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Related Experiment Videos

Human phagocytes have multiple lipid A-binding sites.

D T Golenbock1, R Y Hampton, C R Raetz

  • 1Laboratory of Cellular Physiology and Immunology, Rockefeller University, New York, New York 10021.

Infection and Immunity
|December 1, 1990
PubMed
Summary
This summary is machine-generated.

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Researchers identified distinct bacterial lipopolysaccharide (LPS) binding mechanisms on cell surfaces. CD11-CD18 integrins bind LPS-coated erythrocytes, while a separate protein binds lipid IVA, suggesting context-dependent LPS interactions.

Area of Science:

  • Immunology
  • Cell Biology
  • Biochemistry

Background:

  • Bacterial lipopolysaccharide (LPS) is a key immune stimulus, but its cell surface targets remain incompletely defined.
  • Understanding LPS-cell interactions is crucial for deciphering immune responses and developing targeted therapies.

Purpose of the Study:

  • To identify and characterize the specific cell surface proteins that bind bacterial lipopolysaccharide (LPS).
  • To investigate whether the CD11-CD18 integrin family mediates LPS binding.

Main Methods:

  • Utilized two distinct assays: erythrocyte-lipopolysaccharide conjugates (ELPS) binding to human cells and radiolabeled [32P]lipid IVA binding to leukocytes.
  • Employed Western blotting and antibody inhibition assays to identify and characterize LPS-binding proteins.

Related Experiment Videos

  • Examined LPS binding in cells from patients with CD18 deficiency.

    • Main Results:

    • The CD11-CD18 integrin family was identified as a binding site for lipid A in human phagocytes using the ELPS assay.
    • A distinct approximately 95-kDa protein, not identical to CD18, was found to bind [32P]lipid IVA in murine macrophages.
    • Mononuclear cells deficient in CD18 showed impaired ELPS binding but normal [32P]lipid IVA binding, indicating differential binding mechanisms.

    Conclusions:

    • Bacterial lipopolysaccharide (LPS) can bind to cell surfaces via CD18-dependent and CD18-independent pathways.
    • The physical state of LPS (particulate vs. dispersed) influences the identity of the cell surface binding protein.
    • These findings reveal a more complex mechanism of LPS-cell interaction than previously understood.