Evidence map›Paper›PMID 34581598›Full record

ArticlemSystems2021

Streptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.

Sounak Chowdhury, Hamed Khakzad, Gizem Ertürk Bergdahl, Rolf Lood, Simon Ekstrom, Dirk Linke, Lars Malmström, Lotta Happonen, Johan Malmström

Open access · goldAbstract read
In one paragraph

Article in mSystems, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Rapid Proteome-Wide Discovery of Protein-Protein Interactions With ppIRIS.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

9 authors at 3 institutions in 3 countries.

Sounak ChowdhuryDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.
Hamed KhakzadEquipe Signalisation Calcique et Infections Microbiennes, Ecole Normale Supérieure Paris-Saclay, Gif-sur-Yvette, France.
Gizem Ertürk BergdahlDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.
Rolf LoodDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.ORCID 0000-0002-5974-0674
Simon EkstromBioMS, Lund, Sweden.
Dirk LinkeDepartment of Biosciences, Section for Genetics and Evolutionary Biology, University of Oslo, Oslo, Norway.
Lars MalmströmDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.
Lotta HapponenDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.
Johan MalmströmDivision of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.
Lund University · SEÉcole Normale Supérieure Paris-Saclay · FRUniversity of Oslo · NO

Funding

Alfred Österlunds Stiftelse (Alfred Österlunds Foundation)EC | H2020 | H2020 Priority Excellent Science | H2020 Marie Skłodowska-Curie Actions (MSCA) Viral and Bacterial Adhesin Network Training (ViBrANT) Program 765042Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation) 2016.0023Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation) 2019.0353Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (SNF) P2ZHP3_191289Vetenskapsrådet (VR) 2019-01646
6 · The paper itself

Abstract

Streptococcus pyogenes is known to cause both mucosal and systemic infections in humans. In this study, we used a combination of quantitative and structural mass spectrometry techniques to determine the composition and structure of the interaction network formed between human plasma proteins and the surfaces of different S. pyogenes serotypes. Quantitative network analysis revealed that S. pyogenes forms serotype-specific interaction networks that are highly dependent on the domain arrangement of the surface-attached M protein. Subsequent structural mass spectrometry analysis and computational modeling of one of the M proteins, M28, revealed that the network structure changes across different host microenvironments. We report that M28 binds secretory IgA via two separate binding sites with high affinity in saliva. During vascular leakage mimicked by increasing plasma concentrations in saliva, the binding of secretory IgA was replaced by the binding of monomeric IgA and C4b-binding protein (C4BP). This indicates that an upsurge of C4BP in the local microenvironment due to damage to the mucosal membrane drives the binding of C4BP and monomeric IgA to M28. These results suggest that S. pyogenes has evolved to form microenvironment-dependent host-pathogen protein complexes to combat human immune surveillance during both mucosal and systemic infections.

Indexed as

DIA-MShost-pathogen interactionsM proteinsprotein-protein interactionsStreptococcus pyogenesXL-MS

Identifiers

PMID34581598
PMCPMC8547449
OpenAlexW3203934297

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.