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Antibody against the Leu-CAM beta-chain (CD18) promotes both LFA-1- and CR3-dependent adhesion events

M K Robinson1, D Andrew, H Rosen

  • 1Celltech Ltd., Slough, England.

Journal of Immunology (Baltimore, Md. : 1950)
|February 15, 1992
PubMed

Insights

A novel antibody targeting the Leukocytic cell-adhesion molecule common beta-chain (CD18) enhances immune cell adhesion. This antibody mimics natural activation pathways, promoting crucial cellular interactions for immune function.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • Leukocytic cell-adhesion molecules (beta 2 integrins) are vital for immune cell interactions.
  • These molecules mediate essential adhesive functions for immune cell activity.

Purpose of the Study:

  • To investigate an antibody targeting the common beta-chain (CD18) of Leukocytic cell-adhesion molecules.
  • To determine the antibody's effect on lymphocyte function-associated Ag-1 and CR3-dependent adhesion.

Main Methods:

  • Development and characterization of a novel antibody against CD18.
  • Assay of antibody-mediated promotion of lymphocyte function-associated Ag-1 and CR3 adhesion.
  • Analysis of epitope characteristics, including temperature sensitivity and cation dependence.

Main Results:

  • The antibody recognizes a temperature-sensitive epitope on CD18.
  • Antibody binding enhances both lymphocyte function-associated Ag-1 and CR3-dependent adhesion.
  • Adhesion promotion is independent of divalent cations.

Conclusions:

  • The antibody induces a conformational change in lymphocyte function-associated Ag-1 and CR3.
  • This conformational change may replicate natural immune cell activation mechanisms.
  • The findings suggest a new method for modulating immune cell adhesion.

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