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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Oct 18, 2025

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Streptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.

Sounak Chowdhury1, Hamed Khakzad2,3, Gizem Ertürk Bergdahl1

  • 1Division of Infection Medicine, Department of Clinical Sciences, Faculty of Medicine, Lund Universitygrid.4514.4, Lund, Sweden.

Msystems
|September 28, 2021
PubMed
Summary

Streptococcus pyogenes forms unique protein interaction networks on its surface, dictated by M protein structure. These networks adapt to the host environment, enabling the pathogen to evade immune responses during infection.

Keywords:
DIA-MSM proteinsStreptococcus pyogenesXL-MShost-pathogen interactionsprotein-protein interactions

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Area of Science:

  • Microbiology and Immunology
  • Host-Pathogen Interactions
  • Proteomics

Background:

  • Streptococcus pyogenes (group A Streptococcus) causes millions of infections and deaths globally.
  • The bacterium utilizes surface virulence factors, particularly M protein, to establish infections.
  • Understanding host-pathogen protein interactions is crucial for combating S. pyogenes.

Purpose of the Study:

  • To determine the composition and structure of human plasma protein interaction networks on S. pyogenes surfaces.
  • To investigate how M protein structure and host microenvironments influence these interactions.
  • To elucidate the adaptive strategies of S. pyogenes in evading immune surveillance.

Main Methods:

  • Quantitative and structural mass spectrometry techniques were employed.
  • Network analysis was used to characterize protein interactions across different S. pyogenes serotypes.
  • Computational modeling and in vitro assays (saliva, plasma) were used to study M28 protein interactions.

Main Results:

  • S. pyogenes exhibits serotype-specific protein interaction networks dependent on M protein domain arrangement.
  • The M28 protein binds secretory IgA in saliva, but this shifts to monomeric IgA and C4b-binding protein (C4BP) during simulated vascular leakage.
  • These microenvironment-dependent interactions suggest an adaptive mechanism for immune evasion.

Conclusions:

  • Streptococcus pyogenes dynamically alters its surface protein complexes in response to host microenvironmental changes.
  • M protein plays a key role in mediating these adaptive, microenvironment-specific host-pathogen interactions.
  • These findings highlight a novel strategy used by S. pyogenes to evade immune detection during infection.