Evidence map›Paper›PMID 22117078›Full record

ArticleThe Journal of biological chemistry2012

Streptococcus pyogenes in human plasma: adaptive mechanisms analyzed by mass spectrometry-based proteomics.

Johan Malmström, Christofer Karlsson, Pontus Nordenfelt, Reto Ossola, Hendrik Weisser, Andreas Quandt, Karin Hansson, Ruedi Aebersold, Lars Malmström, Lars Björck

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.8field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Molecular & cellular proteomics : MCP · 2018
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  11. SCM, the M Protein ofFrontiers in cellular and infection microbiology · 2017
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 3 countries.

Johan MalmströmDepartment of Immunotechnology, Lund University, SE-22100 Lund, Sweden. Johan.Malmstrom@immun.lth.se
Christofer Karlsson
Pontus Nordenfelt
Reto Ossola
Hendrik Weisser
Andreas Quandt
Karin Hansson
Ruedi Aebersold
Lars Malmström
Lars Björck
ETH Zurich · CHLund University · SEInstitute of Nanotechnology · GBLife Science Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus pyogenes is a major bacterial pathogen and a potent inducer of inflammation causing plasma leakage at the site of infection. A combination of label-free quantitative mass spectrometry-based proteomics strategies were used to measure how the intracellular proteome homeostasis of S. pyogenes is influenced by the presence of human plasma, identifying and quantifying 842 proteins. In plasma the bacterium modifies its production of 213 proteins, and the most pronounced change was the complete down-regulation of proteins required for fatty acid biosynthesis. Fatty acids are transported by albumin (HSA) in plasma. S. pyogenes expresses HSA-binding surface proteins, and HSA carrying fatty acids reduced the amount of fatty acid biosynthesis proteins to the same extent as plasma. The results clarify the function of HSA-binding proteins in S. pyogenes and underline the power of the quantitative mass spectrometry strategy used here to investigate bacterial adaptation to a given environment.

Indexed as

Adaptation, PhysiologicalPlasmaBacterial ProteinsHumansMass SpectrometryProteomeProteomicsSerum AlbuminStreptococcus pyogenesBacterial ProteinsProteomeSerum Albumin

Identifiers

PMID22117078
PMCPMC3256886
OpenAlexW1972029046

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.