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Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes

Wilk, Laura LU ; Happonen, Lotta LU ; Malmström, Johan LU and Herwald, Heiko LU (2018) In Journal of Proteome Research 17(1). p.600-617
Abstract

Streptococcus pyogenes is a major global health burden causing a wide variety of diseases. Because a vaccine against this bacterium is still lacking, vaccine candidates or antimicrobial therapies are urgently needed. Here we use an invasive and clinically relevant streptococcal M1 serotype to characterize the bacterial proteome in-depth. An elaborate fractionation technique is employed to separate the different cell fractions, followed by shotgun mass-spectrometry analysis, allowing us to confirm the expression of nearly two-thirds (1022) of the 1690 open reading frames predicted for the streptococcal M1 reference proteome. In contrast with other studies, we present the entire isolated membrane proteome, which opens up a whole new... (More)

Streptococcus pyogenes is a major global health burden causing a wide variety of diseases. Because a vaccine against this bacterium is still lacking, vaccine candidates or antimicrobial therapies are urgently needed. Here we use an invasive and clinically relevant streptococcal M1 serotype to characterize the bacterial proteome in-depth. An elaborate fractionation technique is employed to separate the different cell fractions, followed by shotgun mass-spectrometry analysis, allowing us to confirm the expression of nearly two-thirds (1022) of the 1690 open reading frames predicted for the streptococcal M1 reference proteome. In contrast with other studies, we present the entire isolated membrane proteome, which opens up a whole new source for drug targets. We show both the unique and most prevalent proteins for each cellular fraction and analyze the presence of predicted cell-wall-anchored proteins and lipoproteins. With our approach, we also identify a variety of novel proteins whose presence has not been reported in previous proteome studies. Proteins of interest, potential virulence factors, and drug or vaccine targets are discussed for each cellular fraction. Overall, the results of this work represent the so-far widest proteomic approach to characterize the protein composition and localization in S. pyogenes.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
bacterial proteome, cell wall, cellular fractionation, drug target, mass spectrometry, membrane, secretome, Streptococcus pyogenes, vaccine, virulence factor
in
Journal of Proteome Research
volume
17
issue
1
pages
600 - 617
publisher
The American Chemical Society
external identifiers
  • scopus:85040177275
ISSN
1535-3893
DOI
10.1021/acs.jproteome.7b00701
language
English
LU publication?
yes
id
20b8a884-5ab7-4e20-b4f2-6d6dd6cfad9a
date added to LUP
2018-01-15 08:07:03
date last changed
2018-05-29 11:16:02
@article{20b8a884-5ab7-4e20-b4f2-6d6dd6cfad9a,
  abstract     = {<p>Streptococcus pyogenes is a major global health burden causing a wide variety of diseases. Because a vaccine against this bacterium is still lacking, vaccine candidates or antimicrobial therapies are urgently needed. Here we use an invasive and clinically relevant streptococcal M1 serotype to characterize the bacterial proteome in-depth. An elaborate fractionation technique is employed to separate the different cell fractions, followed by shotgun mass-spectrometry analysis, allowing us to confirm the expression of nearly two-thirds (1022) of the 1690 open reading frames predicted for the streptococcal M1 reference proteome. In contrast with other studies, we present the entire isolated membrane proteome, which opens up a whole new source for drug targets. We show both the unique and most prevalent proteins for each cellular fraction and analyze the presence of predicted cell-wall-anchored proteins and lipoproteins. With our approach, we also identify a variety of novel proteins whose presence has not been reported in previous proteome studies. Proteins of interest, potential virulence factors, and drug or vaccine targets are discussed for each cellular fraction. Overall, the results of this work represent the so-far widest proteomic approach to characterize the protein composition and localization in S. pyogenes.</p>},
  author       = {Wilk, Laura and Happonen, Lotta and Malmström, Johan and Herwald, Heiko},
  issn         = {1535-3893},
  keyword      = {bacterial proteome,cell wall,cellular fractionation,drug target,mass spectrometry,membrane,secretome,Streptococcus pyogenes,vaccine,virulence factor},
  language     = {eng},
  month        = {01},
  number       = {1},
  pages        = {600--617},
  publisher    = {The American Chemical Society},
  series       = {Journal of Proteome Research},
  title        = {Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes},
  url          = {http://dx.doi.org/10.1021/acs.jproteome.7b00701},
  volume       = {17},
  year         = {2018},
}