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.advisorLopata, Andreasen_ZA
dc.contributor.advisorJeebhay, Mohameden_ZA
dc.contributor.authorBeale, Janineen_ZA
dc.date.accessioned2014-07-28T18:16:02Z
dc.date.available2014-07-28T18:16:02Z
dc.date.issued2008en_ZA
dc.descriptionIncludes abstract.
dc.descriptionIncludes bibliographical references (leaves 101-108).
dc.description.abstractParvalbumin, 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.identifier.apacitationBeale, 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/11427/3223en_ZA
dc.identifier.chicagocitationBeale, 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/11427/3223en_ZA
dc.identifier.citationBeale, 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.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
dc.identifier.urihttp://hdl.handle.net/11427/3223
dc.identifier.vancouvercitationBeale 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/11427/3223en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Human Biologyen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.titleMolecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workersen_ZA
dc.typeMaster Thesis
dc.type.qualificationlevelMasters
dc.type.qualificationnameMScen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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