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N-glycosylation is required for human CD2 immunoadhesion functions

M A Recny1, M A Luther, M H Knoppers

  • 1PROCEPT, Inc., Cambridge, Massachusetts 02139.

The Journal of Biological Chemistry
|November 5, 1992
PubMed

Insights

N-glycosylation at Asn65 is crucial for T-lymphocyte CD2 receptor adhesion functions. This process stabilizes the CD2 adhesion domain, enabling CD2-CD58 interactions necessary for cell-cell binding.

Area of Science:

  • Immunology
  • Glycobiology
  • Cell Biology

Background:

  • CD2 is a T-lymphocyte glycoprotein receptor mediating cell-cell adhesion through binding to CD58.
  • The extracellular segment of CD2 has two domains, with adhesion functions localized to the N-terminal domain.
  • This N-terminal domain contains a single N-glycosylation site at Asn65.

Purpose of the Study:

  • To define the role of N-linked glycans at Asn65 in CD2-CD58 interactions.
  • To characterize the N-glycotype structure of CD2.
  • To investigate the necessity of N-glycosylation for CD2 adhesion functions.

Main Methods:

  • Analysis of deglycosylated soluble recombinant CD2.
  • Characterization of a mutant transmembrane CD2 molecule (Asn65-Gln65 substitution).
  • Electrospray ionization-mass spectrometry (ESI-MS) for N-glycotype analysis.

Main Results:

  • Deglycosylated CD2 and the Asn65-Gln65 mutant CD2 failed to bind CD58.
  • These modified CD2 molecules also did not bind to monoclonal antibodies targeting native CD2 adhesion epitopes.
  • ESI-MS revealed high mannose oligosaccharides (Man5-9GlcNAc2) as the sole N-glycotypes at Asn65 in CHO cell-expressed soluble CD2.

Conclusions:

  • N-glycosylation at Asn65 is essential for CD2-mediated cell adhesion.
  • N-glycosylation likely stabilizes the first domain of the human CD2 receptor.
  • These findings highlight the critical role of glycosylation in immune cell interactions.

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