Molecular Cloning and Expression of T11 cDNAs Reveal a Receptor-Like Structure on Human T Lymphocytes

• Published in: Proceedings of the National Academy of Sciences - PNAS 1987-05, Vol.84 (9), p.2941-2945
• Main Authors: Sayre, Peter H., Chang, Hsiu-Ching, Hussey, Rebecca E., Brown, Nicholas R., Richardson, Neil E., Spagnoli, Giulio, Clayton, Linda K., Reinherz, Ellis L.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Amino acids; Animals; Antibodies; Antigens, Surface - genetics; B lymphocytes; Base Sequence; Carrier Proteins - genetics; CD2 Antigens; Cell Line; Cell lines; Cloning, Molecular; Complementary DNA; COS cells; DNA - metabolism; Gels; Genes; Humans; Molecules; Receptors, Antigen, T-Cell - genetics; Receptors, Immunologic - genetics; RNA; RNA, Messenger - genetics; T lymphocytes; T-Lymphocytes - immunology; Transcription, Genetic
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.84.9.2941

The T11 (CD2) sheep-erythrocyte-binding protein is a T-cell surface molecule involved in activation of T lymphocytes and thymocytes, including those lacking the T3-Ti antigen-receptor complex. The primary structure of T11 was deduced from protein microsequencing and cDNA cloning. The mature human protein appears to be divided into three domains: a hydrophilic 185 amino acid external domain bearing only limited homology to the T-cell surface protein T4 and the immunoglobulin κ light chain variable region, a 25 amino acid hydrophobic transmembrane segment, and a 126 amino acid cytoplasmic domain rich in prolines and basic residues. Transfection of cDNAs encoding either the 1.7- or the 1.3-kilobase T11 mRNA into COS-1 cells resulted in expression of surface T11 epitopes as well as sheep-erythrocyte-binding capacity. The predicted structure is consistent with the possibility that T11 functions in signal transduction.