1H, 13C and 15N resonance assignments and second structure information of Gad m 1: a β-parvalbumin allergen from Atlantic cod (Gadus morhua)

Moraes, Adolfo H.; Ackerbauer, Daniela; Kostadinova, Maria; Bublin, Merima; Ferreira, Fátima; Almeida, Fábio C. L.; Breiteneder, Heimo; Valente, Ana Paula

doi:10.1007/s12104-012-9393-y

Cited by 3 publications

(6 citation statements)

References 9 publications

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“…The solution structure of Gad m 1 was calculated using distance and dihedral angle restraints with Aria 2.3 combined with CNS solve 1.2 . Figure (A) shows the ribbon representation of the structure with the lowest calculated energy, and Figure (B) shows the ensemble of the 20 superimposed lowest energy structures.…”

Section: Resultsmentioning

confidence: 99%

“…All spectra were processed using Topspin 2.1 (Bruker, BioSpin) and analyzed by CCPN (http://www.ccpn.ac.uk/). Resonance assignments were performed using triple resonance experiments as described in Moraes et al …”

Section: Methodsmentioning

confidence: 99%

“…All spectra were processed using Topspin 2.1 (Bruker, BioSpin) and analyzed by CCPN (http://www.ccpn.ac.uk/ ). 18 Resonance assignments were performed using triple resonance experiments as described in Moraes et al 19 The NOE distance restraints were based on 3D-13 Cedited and 15 N-edited NOESY-HSQCs experiments. Semiautomatic NOE assignments were carried out with the Aria 2.3.…”

Section: Structure Calculationmentioning

confidence: 99%

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Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1

et al. 2014

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Beta‐parvalbumins from different fish species have been identified as the main elicitors of IgE‐mediated reactions in fish‐allergic individuals. Here, we report for the first time the NMR determination of the structure and dynamics of the major Atlantic cod (Gadus morhua) allergen Gad m 1 and compare them with other known parvalbumins. Although the Gad m 1 structure and accessibility of putative IgE epitopes are similar to parvalbumins in mackerel and carp, the charge distribution at the putative epitopes is different. The determination of the Gad m 1 structure contributes to a better understanding of cross‐reactivity among fish parvalbumins. In addition, the high‐pressure NMR and temperature variation experiments revealed the important contribution of the AB motif and other regions to the protein folding. This structural information could assist the future identification of hot spots for targeted mutations to develop hypoallergenic Ca2+‐free forms for potential use in immunotherapy. Proteins 2014; 82:3032–3042. © 2014 Wiley Periodicals, Inc.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Structure Calculationmentioning

confidence: 99%

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Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1

et al. 2014

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“…They are typically 10–12 kDa, acidic (p I = 4.0–5.2), and structurally characterized by the presence of three typical helix–loop–helix domains, of which two are capable of binding divalent cations, such as Ca + . The third domain forms a cap that covers the hydrophobic surface of the pair of functional domains. , On the basis of the amino acid sequences, two distinct phylogenetic lineages of parvalbumins, named α and β, have been identified . The β lineage is reported to be especially allergenic, and its IgE binding has been shown to be strongly calcium-dependent …”

Section: Introductionmentioning

confidence: 99%

“…Heat treatment is an important food preparation and preservation procedure. It is required to ensure microbial safety or to obtain desirable organoleptic attributes, improving the appearance, texture, flavor, and taste of products . Parvalbumins are renowned for their strong resistance against heat treatment, associated with the high reversibility in their denaturation in the presence of calcium and other denaturing conditions .…”

Section: Introductionmentioning

confidence: 99%

Electrophoretic Behavior in Relation to the Structural Integrity of Codfish Parvalbumin upon Heat Treatment

Jongh

Jimenez

Baumert³

et al. 2015

J. Agric. Food Chem.

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This work evaluates the impact of heat processing of parvalbumin, a major fish allergen, on the consequences for quantitative analysis of this protein embedded in different matrices during heating (either isolated, in an aqueous extract, or in whole fillets) to assess potential health risks. It is shown that oligomerization of parvalbumin does occur, but only upon heat treatment above 80 °C. This coincides with the ability of the isolated protein to refold up to this temperature in a fully reversible way, as demonstrated by circular dichroism analysis. In autoclaved samples a disintegration of the protein structure is observed. The situation becomes different when parvalbumin is embedded in a matrix with other constituents, as in fish extracts or whole fillets. The electrophoretic analysis of parvalbumin (SDS-PAGE and immunoblotting) is largely determined by complexation with other proteins resulting in insoluble materials caused by the partial unfolding of the parvalbumin at elevated temperatures. This effect is more strongly observed for cod fish extract, compared to whole cod fillets, as in the latter situation the integrity of the tissue hampers this interprotein complexation. Moreover, it is shown by ELISA analysis of heat-treated samples that using blotting procedures where disintegration of complexes may be promoted, restoring some of the IgG-binding propensity, may provide false outcomes. It was concluded that antibody binding to parvalbumin is dominated by the potential to form heat-induced complexes with other proteins. The possibly less-soluble or extractable character of these complexes may provide confusing information regarding potential health risks of fish and fish protein-containing food composites when such heat-treated samples are analyzed by immunochemical assays.

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Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens

Fernandes

Costa

Carrapatoso

et al. 2017

Critical Reviews in Food Science and Nutrition

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Gadiform order includes several fish families, from which Gadidae and Merlucciidae are part of, comprising the most commercially important and highly appreciated fish species, such as cod, pollock, haddock, and hake. Parvalbumins, classified as calcium-binding proteins, are considered the main components involved in the majority of fish allergies. Nine and thirteen parvalbumins were identified in different fish species from Gadidae and Merlucciidae families, respectively. This review intends to describe their molecular characterization and the clinical relevance, as well as the prevalence of fish allergy. In addition, the main protein- and DNA-based methods to detect fish allergens are fully reviewed owing to their importance in the safeguard of sensitized/allergic individuals.

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1H, 13C and 15N resonance assignments and second structure information of Gad m 1: a β-parvalbumin allergen from Atlantic cod (Gadus morhua)

Cited by 3 publications

References 9 publications

Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1

Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1

Electrophoretic Behavior in Relation to the Structural Integrity of Codfish Parvalbumin upon Heat Treatment

Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens

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