An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2

Nature. 1987 Oct 29-Nov 4;329(6142):840-2. doi: 10.1038/329840a0.

Abstract

Recently the human T cell erythrocyte receptor CD2 has been shown to bind human erythrocytes through LFA-3, a heavily glycosylated surface protein of broad tissue distribution. CD2-LFA-3 interactions are important for cytolytic conjugate formation, for thymocyte adhesion, and for T cell activation. A complementary DNA clone encoding LFA-3 was isolated using a complementary DNA clone encoding LFA-3 was isolated using a novel transient expression system of mouse cells. The cDNA encodes a phospholipid-linked membrane protein whose extracellular domain shares significant homology with CD2. As CD2 is homologous with the neural cell adhesion molecule NCAM in immunoglobulin-like domains, cellular adhesion molecules in both neural and lymphoid tissues could have a common ancestor.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, Differentiation, T-Lymphocyte / genetics*
  • Antigens, Ly / genetics*
  • Antigens, Surface / genetics*
  • Base Sequence
  • DNA / metabolism*
  • Humans
  • Lymphocyte Function-Associated Antigen-1
  • Molecular Sequence Data
  • Nucleic Acid Hybridization
  • Phospholipids / metabolism
  • Protein Biosynthesis
  • Sequence Homology, Nucleic Acid
  • Transcription, Genetic

Substances

  • Antigens, Differentiation, T-Lymphocyte
  • Antigens, Ly
  • Antigens, Surface
  • Lymphocyte Function-Associated Antigen-1
  • Phospholipids
  • DNA

Associated data

  • GENBANK/X06296