp and HtsA. The data suggest that the putative cell surface protein SeShp and lipoprotein SeHtsA are part of the machinery to acquire heme in S. equi. The results also imply that the structure, function, and functional mechanism of the heme acquisition machinery are conserved in S. equi and S. pyogenes.
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Publication Date: 2006-09-28 PubMed ID: 17007644PubMed Central: PMC1592302DOI: 10.1186/1471-2180-6-82Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates the presence and nature of heme-binding proteins in the bacterial pathogen Streptococcus equi subspecies equi which cause infection in horses. The study identifies two proteins, designated SeShp and SeHtsA, which exhibit similar structure and function to those of Streptococcus pyogenes, suggesting that these proteins play a pivotal role in heme acquisition for S. equi.

Research Analysis

The article delves into the investigation of heme-binding proteins, which are vital for bacteria to acquire iron, in order to survive and propagate. The research focuses on one such bacteria, Streptococcus equi subspecies equi, that is known to infect horses.

  • An initial search in the S. equi genome database using Shp and HtsA, the heme binding proteins of Streptococcus pyogenes, revealed that S. equi also has similar proteins, which the researchers named SeShp and SeHtsA. After these proteins were identified, they were prepared and analyzed.
  • The study found that purified holoSeShp and holoSeHtsA can bind to Fe(II)-protoporphyrin IX (commonly called heme) and Fe(III)-protoporphyrin IX (known as hemin), respectively, in a 1:1 ratio. These proteins were referred to as hemoSeShp and hemiSeHtsA.
  • Further investigation using ferricyanide demonstrated that hemoSeShp is air-stable and can be oxidized to hemiSeShp. HemiSeHtsA, in contrast, can be reduced to hemoSeHtsA which oxidizes readily.
  • A key discovery was that hemoSeShp can quickly transfer its heme to the protein apoSeHtsAHis. Additionally, hemoSeShp was found to transfer its heme to both apoHtsA and apoSeHtsAHis, highlighting its potential role in heme transport and acquisition.

Conclusions of the Study

This research has expanded our understanding of the iron acquisition process in S. equi bacteria. The findings revealed that:

  • The primary structures, optical properties, oxidative stability, and in vitro heme transfer reaction of SeShp and SeHtsA are very similar to those of S. pyogenes Shp and HtsA.
  • These similarities suggest that the cell surface protein SeShp and lipoprotein SeHtsA are part of the machinery responsible for acquiring heme in S. equi. This indicates that these proteins play a crucial role in the survival and proliferation of the bacteria.
  • The study also implies that the structure, function, and operational mechanism of the heme acquisition machinery are preserved across both S. equi and S. pyogenes species, suggesting possibilities of a common bacterial strategy for iron acquisition.

All these insights could be crucial for the development of new treatments for infections caused by S. equi and other similar pathogens, by potentially targeting these heme-binding proteins.

Cite This Article

APA
Nygaard TK, Liu M, McClure MJ, Lei B. (2006). Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi. BMC Microbiol, 6, 82. https://doi.org/10.1186/1471-2180-6-82

Publication

BMC microbiology
ISSN: 1471-2180
NlmUniqueID: 100966981
Country: England
Language: English
Volume: 6
Pages: 82

Researcher Affiliations

Nygaard, Tyler K
  • Department of Veterinary Molecular Biology, Montana State University, Bozeman, Montana 59717, USA. draagynfly@hotmail.com
Liu, Mengyao
    McClure, Michael J
      Lei, Benfang

        MeSH Terms

        • Amino Acid Sequence
        • Bacterial Proteins / chemistry
        • Bacterial Proteins / metabolism
        • Carrier Proteins / chemistry
        • Carrier Proteins / metabolism
        • Gene Expression Regulation, Bacterial
        • Genome, Bacterial
        • Heme / metabolism
        • Heme-Binding Proteins
        • Hemeproteins / chemistry
        • Hemeproteins / metabolism
        • Molecular Sequence Data
        • Protein Binding
        • Streptococcus equi / classification
        • Streptococcus equi / metabolism

        Grant Funding

        • K22 AI057347 / NIAID NIH HHS
        • P20 RR-020185 / NCRR NIH HHS
        • P20 RR020185-020002 / NCRR NIH HHS
        • P20 RR020185-010002 / NCRR NIH HHS
        • K22 AI057347-01 / NIAID NIH HHS
        • K22 AI057347-02 / NIAID NIH HHS
        • P20 RR020185 / NCRR NIH HHS

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