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A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network.

Sjöholm, Kristoffer; Karlsson, Christofer LU ; Linder, Adam LU and Malmström, Johan LU (2014) In Molecular BioSystems 10(7). p.1698-1708
Abstract
Streptococcus pyogenes is a major human bacterial pathogen responsible for severe and invasive disease associated with high mortality rates. The bacterium interacts with several human blood plasma proteins and clarifying these interactions and their biological consequences will help to explain the progression from mild to severe infections. In this study, we used a combination of mass spectrometry (MS) based techniques to comprehensively quantify the components of the S. pyogenes-plasma protein interaction network. From an initial list of 181 interacting human plasma proteins defined using liquid chromatography (LC)-MS/MS analysis we further subdivided the interacting protein list using selected reaction monitoring (SRM) depending on the... (More)
Streptococcus pyogenes is a major human bacterial pathogen responsible for severe and invasive disease associated with high mortality rates. The bacterium interacts with several human blood plasma proteins and clarifying these interactions and their biological consequences will help to explain the progression from mild to severe infections. In this study, we used a combination of mass spectrometry (MS) based techniques to comprehensively quantify the components of the S. pyogenes-plasma protein interaction network. From an initial list of 181 interacting human plasma proteins defined using liquid chromatography (LC)-MS/MS analysis we further subdivided the interacting protein list using selected reaction monitoring (SRM) depending on the level of enrichment and protein concentration on the bacterial surface. The combination of MS methods revealed several previously characterized interactions between the S. pyogenes surface and human plasma along with many more, so far uncharacterised, possible plasma protein interactions with S. pyogenes. In follow-up experiments, the combination of MS techniques was applied to study differences in protein binding to a S. pyogenes wild type strain and an isogenic mutant lacking several important virulence factors, and a unique pair of invasive and non-invasive S. pyogenes isolates from the same patient. Comparing the plasma protein-binding properties of the wild type and the mutant and the invasive and non-invasive S. pyogenes bacteria revealed considerable differences, underlining the significance of these protein interactions. The results also demonstrate the power of the developed mass spectrometry method to investigate host-microbial relationships with a large proteomics depth and high quantitative accuracy. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Molecular BioSystems
volume
10
issue
7
pages
1698 - 1708
publisher
Royal Society of Chemistry
external identifiers
  • pmid:24525632
  • wos:000337103600008
  • scopus:84901835483
ISSN
1742-2051
DOI
10.1039/c3mb70555b
language
English
LU publication?
yes
id
7a0d08c8-89b5-4d6b-8d69-aedf8e1b53dd (old id 4334644)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/24525632?dopt=Abstract
date added to LUP
2014-03-05 23:42:38
date last changed
2017-09-03 03:02:14
@article{7a0d08c8-89b5-4d6b-8d69-aedf8e1b53dd,
  abstract     = {Streptococcus pyogenes is a major human bacterial pathogen responsible for severe and invasive disease associated with high mortality rates. The bacterium interacts with several human blood plasma proteins and clarifying these interactions and their biological consequences will help to explain the progression from mild to severe infections. In this study, we used a combination of mass spectrometry (MS) based techniques to comprehensively quantify the components of the S. pyogenes-plasma protein interaction network. From an initial list of 181 interacting human plasma proteins defined using liquid chromatography (LC)-MS/MS analysis we further subdivided the interacting protein list using selected reaction monitoring (SRM) depending on the level of enrichment and protein concentration on the bacterial surface. The combination of MS methods revealed several previously characterized interactions between the S. pyogenes surface and human plasma along with many more, so far uncharacterised, possible plasma protein interactions with S. pyogenes. In follow-up experiments, the combination of MS techniques was applied to study differences in protein binding to a S. pyogenes wild type strain and an isogenic mutant lacking several important virulence factors, and a unique pair of invasive and non-invasive S. pyogenes isolates from the same patient. Comparing the plasma protein-binding properties of the wild type and the mutant and the invasive and non-invasive S. pyogenes bacteria revealed considerable differences, underlining the significance of these protein interactions. The results also demonstrate the power of the developed mass spectrometry method to investigate host-microbial relationships with a large proteomics depth and high quantitative accuracy.},
  author       = {Sjöholm, Kristoffer and Karlsson, Christofer and Linder, Adam and Malmström, Johan},
  issn         = {1742-2051},
  language     = {eng},
  number       = {7},
  pages        = {1698--1708},
  publisher    = {Royal Society of Chemistry},
  series       = {Molecular BioSystems},
  title        = {A comprehensive analysis of the Streptococcus pyogenes and human plasma protein interaction network.},
  url          = {http://dx.doi.org/10.1039/c3mb70555b},
  volume       = {10},
  year         = {2014},
}