Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers

 

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dc.contributor.advisor Lopata, Andreas en_ZA
dc.contributor.advisor Jeebhay, Mohamed en_ZA
dc.contributor.author Beale, Janine en_ZA
dc.date.accessioned 2014-07-28T18:16:02Z
dc.date.available 2014-07-28T18:16:02Z
dc.date.issued 2008 en_ZA
dc.identifier.citation Beale, J. 2008. Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers. University of Cape Town. en_ZA
dc.identifier.uri http://hdl.handle.net/11427/3223
dc.description Includes abstract.
dc.description Includes bibliographical references (leaves 101-108).
dc.description.abstract Parvalbumin, the fish major allergen, accounts for over 95% of clinical symptoms in allergic fish consumers. Importantly, this allergen displays lgE cross-reactivity thus allergic sufferers can exhibit clinical symptoms after the ingestion of non-sesitising fish species. In an occupational setting, fish products have also been shown to cause allergic disease in fish-processing factory workers. Whether parvalbumin is a causative allergen in this occupational environment is unknown. The aim of this study was to evaluate IgE reactivity to parvalbumin and other fish fillet proteins using sera from domestic consumers with ingestion-induced fish allergies and sera from occupationally exposed allergic workers. In addition, cross-reactivity among parvalbumins from five highly consumed fish species in South Africa were assessed by immunoblotting and the most cross-reactive species was characterised further. Pilchard parvalbumin was identified as the most cross-reactive allergen in fish-allergic consumers. The cDNA sequenceß form of pilchard parvalbumin was determined. This is the first time that parvalbumin from the fish order, Clupeiformes, has been characterised and represents a crucual primary step towards the generation of a recombinant form for potential diagnostic and therapeutic use in allergic individuals. Interestingly, sera IgE from fish-processing factory workers displayed no bing to parvalbumin, nor any other fish fillet proteins in immunoblotting. This result has raised several intriguing questions. Namely, does parvalbumin lack the intrinsic features required for eliciting allergic symptoms via inhalation and/or contact, as are primary routes of exposure in workers? Alternatively, could causative occupational allergens that appear to be absent in the fillet of fish occur in the enzyme-rich digestive tract or potentially the skin of fish species? Future studies aim to addess these questions amongst others, which will contribute to preventative and therapeutic strategies of occupational allergies in workers. en_ZA
dc.language.iso eng en_ZA
dc.title Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers en_ZA
dc.type Master Thesis
uct.type.publication Research en_ZA
uct.type.resource Thesis en_ZA
dc.publisher.institution University of Cape Town
dc.publisher.faculty Faculty of Health Sciences en_ZA
dc.publisher.department Department of Human Biology en_ZA
dc.type.qualificationlevel Masters
dc.type.qualificationname MSc en_ZA
uct.type.filetype Text
uct.type.filetype Image
dc.identifier.apacitation Beale, J. (2008). <i>Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Department of Human Biology. Retrieved from http://hdl.handle.net/11427/3223 en_ZA
dc.identifier.chicagocitation Beale, Janine. <i>"Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Department of Human Biology, 2008. http://hdl.handle.net/11427/3223 en_ZA
dc.identifier.vancouvercitation Beale J. Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Department of Human Biology, 2008 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/3223 en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Beale, Janine AB - Parvalbumin, the fish major allergen, accounts for over 95% of clinical symptoms in allergic fish consumers. Importantly, this allergen displays lgE cross-reactivity thus allergic sufferers can exhibit clinical symptoms after the ingestion of non-sesitising fish species. In an occupational setting, fish products have also been shown to cause allergic disease in fish-processing factory workers. Whether parvalbumin is a causative allergen in this occupational environment is unknown. The aim of this study was to evaluate IgE reactivity to parvalbumin and other fish fillet proteins using sera from domestic consumers with ingestion-induced fish allergies and sera from occupationally exposed allergic workers. In addition, cross-reactivity among parvalbumins from five highly consumed fish species in South Africa were assessed by immunoblotting and the most cross-reactive species was characterised further. Pilchard parvalbumin was identified as the most cross-reactive allergen in fish-allergic consumers. The cDNA sequenceß form of pilchard parvalbumin was determined. This is the first time that parvalbumin from the fish order, Clupeiformes, has been characterised and represents a crucual primary step towards the generation of a recombinant form for potential diagnostic and therapeutic use in allergic individuals. Interestingly, sera IgE from fish-processing factory workers displayed no bing to parvalbumin, nor any other fish fillet proteins in immunoblotting. This result has raised several intriguing questions. Namely, does parvalbumin lack the intrinsic features required for eliciting allergic symptoms via inhalation and/or contact, as are primary routes of exposure in workers? Alternatively, could causative occupational allergens that appear to be absent in the fillet of fish occur in the enzyme-rich digestive tract or potentially the skin of fish species? Future studies aim to addess these questions amongst others, which will contribute to preventative and therapeutic strategies of occupational allergies in workers. DA - 2008 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2008 T1 - Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers TI - Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers UR - http://hdl.handle.net/11427/3223 ER - en_ZA


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