Epitopic hexapeptide sequences from Baltic cod parvalbumin beta (allergen Gad c 1) are common in the universal proteome

Minkiewicz, Piotr; Bucholska, Justyna; Darewicz, Małgorzata; Borawska, Justyna

doi:10.1016/j.peptides.2012.08.011

Cited by 6 publications

(15 citation statements)

References 64 publications

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“…This fi nding is consistent with the distribution of hexapeptides from Gadus morhua subsp. callarias parvalbumin [Minkiewicz et al, 2012]. The fact that pathogens are the most abundant category among the species synthesising proteins not belonging to the tropomyosin family and containing epitopes from Pen a 1.0102 is also in line with previous fi ndings [Minkiewicz et al, 2012].…”

Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 85%

“…callarias parvalbumin [Minkiewicz et al, 2012]. The fact that pathogens are the most abundant category among the species synthesising proteins not belonging to the tropomyosin family and containing epitopes from Pen a 1.0102 is also in line with previous fi ndings [Minkiewicz et al, 2012]. The presence of the same epitopes in allergens and pathogens should be taken into account during vaccine design, as discussed previously [Minkiewicz et al, 2012].…”

Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 71%

“…The fact that pathogens are the most abundant category among the species synthesising proteins not belonging to the tropomyosin family and containing epitopes from Pen a 1.0102 is also in line with previous fi ndings [Minkiewicz et al, 2012]. The similarity between proteins is also molecular basis of so called hygiene hypothesis assuming that in the case of lack of pathogens, the immune system may be provoked by proteins similar to those originated from pathogens [da Costa Santiago et al, 2013].…”

Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 66%

“…Protein entries in UniProt contain, for example, links to the InterPro domain database [Hunter et al, 2012] and to the Allergome database [Mari et al, 2009] if they are known allergens. The following parameters were applied: the PAM 10 matrix, expected threshold: 1000, data sorting according to high score [Minkiewicz et al, 2012]. The remaining parameters were set at default values.…”

Section: Methodsmentioning

confidence: 99%

“…Only in two cases (FMRFamide-related peptide-like (IPR002544) and uncharacterised protein family, calcium binding protein CcbP (IPR020994) did the percentage of proteins with epitopes from Pen a 1.0102 exceed 1% of proteins containing a domain. Selected species synthesising proteins containing pentapeptide DEERM are organised into categories as described previously [Minkiewicz et al, 2012] (Table 6): edible plants and animals (7 species), microorganisms involved or potentially involved in food technology (2 species), human symbionts and commensals (12 species) as well as human pathogens (18 species). Some species are annotated in two categories: human symbionts and commensals as well as human pathogens.…”

Section: Occurrence Of the Rare Pentapeptidesmentioning

confidence: 99%

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The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

Minkiewicz¹,

Sokołowska²,

Darewicz³

2015

Pol. J. Food Nutr. Sci.

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Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 85%

Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 71%

Section: Occurrence Of the Rare Pentapeptidessupporting

confidence: 66%

Section: Methodsmentioning

confidence: 99%

Section: Occurrence Of the Rare Pentapeptidesmentioning

confidence: 99%

See 3 more Smart Citations

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

Minkiewicz¹,

Sokołowska²,

Darewicz³

2015

Pol. J. Food Nutr. Sci.

Self Cite

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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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The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

Zhang

Liu

et al. 2020

J. Food Biochem.

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Parvalbumin (PV) is one of the major allergens in fish. The aim of our present work was to research the influence mechanism of glycation with different reducing sugars (glucose, fructose, ribose, lactose, and galactose) on the immunoglobulin E (IgE) and immunoglobulin G (IgG) binding capacity and structure changes of PV in Alaska Pollock. PV glycated with glucose or fructose (PV-Glu/ PV-Fru) exhibited the higher IgE/IgG binding capacities than that of ribose, galactose, or lactose. During glycation, the lysine (Lyr), tyrosine (Tyr), and phenylalanine (Phe) of PV were gradually embed into core area of three-dimensional structure of protein, which reflected in the ultraviolet (UV) spectrum and fluorescence spectra. Moreover, the increase of surface hydrophobicity had confirmed the conformation alteration of glycated PV. These results suggest that there is a specific association among the change of PV in glycation and in potential allergenicity. The types and conformation of reducing sugar greatly influenced the IgE/IgG binding capacity of PV, and glycation with ribose and galactose was a promising approach for reducing the IgE/IgG binding capacity of PV from Alaska Pollock. Practical applications Parvalbumin (PV), the major allergen of fish, it can not only maintain the physiological activity of cells, but also cross react with human amyloid protein to alleviate Alzheimer's disease and Parkinson's syndrome. This study revealed that the IgE/IgG binding capacity and structural changes of PV from Alaska Pollock modified by glycation with different reducing sugars. This will help us to understand the sensitization and structural change of the glycated products after the reaction of PV with different reducing sugars. It provides an effective carbonyl source for the preparation of low antigenicity PV based on glycation and lays a foundation for glycation modification of other food allergens.

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Epitopic hexapeptide sequences from Baltic cod parvalbumin beta (allergen Gad c 1) are common in the universal proteome

Cited by 6 publications

References 64 publications

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

The Occurrence of Sequences Identical with Epitopes from the Allergen Pen a 1.0102 Among Food and Non-Food Proteins

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

The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

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