Identification and characterization of the heme-binding proteins SeShp and SeHtsA of Streptococcus equi subspecies equi
2006

Study of Heme-Binding Proteins in Streptococcus equi

publication Evidence: moderate

Author Information

Author(s): Nygaard Tyler K, Liu Mengyao, McClure Michael J, Lei Benfang

Primary Institution: Montana State University

Hypothesis

Does Streptococcus equi have a heme acquisition transporter similar to that of Streptococcus pyogenes?

Conclusion

The study found that SeShp and SeHtsA in Streptococcus equi are heme-binding proteins that function similarly to their counterparts in Streptococcus pyogenes.

Supporting Evidence

  • SeShp and SeHtsA were found to bind heme in a 1:1 stoichiometry.
  • The primary structures of SeShp and SeHtsA are highly conserved compared to those of S. pyogenes.
  • HemoSeShp can rapidly transfer its heme to apoSeHtsA.

Takeaway

Researchers discovered that a bacteria called Streptococcus equi has special proteins that help it grab iron from heme, just like another bacteria called Streptococcus pyogenes.

Methodology

The study involved preparing and characterizing recombinant proteins SeShp and SeHtsA, and analyzing their heme-binding properties through various assays.

Digital Object Identifier (DOI)

10.1186/1471-2180-6-82

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