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Cloning, recombinant expression and biochemical characterization of the murine CD83 molecule which is specifically
S Berchtold1, P Mühl-Zürbes, C Heufler
1Department of Dermatology, University of Erlangen, Hartmannstrasse 14, 91052, Erlangen, Germany. susanne.berchtold@derma.med.uni-erlangen.de
Insights
Researchers cloned mouse CD83 (mCD83) cDNA from dendritic cells (DCs). Mouse CD83 shares structural similarities with human CD83 and is expressed on mature DCs, aiding in immune response studies.
Area of Science:
- Immunology
- Molecular Biology
Background:
- Human CD83 (hCD83) is a key surface glycoprotein and the most reliable marker for mature dendritic cells (DCs).
- Understanding the murine counterpart is crucial for comparative immunology and DC research.
Purpose of the Study:
- To clone and characterize the cDNA encoding mouse CD83 (mCD83).
- To investigate the expression patterns and structural properties of mCD83.
Main Methods:
- Cloning mCD83 cDNA from a murine bone marrow-derived DC (BM-DC) library.
- DNA sequencing and amino acid identity analysis with hCD83.
- Northern blot analysis to assess mCD83 mRNA expression.
- Transfection of COS-7 cells to study glycosylation.
- Recombinant expression of the extracellular domain in E. coli and NMR analysis.
Main Results:
- Successfully cloned mCD83 cDNA, encoding a 196 amino acid protein with 63% identity to hCD83.
- mCD83 mRNA is highly expressed in BM-DCs and upregulated by LPS and TNF-alpha.
- mCD83 undergoes glycosylation, and its extracellular domain is structurally folded.
Conclusions:
- Mouse CD83 is a structurally conserved homolog of human CD83.
- mCD83 expression is regulated by inflammatory stimuli, similar to hCD83.
- These findings provide a foundation for studying mCD83 function in murine immune responses.
Abstract:
Human CD83 (hCD83) is a glycoprotein expressed predominantly on the surface of dendritic cells (DC) and represents the best marker for mature DC. Here, we report the cloning of the cDNA encoding mouse CD83 (mCD83) from a murine bone marrow-derived DC (BM-DC) cDNA library. DNA sequence analysis revealed a 196 amino acid protein including a signal peptide of 21 amino acids which shares 63% amino acid identity with hCD83. Using Northern blot analyses, mCD83 mRNA was found to be strongly expressed in mouse BM-DC and its expression was upregulated following stimulation with LPS or TNF-alpha. Transfection experiments using COS-7 cells revealed that mCD83 is glycosylated. Furthermore, the extracellular CD83 domain was recombinantly expressed in Escherichia coli and one-dimensional NMR data strongly support that the protein is structurally folded.
