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

Evaluation of the IgE reactivity of common pandora parvalbumin in a Moroccan population and action of heating and enzymatic treatments

“…On the other hand, when IgE immunoreactivity to heated CPP was analyzed by ELISA and dot-blotting, we noted that 95% of patients showed a high reduction in the human IgE binding to CPP, with an average diminution of 41.9%. These results were similar to previous works studying the effect of heating (>80°C ) on the IgE reactivity of parvalbumin extracted from various fish species (Cai et al, 2010;Li, Jiang, You, Luo, & Feng, 2014;Saptarshi et al, 2014; Shibahara, Uesaka, Wang, Yamada, & Shiomi, 2013). Interestingly, a recent study by Kubota et al (2016) found that the IgE reactivity of Pacific mackerel parvalbumin is linearly reduced with the increase in heating temperature, suggesting that more than 50% reduction of IgE reactivity was caused by heating at 80°C and almost complete loss of IgE reactivity by heating at 140°C.…”

“…Concerning the results of heat treatment (90°C), the SDS-PAGE profile showed a parvalbumin band in heated extract CPP, but with a slight decrease in their intensity compared with the original band. Previous studies with SDS-PAGE showed the presence of parvalbumin in heated extracts from various fish species (Kubota, Kobayashi, Kobayashi, Shiomi, & Hamada-Sato, 2016;Saptarshi, Sharp, Kamath, & Lopata, 2014). On the other hand, when IgE immunoreactivity to heated CPP was analyzed by ELISA and dot-blotting, we noted that 95% of patients showed a high reduction in the human IgE binding to CPP, with an average diminution of 41.9%.…”

Immunological cross-reactivity between four distant parvalbumins—Impact on allergen detection and diagnostics

“…Parvalbumins range between 10 and 15 kDa in size and have low isoelectric points ranging from 3.5 to 5. Fish may express multiple parvalbumins (isoforms), which can be seen as monomeric, dimeric or oligomeric forms and may differ significantly in primary structure (Saptarshi et al, 2014;. Although different in parvalbumin primary structure, they have highly conserved tertiary structures and calcium binding residues located on paired ␣-helices (EF-Hand motif) (Arif, 2009).…”

“…Current methods of detecting fish allergens include real-time PCR (Sun et al, 2009) and antibody based assays that detect either fish proteins or the allergens themselves (Faeste and Plassen, 2008;Lopata et al, 2005;Shibahara et al, 2013). The most investigated antibody against parvalbumin is the commercial monoclonal antifrog parvalbumin, PARV-19 (Gajewski and Hsieh, 2009;Saptarshi et al, 2014). This antibody has been evaluated against fish parvalbumins from North America, Europe and Australasia and has been found to cross-react to most but not all parvalbumins (Chen et al, 2006;Lee et al, 2011;.…”

“…Parvalbumin cross-reactivity has been linked with their phylogenetic relationships (Faeste and Plassen, 2008;Saptarshi et al, 2014). In this study, four polyclonal antibodies are generated against parvalbumin from four phylogentically diverse fish species; Atlantic salmon (Samoniformes), barramundi (Perciformes), basa/catfish (Siluriformes) and pilchard (Clupeoformes).…”