Thesis

Investigation of preferential binding properties of monoclonal antibodies M1:1D2 and H4:4 towards the conformers of recombinant prion protein

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Awarding institution
  • University of Strathclyde
Date of award
  • 2010
Thesis identifier
  • T12764
Qualification Level
Qualification Name
Department, School or Faculty
Abstract
  • Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc.
Resource Type
Note
  • This thesis was previously held under moratorium from 10th May 2011 until 10th May 2015.
DOI
Alternative Title
  • Investigation of preferential binding properties of mAbs M1:1D2 and H4:4 towards the conformers of recombinant prion protein
Date Created
  • 2010
Former identifier
  • 821695

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