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Engineering single-domain antibodies for bioactive paper applications

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dc.contributor.author Wood, Sarah
dc.date.accessioned 2011-03-29T13:37:29Z
dc.date.available 2011-03-29T13:37:29Z
dc.date.copyright 2011-03
dc.date.created 2010-09-14
dc.date.issued 2011-03-29
dc.identifier.uri http://hdl.handle.net/10214/2529
dc.description.abstract This thesis is an investigation of the fusion of a carbohydrate-binding module (CBM) to a high-affinity single-domain antibody (sdAb) which binds to bacteriophage M13. This fusion protein was applied to paper filters for detection of M13 phage. A CBM-sdAb fusion protein with nanomolar affinity for immobilized M13 phage was successfully expressed in E. coli. The CBM-sdAb fusion protein was effective in binding M13 phage in water to a cellulose filter paper. However, the sdAb and the CBM-sdAb fusion protein were ineffective in enhancing filter capture of M13 phage particles from water or air, respectively. This research demonstrates that a CBM-sdAb fusion protein will bind simultaneously to cellulose and a model virus. In the future, CBM-sdAb fusion proteins may be useful in the development of ‘bioactive’ paper products capable of detecting and/or inactivating pathogens which are a threat to public health. en_US
dc.description.sponsorship NRC Graduate Student Scholarship Supplement Program, NSERC Canada Graduate Scholarship, SENTINEL (Canadian Network for the Development and Use of Bioactive Paper) en_US
dc.language.iso en en_US
dc.title Engineering single-domain antibodies for bioactive paper applications en_US
dc.type Thesis en_US
dc.degree.programme Environmental Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Environmental Biology en_US
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