Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax

Beale, J, Jeebhay, M and Lopata, A 2009, 'Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax', Molecular Immunology, vol. 46, no. 15, pp. 2985-2993.


Document type: Journal Article
Collection: Journal Articles

Title Characterisation of purified parvalbumin from five fish species and nucleotide sequencing of this major allergen from Pacific pilchard, Sardinops sagax
Author(s) Beale, J
Jeebhay, M
Lopata, A
Year 2009
Journal name Molecular Immunology
Volume number 46
Issue number 15
Start page 2985
End page 2993
Total pages 9
Publisher Pergamon
Abstract IgE-mediated allergic reaction to seafood is a common cause of food allergy including anaphylactic reactions. Parvalbumin, the major fish allergen, has been shown to display IgE cross-reactivity among fish species consumed predominantly in Europe and the and the Far East. However, cross-reactivity studies of parvalbumin from fish species widely consumed in the Southern hemisphere are limited as is data relating to immunological and molecular characterisation. In this study, antigenic cross-reactivity and the presence of oligomers and isomers of parvalbumin from five highly consumed fish species in Southern Africa were assessed by immunoblotting using purified parvalbumin and crude fish extracts. Pilchard (Sardinops sagax) parvalbumin was found to display the strongest IgE reactivity among 10 fish-allergic consumers. The cDNA sequence of the ?-form of pilchard parvalbumin was determined and designated Sar sa 1.0101 (accession number FM177701 EMBL/GenBank/DDBJ databases). Oligomeric forms of parvalbumin were observed in all fish species using a monoclonal anti-parvalbumin antibody and subject's sera. Isoforms varied between approximately 10-13 kDa. A highly cross-reactive allergenic isoform of parvalbumin was identified and sequenced, providing a successful primary step towards the generation of a recombinant form that could be used for diagnostic and potential therapeutic use in allergic individuals.
Subject Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
Keyword(s) Allergen
Fish
IgE
Parvalbumin
Sardinops sagax
DOI - identifier 10.1016/j.molimm.2009.06.018
Copyright notice © 2009 Elsevier Ltd. All rights reserved.
ISSN 0161-5890
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