Abstract
Recently the human T cell erythrocyte receptor CD2 has been shown to bind human erythrocytes through LFA-3, a heavily gly-cosylated surface protein of broad tissue distribution1,2. CD2–LFA-3 interactions are important for cytolytic conjugate formation3,4, for thymocyte adhesion5, and for T cell activation6. A complementary DNA clone encoding LFA-3 was isolated using a novel transient expression system of mouse cells11. 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 domains7, cellular adhesion molecules in both neural and lymphoid tissues could have a common ancestor.
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Seed, B. An LFA-3 cDNA encodes a phospholipid-linked membrane protein homologous to its receptor CD2. Nature 329, 840–842 (1987). https://doi.org/10.1038/329840a0
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DOI: https://doi.org/10.1038/329840a0
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