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Related Experiment Videos

FbsA-driven fibrinogen polymerization: a bacterial "deceiving strategy".

Matteo Pierno1, Laura Maravigna, Roberto Piazza

  • 1Dipartimento di Ingegneria Nucleare, CSGI-Politecnico di Milano, via Ponzio 34/3, 20133 Milano, Italy.

Physical Review Letters
|February 21, 2006
PubMed
Summary

Streptococcus agalactiae's FbsA protein causes human fibrinogen to aggregate, forming a network. This bacterial coating masks the pathogen from immune cells.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Immunology

Background:

  • Streptococcus agalactiae is a significant human pathogen.
  • Bacterial cell wall proteins play crucial roles in host-pathogen interactions.
  • Fibrinogen is a key protein in blood coagulation and immune responses.

Purpose of the Study:

  • To investigate the function of the Streptococcus agalactiae cell wall protein FbsA.
  • To determine the effect of FbsA on human plasma fibrinogen.
  • To understand the role of FbsA-mediated fibrinogen aggregation in bacterial evasion of phagocytosis.

Main Methods:

  • Protein-protein interaction studies.
  • Fibrinogen aggregation assays.
  • Microscopy to visualize bacterial cell wall coatings.

Related Experiment Videos

  • Phagocytosis assays using immune cells.

    • Main Results:

    • FbsA promotes large-scale aggregation of human plasma fibrinogen.
    • This aggregation forms a semiflexible polymerlike network in solution and on surfaces.
    • A thick layer of aggregated fibrinogen forms on the bacterial cell wall.
    • This layer effectively masks Streptococcus agalactiae from phagocytosis.

    Conclusions:

    • FbsA is a potent fibrinogen-binding protein.
    • FbsA-mediated fibrinogen aggregation contributes to bacterial immune evasion.
    • FbsA represents a potential target for therapeutic interventions against Streptococcus agalactiae infections.