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Selected Publication:

Publication type: Journal Article
Document type: Full Paper

Year: 2002

Author(s): Wienhold, D; Berger, N; Armengol, E; Büttner, M; Saalmüller, A; Pfaff, E

Title: Cloning, sequencing and expression of porcine CD40 ligand in Escherichia coli and human and porcine cells.

Source: Cytokine (20), 6 274-282.

Authors Vetmeduni Vienna:

Saalmüller Armin

The CD40L ligand (CD40L) plays an important role in the interaction between antigen-specific T lymphocytes and antigen-presenting cells. The porcine CD40L encoding gene was isolated from porcine peripheral blood mononuclear cells (PBMC) using RT-PCR. Sequence analysis of the cloned CD40L gene showed an open reading frame of 786 base pairs encoding a 262 amino acid protein with a predicted molecular mass of 29 kD. The deduced amino acid sequence of the porcine CD40L shared 82%, 88% and 93% similarity with the CD40L protein of mouse, human and cattle. The isolated CD40L sequence was expressed as a hexahistidine fusion protein in Escherichia coli and purified by affinity chromatography. The analysis of the CD40L-expression in human 293 and porcine MAX cells by immunofluorescence showed its location on the cell surface.

Keywords Pubmed: Amino Acid Sequence
Base Sequence
Blotting, Western
CD40 Ligand/biosynthesis
CD40 Ligand/genetics*
Cloning, Molecular*
Escherichia coli/metabolism*
Fluorescent Antibody Technique
Molecular Sequence Data

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