Isolation and characterization of a human interleukin cDNA clone, homologous to mouse B-cell stimulatory factor 1, that expresses B-cell- and T-cell-stimulating activities

Abstract

A cDNA sequence coding for a human interleukin has been isolated from a concanavalin A-activated human T-cell cDNA library based on homology with a mouse interleukin cDNA that expresses B-cell stimulatory factor 1 (BSF-1) activity and T-cell- and mast-cell-stimulating activities. The human cDNA contains a single open reading frame encoding a protein of 153 amino acid residues including a putative signal peptide. Amino acid sequences of the mouse and human polypeptides, deduced from their cDNAs, share extensive homology with the exception of about 40 amino acid residues near the middle portion, which share little homology. Supernatant of COS-7 monkey cells transfected with the human cDNA clone stimulated proliferation of human helper T-cell clones and of anti-IgM-activated human B cells, two properties of mouse BSF-1 on mouse cells. These results indicate that this human cDNA clone encodes a protein structurally and functionally homologous to mouse BSF-1.