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Food Chem. 2014 Apr 1;148:321-8. doi: 10.1016/j.foodchem.2013.10.035. Epub 2013 Oct 18.

Antibody reactivity to the major fish allergen parvalbumin is determined by isoforms and impact of thermal processing.

Author information

1
School of Pharmacy and Molecular Science, Centre for Biodiscovery and Molecular Development of Therapeutics, James Cook University, Townsville, Queensland, Australia. Electronic address: shruti.saptarshi@jcu.edu.au.

Abstract

The EF-hand calcium binding protein, parvalbumin, is a major fish allergen. Detection of this allergen is often difficult due to its structural diversity among various fish species. The aim of this study was to evaluate the cross-reactivity of parvalbumin in a comprehensive range of bony and cartilaginous fish, from the Asia-Pacific region, and conduct a molecular analysis of this highly allergenic protein. Using the monoclonal anti-parvalbumin antibody PARV-19, we demonstrated the presence of monomeric and oligomeric parvalbumin in all fish analysed, except for gummy shark a cartilaginous fish. Heat processing of this allergen greatly affected its antibody reactivity. While heating caused a reduction in antibody reactivity to multimeric forms of parvalbumins for most bony fish, a complete loss of reactivity was observed for cartilaginous fish. Molecular analysis demonstrated that parvalbumin cross-reactivity, among fish species, is due to the molecular phylogenetic association of this major fish allergen.

KEYWORDS:

Allergen; Asia-Pacific fish; IgE epitopes; Monoclonal antibody; Parvalbumin; Seafood

PMID:
24262564
DOI:
10.1016/j.foodchem.2013.10.035
[Indexed for MEDLINE]

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