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CLONING, SEQUENCING AND EXPRESSION OF PORCINE CD40 LIGAND IN ESCHERICHIA COLI AND HUMAN AND PORCINE CELLS
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...
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Published in: | Cytokine (Philadelphia, Pa.) Pa.), 2002-12, Vol.20 (6), p.274-282 |
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Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 1043-4666 1096-0023 |
DOI: | 10.1006/cyto.2003.2000 |