Characterization of human homologue of 4-1BB and its ligand

Zhen Zhou, Seung Kim, José Hurtado, Zang H. Lee, Kack K. Kim, Karen E. Pollok, Byoung S. Kwon

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The human homologue of 4-1BB (H4-1BB) cDNA was isolated from PMA plus ionomycin-treated human peripheral T-cell cDNA libraries. The amino acid sequence deduced from the nucleotide sequence showed that the protein is composed of 255 amino acids with 2 potential N-linked glycosylation sites. The molecular weight of its protein backbone is calculated to be 27 kDa. The H4-1BB contains features such as signal sequence and transmembrane domain, indicating that it is a receptor protein. This protein showed 60% identity of amino acid sequence to mouse 4-1BB. In the cytoplasmic domain there are 5 regions of amino acid sequences conserved from mouse to human, indicating that these residues might be important in the 4-1BB function. H4-1BB mRNA was detected in unstimulated peripheral blood T cells and was inducible in T-cell lines such as Jurkat and CEM. H4-1BB-AP, a fusion protein between the H4-1BB extracellular domain and alkaline phosphatase, was used to identify the ligand for the H4-1BB. Although the H4-1BB ligand was detected in both T and B cells of human peripheral blood, the ligand was preferentially expressed in primary B cells and B-cell lines. Daudi, a B-cell lymphoma, was one of the B-cell lines that carried a higher number of ligands. Scatchard analysis showed that the Kd = 1.4 × 109 M and the number of ligands in Daudi cell was 4.2 × 103.

Original languageEnglish (US)
Pages (from-to)67-73
Number of pages7
JournalImmunology Letters
Issue number1-2
StatePublished - Feb 1995


  • Binding site
  • Dissociation constant
  • Human 4-1BB
  • Human 4-1BB ligand

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

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    Zhou, Z., Kim, S., Hurtado, J., Lee, Z. H., Kim, K. K., Pollok, K. E., & Kwon, B. S. (1995). Characterization of human homologue of 4-1BB and its ligand. Immunology Letters, 45(1-2), 67-73.