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J Agric Food Chem. 2014 Jun 25;62(25):5734-42. doi: 10.1021/jf5007962. Epub 2014 Jun 16.

Overview of plant chitinases identified as food allergens.

Author information

1
Department of Biosciences, Biotechnologies and Biopharmaceutics, University of Bari , Via Amendola 165/A, 70126 Bari, Italy.

Erratum in

  • J Agric Food Chem. 2014 Aug 20;62(33):8541.

Abstract

Food allergies are induced by proteins belonging to a limited number of families. Unfortunately, relationships between protein structure and capacity to induce the immune response have not been completely clarified yet, which precludes possible improvements in the diagnosis, prevention, and therapy of allergies. Plant chitinases constitute a good example of food allergenic proteins for which structural analysis of allergenicity has only been carried out partially. In plants, there are at least five structural classes of chitinases plus a number of chitinase-related polypeptides. Their allergenicity has been mostly investigated for chitinases of class I, due to both their higher prevalence among plant chitinases and by the high structural similarity between their substrate-binding domain and hevein, a well-known allergen present in the latex of rubber trees. Even if allergenic molecules have been identified for at least three other classes of plant chitinases, the involvement of the different structural motifs in the allergenicity of molecules has been disregarded so far. In this review, we provide a structurally based catalog of plant chitinases investigated for allergenicity, which could be a useful base for further studies aimed at better clarifying the structure-allergenicity relationships for this protein family.

PMID:
24841122
DOI:
10.1021/jf5007962
[Indexed for MEDLINE]

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