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Functional and Structural Properties of a Novel Protein and Virulence Factor (sHIP) in Streptococcus pyogenes.

Wisniewska, Magdalena; Happonen, Lotta LU ; Kahn, Fredrik LU ; Varjosalo, Markku; Malmström, Lars; Rosenberger, George; Karlsson, Christofer LU ; Cazzamali, Giuseppe; Pozdnyakova, Irina and Frick, Inga-Maria LU , et al. (2014) In Journal of Biological Chemistry 289(26). p.18175-18188
Abstract
Streptococcus pyogenes is a significant bacterial pathogen in the human population. The importance of virulence factors for the survival and colonization of S. pyogenes is well established, and many of these factors are exposed to the extracellular environment enabling bacterial interactions with the host. In the present study we quantitatively analyzed and compared S. pyogenes proteins in the growth medium of a strain that is virulent to mice, with a non-virulent strain. Particularly one of these proteins was present at significantly higher levels in stationary growth medium from the virulent strain. We determined the three-dimensional structure of the protein that showed a unique tetrameric organization composed of four helix-loop-helix... (More)
Streptococcus pyogenes is a significant bacterial pathogen in the human population. The importance of virulence factors for the survival and colonization of S. pyogenes is well established, and many of these factors are exposed to the extracellular environment enabling bacterial interactions with the host. In the present study we quantitatively analyzed and compared S. pyogenes proteins in the growth medium of a strain that is virulent to mice, with a non-virulent strain. Particularly one of these proteins was present at significantly higher levels in stationary growth medium from the virulent strain. We determined the three-dimensional structure of the protein that showed a unique tetrameric organization composed of four helix-loop-helix motifs. Affinity pull-down mass spectrometry analysis in human plasma demonstrated that the protein interacts with histidine-rich glycoprotein (HRG), and the name sHIP (streptococcal Histidine-rich glycoprotein Interacting Protein) is therefore proposed. HRG has antibacterial activity, and when challenged by HRG, sHIP was found to rescue S. pyogenes bacteria. This and the finding that patients with invasive S. pyogenes infection respond with antibody production against sHIP, suggest a role for the protein in S. pyogenes pathogenesis. (Less)
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published
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Journal of Biological Chemistry
volume
289
issue
26
pages
18175 - 18188
publisher
ASBMB
external identifiers
  • pmid:24825900
  • wos:000338042000020
  • scopus:84903543152
ISSN
1083-351X
DOI
10.1074/jbc.M114.565978
language
English
LU publication?
yes
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54192451-04c0-4b8a-9505-62d9fbf12b86 (old id 4455262)
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http://www.ncbi.nlm.nih.gov/pubmed/24825900?dopt=Abstract
date added to LUP
2014-06-04 20:08:38
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2017-03-26 03:11:25
@article{54192451-04c0-4b8a-9505-62d9fbf12b86,
  abstract     = {Streptococcus pyogenes is a significant bacterial pathogen in the human population. The importance of virulence factors for the survival and colonization of S. pyogenes is well established, and many of these factors are exposed to the extracellular environment enabling bacterial interactions with the host. In the present study we quantitatively analyzed and compared S. pyogenes proteins in the growth medium of a strain that is virulent to mice, with a non-virulent strain. Particularly one of these proteins was present at significantly higher levels in stationary growth medium from the virulent strain. We determined the three-dimensional structure of the protein that showed a unique tetrameric organization composed of four helix-loop-helix motifs. Affinity pull-down mass spectrometry analysis in human plasma demonstrated that the protein interacts with histidine-rich glycoprotein (HRG), and the name sHIP (streptococcal Histidine-rich glycoprotein Interacting Protein) is therefore proposed. HRG has antibacterial activity, and when challenged by HRG, sHIP was found to rescue S. pyogenes bacteria. This and the finding that patients with invasive S. pyogenes infection respond with antibody production against sHIP, suggest a role for the protein in S. pyogenes pathogenesis.},
  author       = {Wisniewska, Magdalena and Happonen, Lotta and Kahn, Fredrik and Varjosalo, Markku and Malmström, Lars and Rosenberger, George and Karlsson, Christofer and Cazzamali, Giuseppe and Pozdnyakova, Irina and Frick, Inga-Maria and Björck, Lars and Streicher, Werner and Malmström, Johan and Wikström, Mats},
  issn         = {1083-351X},
  language     = {eng},
  number       = {26},
  pages        = {18175--18188},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Functional and Structural Properties of a Novel Protein and Virulence Factor (sHIP) in Streptococcus pyogenes.},
  url          = {http://dx.doi.org/10.1074/jbc.M114.565978},
  volume       = {289},
  year         = {2014},
}