Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M

Do, Thien Van; Hordvik, Ivar; Endresen, Curt; Elsayed, S.

doi:10.1016/j.molimm.2004.09.001

Cited by 55 publications

(45 citation statements)

References 28 publications

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“…To date, only a few kinds of allergens, such as tropomyosin 15 and parvalbumins, 10,11 have been identified in seafood as a major IgE-reactive component, and AK in the shrimp as an allergen has been identified by a few researchers, 13,14,23 but only few reports on the identification of crab AK as another kind of allergen. This is the first report of allergenicity of AK identified from Scylla serrata.…”

Section: Discussionmentioning

confidence: 99%

Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen

et al. 2011

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Section: Discussionmentioning

confidence: 99%

Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen

et al. 2011

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“…The first and best-identified parvalbumin allergen is Gad c 1 from codfish Gadus callarias which has high cross-reactivity between different fish species [6,17]. In subsequent molecular studies, parvalbumin has been identified as major allergen in multiple species of fish, such as salmon [18], Atlantic cod [19], carp [20,21], mackerel [22,23], Alaska pollack [24], blunt snout bream [25] and red stingray [26]. In addition to parvalbumin, within the last several years some studies have identified higher-MW fish allergens, including aldehyde phosphate dehydrogenase [27], collagen [28,29,30], transferrin [31], enolase and creatine kinase [25].…”

Section: Introductionmentioning

confidence: 99%

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Misnan

Murad²,

Meinir³

et al. 2013

Int Arch Allergy Immunol

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Background: The longtail tuna (Thunnus tonggol) is widely consumed in Asia. Parvalbumin, the main major allergen of fish, has been well identified in multiple fish species, yet little is known about the allergenic proteins in T. tonggol. Thus, the aim of this study was to characterize the major allergens of T. tonggol using a proteomics approach. Methods: Raw and boiled extracts of the fish were prepared. Fish proteins were separated by means of SDS-PAGE and two-dimensional (2-DE) electrophoresis. 1-DE immunoblotting of raw extract was performed with sera from fish-allergic patients. Ten sera were further analysed by 2-DE immunoblotting. Selected major allergenic protein spots were excised, trypsin digested and analysed by means of mass spectrometry. Results: SDS-PAGE of raw extract revealed 26 protein fractions, while boiled extract demonstrated fewer bands. The 2-DE gel profile of the raw extract further fractionated the protein bands to more than 100 distinct protein spots. 1-DE immunoblotting of raw extract exhibited two thermolabile protein fractions of 42 and 51 kDa as the major allergens, while the boiled extract only revealed a single IgE-binding band at 151 kDa. 2-DE immunoblotting of raw extract further detected numerous major IgE-reactive spots of 11-13, 42 and 51 kDa. Mass spectrometry analysis of the peptides generated from the 12, 42 and 51 kDa digested spots indicated that these spots were parvalbumin, creatine kinase and enolase, respectively. Conclusions: In addition to parvalbumin, two new thermolabile allergens were identified as major allergenic proteins of T. tonggol. This study proved that both thermostable and thermolabile proteins are important in local tuna allergy and should be included in diagnostic strategies.

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“…Parvalbumins, which are sarcoplasmic proteins, were found in the frozen-thawed fillet exudates because membranes rupture following the formation of ice crystals inside cells during freezing (Morel, 1979;Tironi et al, 2010). These proteins are known as the main fish allergens (Swoboda et al, 2002;Van Do, Hordvik, Endresen, & Elsayed, 2005). Parvalbumin shares similarities in numerous species, possibly indicating that this protein is ubiquitous (Chen, Hefle, Taylor, Swoboda, & Goodman, 2006).…”

Section: Discussionmentioning

confidence: 99%

Differentiation between fresh and frozen–thawed sea bass (Dicentrarchus labrax) fillets using two-dimensional gel electrophoresis

et al. 2015

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This study aimed to identify a protein marker that can differentiate between fresh skinless and frozen-thawed sea bass (Dicentrarchus labrax) fillets using the two-dimensional polyacrylamide gel electrophoresis (2-DE) technique. Distinct gel patterns, due to proteins with low molecular weight and low isoelectric points, distinguished fresh fillets from frozen-thawed ones. Frozen-thawed fillets showed two specific protein spots as early as the first day of the study. However, these spots were not observed in fresh fillets until at least 13days of storage between 0 and 4°C, fillets were judged, beyond this period, fish were unfit for human consumption as revealed by complementary studies on fish spoilage indicators namely total volatile basic nitrogen and biogenic amines. Mass spectrometry identified the specific proteins as parvalbumin isoforms. Parvalbumins may thus be useful markers of differentiation between fresh and frozen-thawed sea bass fillets.

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Characterization of parvalbumin, the major allergen in Alaska pollack, and comparison with codfish Allergen M

Cited by 55 publications

References 28 publications

Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen

Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen

Identification of Parvalbumin and Two New Thermolabile Major Allergens of Thunnus tonggol Using a Proteomics Approach

Differentiation between fresh and frozen–thawed sea bass (Dicentrarchus labrax) fillets using two-dimensional gel electrophoresis

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