Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen.

Abstract:

:CD2 (T11, sheep erythrocyte receptor) is a surface antigen of the human T-lymphocyte lineage. cDNA clones encoding CD2 have been isolated by using the purified, denatured CD2 to raise a rat antiserum. Positive clones were recognized in a phage lambda gt11 expression library prepared from the human leukemia T-cell line J6. The DNA sequence contained an open reading frame encoding 360 amino acids. The N-terminal 24 amino acids were characteristic of a signal peptide and were followed by a region that matched all 25 residues of the CD2 N terminus previously determined by amino acid sequencing. The predicted amino acid sequence is consistent with that of a transmembrane glycoprotein containing three potential N-glycosylation sites on the N-terminal side of a 26-amino acid hydrophobic segment. There is a large cytoplasmic domain of 125 amino acids that is rich in proline and in basic residues. RNA blot-hybridization analysis demonstrated hybridization only in those T cells that were positive for surface CD2 antigen. There are limited regions of sequence similarity to members of the immunoglobulin supergene family.

authors

Sewell WA,Brown MH,Dunne J,Owen MJ,Crumpton MJ

doi

10.1073/pnas.83.22.8718

subject

Has Abstract

pub_date

1986-11-01 00:00:00

pages

8718-22

issue

22

eissn

0027-8424

issn

1091-6490

journal_volume

83

pub_type

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