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Activation signals are delivered through two distinct epitopes of CD100, a unique 150 kDa human lymphocyte surface

C Hérold1, G Bismuth, A Bensussan

  • 1INSERM U93, Hôpital Saint-Louis, Paris, France.

International Immunology
|January 1, 1995
PubMed

Insights

A novel antibody, BD16, targets the CD100 glycoprotein on lymphocytes, revealing distinct effects on cell proliferation. This finding offers new insights into immune cell signaling pathways.

Area of Science:

  • Immunology
  • Cell Biology

Background:

  • CD100 is a lymphocyte surface glycoprotein previously identified using the BB18 monoclonal antibody (mAb).
  • A new mAb, BD16, recognizes a distinct epitope on the 150 kDa CD100 structure.

Purpose of the Study:

  • To investigate the differential functional effects of distinct CD100 epitopes on lymphocyte proliferation.
  • To characterize the impact of BD16 mAb on T cell activation via CD2 and CD3 pathways.

Main Methods:

  • Isolation and characterization of a novel monoclonal antibody (BD16) targeting CD100.
  • Functional assays assessing peripheral blood lymphocyte (PBL) and purified T cell proliferation.
  • Stimulation of cells using anti-CD2, anti-CD3, and phorbol myristate acetate (PMA).

Main Results:

  • BD16 mAb differentially modulates CD2 and CD3 induced proliferation in PBLs, inhibiting CD3 and enhancing CD2.
  • In purified T cells, BD16 mAb enhances both CD2 and CD3 induced proliferation.
  • The previously identified BB18 mAb targeting CD100 had no effect on CD2/CD3 induced proliferation but induced proliferation with submitogenic PMA.

Conclusions:

  • Distinct epitopes on the CD100 molecule can elicit differential functional responses in lymphocytes.
  • BD16 mAb provides a tool to dissect the role of specific CD100 epitopes in immune cell activation.
  • The findings highlight the complex regulatory mechanisms of lymphocyte proliferation involving CD100.

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