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The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen

Includes abstract.

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Main Author: Lagardien, Zaida
Other Authors: Blackburn, Jonathan
Format: Thesis
Language:English
Published: Division of Medical Biochemistry 2014
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access_status_str Open Access
author Lagardien, Zaida
author2 Blackburn, Jonathan
author_browse Blackburn, Jonathan
Lagardien, Zaida
author_facet Blackburn, Jonathan
Lagardien, Zaida
author_sort Lagardien, Zaida
collection Thesis
description Includes abstract.
format Thesis
id oai:open.uct.ac.za:11427/3136
institution University of Cape Town (South Africa)
language eng
last_indexed 2026-06-10T12:40:59.889Z
license_str Not specified — see source repository
provenance_str_mv Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository
publishDate 2014
publishDateRange 2014
publishDateSort 2014
publisher Division of Medical Biochemistry
publisherStr Division of Medical Biochemistry
record_format dspace
source_str UCTD — University of Cape Town Open Access Repository
spelling oai:open.uct.ac.za:11427/3136 The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen Lagardien, Zaida Blackburn, Jonathan Medical Biochemistry Includes abstract. Includes bibliographical references. Peanut agglutinin (PNA), a carbohydrate binding protein, is able to recognise and bind a number of distinct carbohydrate structures that have been implicated in a number of disease pathologies in humans. In vitro studies of PNA have previously been shown to have some specificity for the Thomson Freidenriech antigen (T-antigen), found on malignant human cells, and this specificity has made PNA an important target for protein engineering experiments aimed at improving its specificity and affinity. A number of tumour cells are characterised by altered states and patterns of glycosylation on cell surfaces and suitably engineered lectins may be able to recognise tumour specific carbohydrate structures. This study was aimed at carrying out the biophysical characterisation of a set of PNA mutants which showed apparent improvement in specificity for the T-Antigen. Previous studies have aimed to engineer this lectin in order to direct its recognition properties towards the T-antigen and away from lactose, the preliminary binding affinities of these mutants being determined using Surface Plasmon Resonance (SPR). Here a set of PNA mutants were characterised, proteins expressed and purified to determine binding activities to the T-antigen, N-Acetyl-Dlactosamine (LacNAc) and lactose through the use of Protein Micro Array technology as well as Enzyme linked immunosorbant assays (ELISA). 2014-07-28T14:55:34Z 2014-07-28T14:55:34Z 2013 Master Thesis Masters MSc http://hdl.handle.net/11427/3136 eng application/pdf Division of Medical Biochemistry Faculty of Health Sciences University of Cape Town
spellingShingle Medical Biochemistry
Lagardien, Zaida
The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
thesis_degree_str Master's
title The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
title_full The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
title_fullStr The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
title_full_unstemmed The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
title_short The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen
title_sort characterisation of the peanut agglutinin an evolved plant lectin with improved specificity to the thompson freidenriech antigen
topic Medical Biochemistry
url http://hdl.handle.net/11427/3136
work_keys_str_mv AT lagardienzaida thecharacterisationofthepeanutagglutininanevolvedplantlectinwithimprovedspecificitytothethompsonfreidenriechantigen
AT lagardienzaida characterisationofthepeanutagglutininanevolvedplantlectinwithimprovedspecificitytothethompsonfreidenriechantigen