This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Witvliet, M H Articles by Poolman, J T Search for Related Content PubMed PubMed Citation Articles by Witvliet, M H Articles by Poolman, J T

 Previous Article  |  Next Article 

Infect Immun. 1992 December; 60(12): 5085-5090

Interaction of pertussis toxin with human T lymphocytes.

Unit for Bacterial Vaccine Development and Pathogenesis Research, National Institute of Public Health and Environmental Protection, Bilthoven, The Netherlands.

ABSTRACT

The binding of pertussis toxin (PT) to the human T-cell line Jurkat was examined by using flow cytometry. Fluorescein isothiocyanate (FITC)-labeled PT bound rapidly to the cells in a specific manner as determined by blocking experiments with unlabeled toxin, B oligomer, and the S2-S4 and S3-S4 dimers. Monoclonal antibodies against the S3 subunit of the toxin also significantly inhibited the binding of FITC-PT. Sialidase treatment of the cells resulted in decreased binding of FITC-PT, indicating that sialic acid residues are involved in the binding process. In addition, we studied the effect of PT binding on the expression of cell surface molecules. On binding of PT to the cell surface, a rapid down-regulation of the T-cell receptor (TCR)-CD3 complex was observed. The modulation of the TCR-CD3 complex was independent of the toxin's enzymatic activity, as the B oligomer and a nonenzymatic toxin mutant induced modulation comparable to that caused by the native holotoxin. Isolated dimers did not cause down-regulation. Stimulation of the TCR-CD3 complex, leading to reduced cell surface expression of this complex, provides a possible explanation for the second messenger production associated with the interaction of PT or B oligomer with T lymphocytes. We therefore conclude that PT activates T cells by divalent binding to the TCR-CD3 complex itself or by binding a structure closely associated with it.

This article has been cited by other articles:

• Schneider, O. D., Weiss, A. A., Miller, W. E. (2007). Pertussis Toxin Utilizes Proximal Components of the T-Cell Receptor Complex To Initiate Signal Transduction Events in T Cells. Infect. Immun. 75: 4040-4049 [Abstract] [Full Text]  
• Latif, R., de Rosbo, N. K., Amarant, T., Rappuoli, R., Sappler, G., Ben-Nun, A. (2001). Reversal of the CD4+/CD8+ T-Cell Ratio in Lymph Node Cells upon In Vitro Mitogenic Stimulation by Highly Purified, Water-Soluble S3-S4 Dimer of Pertussis Toxin. Infect. Immun. 69: 3073-3081 [Abstract] [Full Text]