Characteristic motifs for families of allergenic proteins

Ivanciuc, Ovidiu; Garcia, Tzintzuni; Torres, Miguel; Schein, Catherine H.; Braun, Werner

doi:10.1016/j.molimm.2008.07.034

Cited by 72 publications

(66 citation statements)

References 86 publications

(121 reference statements)

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“…The advances in bioinformatics enabled the classification of allergens into protein families, which was performed by several researchers using different methods, but reaching similar conclusions [12,15,52,53,54]. It turned out that most allergens belonged to a surprisingly small number of protein families.…”

Section: Allergen Databasesmentioning

confidence: 99%

Navigating through the Jungle of Allergens: Features and Applications of Allergen Databases

Radauer

2017

Int Arch Allergy Immunol

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The increasing number of available data on allergenic proteins demanded the establishment of structured, freely accessible allergen databases. In this review article, features and applications of 6 of the most widely used allergen databases are discussed. The WHO/IUIS Allergen Nomenclature Database is the official resource of allergen designations. Allergome is the most comprehensive collection of data on allergens and allergen sources. AllergenOnline is aimed at providing a peer-reviewed database of allergen sequences for prediction of allergenicity of proteins, such as those planned to be inserted into genetically modified crops. The Structural Database of Allergenic Proteins (SDAP) provides a database of allergen sequences, structures, and epitopes linked to bioinformatics tools for sequence analysis and comparison. The Immune Epitope Database (IEDB) is the largest repository of T-cell, B-cell, and major histocompatibility complex protein epitopes including epitopes of allergens. AllFam classifies allergens into families of evolutionarily related proteins using definitions from the Pfam protein family database. These databases contain mostly overlapping data, but also show differences in terms of their targeted users, the criteria for including allergens, data shown for each allergen, and the availability of bioinformatics tools.

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Section: Allergen Databasesmentioning

confidence: 99%

Navigating through the Jungle of Allergens: Features and Applications of Allergen Databases

Radauer

2017

Int Arch Allergy Immunol

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“…Allergens from this group are formed by seven antiparallel -strands and three a-helices. Besides, they also share a C-terminal amphipathic helical motif, which consists of a helix (Ivanciuc et al, 2009). This family is classified by sequence similarity into three sub-families: pathogenesis-related (PR)-10, Bet v 1 major allergen, and ripening-related (RRP) proteins (Ivanciuc et al, 2009).…”

Section: Bioinformatics Analysis and Classification Of The Test Food mentioning

confidence: 99%

“…Besides, they also share a C-terminal amphipathic helical motif, which consists of a helix (Ivanciuc et al, 2009). This family is classified by sequence similarity into three sub-families: pathogenesis-related (PR)-10, Bet v 1 major allergen, and ripening-related (RRP) proteins (Ivanciuc et al, 2009). PR-10 includes a majority of allergens in those three sub-families (Wen et al, 1997).…”

Section: Bioinformatics Analysis and Classification Of The Test Food mentioning

confidence: 99%

Food proteins from different allergen families sensitize Balb/c mice to family-specific immune responses

Wang

Sun

Zhou

et al. 2013

Journal of Immunotoxicology

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The classification of food allergens based on the structure and function of proteins contributes to the study of the relationship between bioinformatics and potential allergenicity of allergens. Food allergens always share sequence similarity with the allergens in the same allergen families. For that reason, food proteins from different allergen families may induce different patterns of immune responses in animal models. Female Balb/c mice (3-4-weeks-old) were sensitized with food proteins once per week for 4 weeks, and then challenged 2 weeks later (on Day 42 of study). Blood was collected (to obtain serum levels of histamine and protein-specific IgG 1 and IgE antibodies) and measures of vascular permeability were performed 20 min after the challenge. Five food proteins (11S globulin, OVA [ovalbumin], HAS [human serum albumin] and LRP [lysine-responsive storage protein] of different allergen families, and Cry 1Ab/Ac [crystal protein]) were used to assess patterns of immune responses for each allergen family and then bioinformatics and digestive stability in simulated gastric fluid were employed to assess the overall utility of the Balb/c. The assay results indicated that, in this model, histamine and protein-specific IgE antibody levels and vascular permeability could be used to identify allergenicity of 11S globulin, OVA, and PAP (potato acid phosphatase) only. However, the results of the protein-specific IgG 1 measures could only distinguish allergic food proteins with negative control. Based on bioinformatic analyses, the five different food proteins clearly induced distinct patterns of immune responses in the Balb/c model.

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“…The other allergen database that utilizes the Pfam protein family information is Motifmate (http://born.utmb.edu/motifmate/index.php) (Ivanciuc et al, 2009a). Motifmate assigns pfam domains to the allergens listed in the SDAP (Structural Database of Allergenic Proteins) database developed and maintained by the University of Texas (http://fermi.utmb.edu/SDAP) (Ivanciuc et al, 2003).…”

Section: Allergen-associated Protein Domainsmentioning

confidence: 99%