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Related Experiment Videos

Pneumococcal immune adherence to human erythrocytes.

J-M Hament1, H van Dijk, A Fleer

  • 1Department of Paediatric Infectious Diseases, Wilhelmina Children's Hospital, University Medical Centre, Utrecht, The Netherlands.

European Journal of Clinical Investigation
|February 18, 2003
PubMed
Summary

Human red blood cells bind to C3b-coated pneumococci via complement receptor 1, involving both innate and adaptive immunity. Factor I facilitates bacterial detachment, supporting the immune adherence hypothesis.

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Area of Science:

  • Immunology
  • Microbiology
  • Hematology

Background:

  • Human red blood cells (RBCs) bind C3b-coated microbes via the C3b/CR1 receptor, a process known as immune adherence.
  • Pneumococcal adherence to RBCs is crucial for understanding bacterial clearance mechanisms.

Purpose of the Study:

  • To quantify pneumococcal adherence to human RBCs using flow cytometry.
  • To investigate the kinetics and immune factors involved in pneumococcal-RBC binding.

Main Methods:

  • Quantification of pneumococcal adherence to human erythrocytes using Fluorescence-Activated Cell Sorting (FACS) analysis.
  • Assessment of the roles of antibodies and complement activation in the binding process.

Main Results:

Related Experiment Videos

  • Pneumococci bind to human RBCs in the presence of human serum, requiring C3b/C4b coating.
  • Complement receptor 1 (CR1) on erythrocytes is the primary ligand for pneumococcal adherence.
  • Both mannose-binding lectin (innate immunity) and IgG antibodies (adaptive immunity) contribute to C3b-coated pneumococcal binding.
  • Factor I induces detachment of bound pneumococci from RBCs.

    • Conclusions:

    • Pneumococci adhere to RBCs, mediated by C3b coating and CR1.
    • Both classical and lectin complement pathways are vital for optimal pneumococcal C3b-coating and subsequent immune adherence.
    • Factor I-mediated detachment of pneumococci from RBCs supports the immune adherence hypothesis, targeting bacteria to the spleen.