Potent immunogenicity of the B subunits of Escherichia coli heat-labile enterotoxin: Receptor binding is essential and induces differential modulation of lymphocyte subsets

Nashar, T.O. and Webb, H.M. and Eaglestone, S. and Williams, N.A. and Hirst, T.R. (1996) Potent immunogenicity of the B subunits of Escherichia coli heat-labile enterotoxin: Receptor binding is essential and induces differential modulation of lymphocyte subsets. Proceedings of the National Academy of Sciences of the United States of America, 93 (1). pp. 226-230. ISSN 0027-8424. (The full text of this publication is not available from this repository)

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Abstract

The importance of receptor binding in the potent immunogenicity of Escherichia coli heat-labile enterotoxin B subunit (EtxB) was tested by comparing its immunogical properties with those of a receptor binding mutant, EtxB(G33D). Subcutaneous immunization of EtxB(G33D) resulted in 160-fold reduction in antibody titer compared with wild-type EtxB, whereas its oral delivery failed to provoke any detectable secretory or serum anti-B subunit responses. Moreover, the two proteins induced strikingly different effects on lymphocyte cultures in vitro. EtxB, in comparison with EtxB(G33D), caused an increase in the proportion of B cells, many of which were activated (CD25(+)); the complete depletion of CD8(+) T cells; an increase in the activation of CD4(+) T cells; and an increase in interleukin 2 and a decrease in interferon gamma. These data indicate that EtxB exerts profound effects on immune cells, suggesting that its potent immunogenicity is dependent not only on efficient receptor-mediated uptake, but also on direct receptor-mediated immunomodulation of lymphocyte subsets.

Item Type: Article
Subjects: Q Science > QR Microbiology > QR180 Immunology
Q Science > QR Microbiology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: F.D. Zabet
Date Deposited: 11 Jun 2009 15:37
Last Modified: 11 Jun 2009 15:37
Resource URI: http://kar.kent.ac.uk/id/eprint/18703 (The current URI for this page, for reference purposes)
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