Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes

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Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes. / Wilk, Laura; Happonen, Lotta; Malmström, Johan; Herwald, Heiko.

I: Journal of Proteome Research, Vol. 17, Nr. 1, 05.01.2018, s. 600-617.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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TY - JOUR

T1 - Comprehensive Mass Spectrometric Survey of Streptococcus pyogenes Subcellular Proteomes

AU - Wilk, Laura

AU - Happonen, Lotta

AU - Malmström, Johan

AU - Herwald, Heiko

PY - 2018/1/5

Y1 - 2018/1/5

N2 - 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.

AB - 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.

KW - bacterial proteome

KW - cell wall

KW - cellular fractionation

KW - drug target

KW - mass spectrometry

KW - membrane

KW - secretome

KW - Streptococcus pyogenes

KW - vaccine

KW - virulence factor

U2 - 10.1021/acs.jproteome.7b00701

DO - 10.1021/acs.jproteome.7b00701

M3 - Article

VL - 17

SP - 600

EP - 617

JO - Journal of Proteome Research

T2 - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 1

ER -