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:
https://lup.lub.lu.se/record/4334644
- author
- Sjöholm, Kristoffer
; Karlsson, Christofer
LU
; Linder, Adam
LU
and Malmström, Johan
LU
- organization
- publishing date
- 2014
- 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
- 2016-04-01 09:52:21
- date last changed
- 2022-02-02 03:38:06
@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 = {{https://lup.lub.lu.se/search/files/1344039/4644724.pdf}},
doi = {{10.1039/c3mb70555b}},
volume = {{10}},
year = {{2014}},
}