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The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization
C R Maliszewski1, G J Delespesse, M A Schoenborn
1Immunex Research and Development Corporation, Seattle, WA 98101.
Journal of Immunology (Baltimore, Md. : 1950)
|October 15, 1994
Summary
CD39 is a novel cell surface glycoprotein cloned and characterized in humans and mice. This molecule has unique structural features and homology to yeast guanosine diphosphatase.
Area of Science:
- Immunology
- Molecular Biology
- Biochemistry
Background:
- CD39 is a cell surface molecule on activated lymphoid cells.
- CD39 mediates B cell homotypic adhesion when ligated by specific antibodies.
- Previous studies indicated CD39's role in cellular adhesion.
Purpose of the Study:
- To clone and perform molecular characterization of human and murine CD39.
- To elucidate the structural characteristics and topology of CD39.
- To identify functional epitopes on the CD39 molecule.
Main Methods:
- Nucleotide sequencing of human and murine CD39.
- Amino acid sequence analysis and homology searches.
- Construction of mouse-human hybrid molecules.
- Phage peptide display library screening.
Main Results:
- Human CD39 encodes a 510 amino acid protein with glycosylation sites and transmembrane regions.
- Murine CD39 shares 75% amino acid identity with human CD39 but lacks cross-reactivity.
- CD39 exhibits homology to yeast guanosine diphosphatase.
- A model suggests a short intracellular N-terminus, a large extracellular loop with an epitope, and a short intracellular C-terminus.
Conclusions:
- CD39 is a novel cell surface glycoprotein with unique structural features.
- The study provides insights into CD39 topology and functional epitope localization.
- CD39 represents a new class of cell surface molecules with potential roles in immune responses.