{"id":{"repo_id":"cape-town","oai_identifier":"oai:open.uct.ac.za:11427/3223"},"canonical_url":"https://search.dev.ndltd.org/etd/cape-town/oai:open.uct.ac.za:11427/3223","repository":{"repo_id":"cape-town","name":"University of Cape Town","base_url":"https://open.uct.ac.za/oai/request"},"display":{"title":"Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers","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.","abstract_html":"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.","abstract_has_math":false,"creators":["Beale, Janine"],"institution":"Department of Human Biology","degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":["Lopata, Andreas","Jeebhay, Mohamed"],"committee_chairs":[],"committee_members":[],"year":2008,"date_issued":"2008","date_published":"2008","updated_at":"2026-07-22T22:23:01Z","subjects":[],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/11427/3223","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Lopata, Andreas","Jeebhay, Mohamed"]},{"key":"dc:creator","label":"Author","values":["Beale, Janine"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-07-28T18:16:02Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-07-28T18:16:02Z"]},{"key":"dc:date.issued","label":"Date","values":["2008"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Department of Human Biology"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Cape Town"]},{"key":"dc:type","label":"Dc Type","values":["Master Thesis"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["Masters"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["MSc"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/11427/3223"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Includes abstract.","Includes bibliographical references (leaves 101-108)."]},{"key":"dc:description.abstract","label":"Abstract","values":["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."]},{"key":"dc:title","label":"Title","values":["Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers"]}]}],"canonical_facts":{"dc:contributor.advisor":["Lopata, Andreas","Jeebhay, Mohamed"],"dc:creator":["Beale, Janine"],"dc:date.accessioned":["2014-07-28T18:16:02Z"],"dc:date.available":["2014-07-28T18:16:02Z"],"dc:date.issued":["2008"],"dc:description":["Includes abstract.","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? 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