Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels

Hamada, Yuki; Tanaka, Hiroyuki; Ishizaki, Shoichiro; Ishida, Masami; Nagashima, Yuji; Shiomi, Kazuro

doi:10.1016/s0278-6915(03)00074-7

Cited by 85 publications

(59 citation statements)

References 24 publications

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“…CPP was extracted as previously described, with modifications Hamada, Tanaka, et al, 2003). Briefly, the raw common pandora muscle was defatted with chloroform to remove lipids.…”

Section: Extraction Of Cppmentioning

confidence: 99%

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

Mejrhit

Azdad

Aarab

2017

Food and Agricultural Immunology

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The aim of this study was to evaluate the immunoglobulin E (IgE) sensitivity to common pandora (Pagellus erythrinus) parvalbumin (CPP) in a Moroccan population from the Fez region, and then to study the effect of temperature and enzymatic digestion on the allergenicity of CPP. This work was conducted with a questionnaire completed by a sera-bank, obtained from 500 patients recruited from Fez hospitals. Their sera were analyzed for specific IgE against CPP. Evaluation of specific IgE showed that 11.8% of patients present higher values (>150 IU/ml). Further indirect ELISA and dot-blot results indicated that CPP showed a decrease in the binding of anti-IgE under heating with an average diminution of 41.9%, while pepsin hydrolysis reduced IgE recognition by 22.9%. These results demonstrate that this population was sensitive to CPP and the sensitivity could be reduced by heating and pepsin hydrolysis with an action higher with temperature than enzymatic digestion processing. ARTICLE HISTORY

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“…CPP was extracted as previously described, with modifications Hamada, Tanaka, et al, 2003). Briefly, the raw common pandora muscle was defatted with chloroform to remove lipids.…”

Section: Extraction Of Cppmentioning

confidence: 99%

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

Mejrhit

Azdad

Aarab

2017

Food and Agricultural Immunology

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“…Cod has been mentioned above. Hamada et al (2003) demonstrate that parvalbumin is a major allergen in three species of mackerels (Scomber japonicus, S. australasicus and S. scombrus) said to be the fish most frequently involved in IgE-mediated food allergy in Japan. Based on amino acid sequence data, the parvalbumin protein family can be subdivided into two evolutionary distinct lineages: the α group and the β group.…”

Section: Fish Musclementioning

confidence: 94%

“…In another study, all out of 30 sera from patients allergic to fish displayed reactivity to parvalbumin. Four of five sera from fish allergic patients reacted to all parvalbumins isolated from three species of mackerel (Hamada et al, 2003).…”

Section: Serological and Skin Prick Test Cross-reactivitymentioning

confidence: 99%

Opinion of the Scientific Panel on Dietetic products, nutrition and allergies [NDA] on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes

2004

EFS2

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“…Moreover, the major IgE epitope of the bovine collagen a2 chain has been elucidated to reside in region 485ῌ494 5) . In fish, the major allergen is parvalbumin, a calciumbinding sarcoplasmic protein with a molecular mass of about 12 kDa, as demonstrated with various species of fish, including cod 6) , carp 7) , Atlantic salmon 8) and Pacific mackerel 9) . Besides parvalbumin, collagen has also been identified as a fish allergen, although not a major one 10), 11) .…”

Section: Introductionmentioning

confidence: 94%

A Major IgE Epitope of Rainbow Trout Collagen α2 Chain

Shiomi¹,

Yoshida²,

Sawaguchi³

et al. 2010

Journal of the Food Hygienics Society of Japan

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Bovine collagen is allergenic and its major IgE epitope has already been identified. Fish collagen is also allergenic but shows no IgE cross-reactivity with bovine collagen, implying that it has specific IgE epitopes. Therefore, this study was initiated to elucidate IgE epitopes of rainbow trout collagen a2 chain. Five overlapping proteins (R1ῌ5; 221 or 225 amino acids long with an o#set of 205 amino acids) covering the entire sequence of the rainbow trout collagen a2 chain were expressed in Escherichia coli. Immunoblotting experiments using 10 patients' sera reacting to fish collagen revealed that the major IgE epitope is included in the R5 protein (region 821ῌ 1,041). Then, 26 overlapping peptides (20 or 21 amino acids long with an o#set of 8 amino acids) encompassing the sequence of the R5 protein were chemically synthesized and examined for IgE-binding ability by fluorescence ELISA. Region 941ῌ960 was found to be most IgE-reactive. When evaluated by inhibition ELISA, this region accounted for more than 50ῌ of the IgE reactivity to the R5 protein. Moreover, the same region was found to be IgE-reactive in bastard halibut and zebrafish collagen a2 chains, but not in bovine collagen a2 chain. Our results strongly suggest that region 941ῌ960 is a major common IgE epitope of fish collagen a2 chains.

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Purification, reactivity with IgE and cDNA cloning of parvalbumin as the major allergen of mackerels

Cited by 85 publications

References 24 publications

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

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

Opinion of the Scientific Panel on Dietetic products, nutrition and allergies [NDA] on a request from the Commission relating to the evaluation of allergenic foods for labelling purposes

A Major IgE Epitope of Rainbow Trout Collagen α2 Chain

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