Robinson, S.A., Smith, J.E. and Millner, P.A. (2004) Toxoplasma gondii major surface antigen (SAG1): in vitro analysis of host cell binding. Parasitology, 128 (4). pp. 391-396. ISSN 0031-1820
Abstract
Previous studies have indicated that SAG1, the major surface molecule of the protozoan parasite Toxoplasma gondii, is an important attachment ligand for the host cell. However, the research data that supports this claim comes largely from studies investigating tachyzoite binding, and not SAG1 binding per se.
In this study we successfully developed an in vitro attachment assay to directly evaluate the mechanism of SAG1-host cell binding. Competition experiments were then performed using SAG1 that had been pre-treated with the neoglycoprotein BSA-glucosamide or with antibody. Soluble BSA-glucosamide blocked SAG1 attachment to MDBK cells in a dose-dependent manner, implying that SAG1 binding is mediated, in part, via attachment to host cell surface glucosamine. Interestingly, pre-incubation of SAG1 in polyclonal sera from chronically infected mice failed to block binding. This challenges the assumption that anti-SAG1 antibodies block parasite attachment through the masking of SAG1 host cell binding domains. Taken together, this evidence presents new strategies for understanding SAG1-mediated attachment.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © Cambridge University Press |
Keywords: | Toxoplasma gondii, attachment, SAG1, glucosamide, antibody |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > Institute of Integrative and Comparative Biology (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > Institute of Membrane and Systems Biology (Leeds) |
Depositing User: | Repository Assistant |
Date Deposited: | 05 Jun 2006 |
Last Modified: | 24 Oct 2016 17:57 |
Published Version: | http://dx.doi.org/10.1017/S0031182003004736 |
Status: | Published |
Publisher: | Cambridge University Press |
Refereed: | Yes |
Identification Number: | 10.1017/S0031182003004736 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:1245 |