Molecular Properties of Plant Food Allergens: A Current Classification into Protein Families

Hauser, Michael; Egger, Matthias; Wallner, Michael; Wopfner, Nicole; Schmidt, Georg; Ferreira, Fátima

doi:10.2174/1874226200801010001

Cited by 30 publications

(2 citation statements)

References 103 publications

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“…An increase in the number of protein sequence and structural studies has made the creation of systematic and scientific databases possible. It is for this reason that Prolamins, cupins and plant pathogen-related proteins (BetV1) are described as superfamilies, while legumins, vicilins, nsLTPS and albumins are described as families [32]. Some proteins are still not completely classified into any specific groups, such as profilins, expansins and chlorophyll-binding proteins.…”

Section: Structural Studies On Seed Storage Proteinsmentioning

confidence: 99%

Seed Storage Protein, Functional Diversity and Association with Allergy

Jain

2023

Allergies

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Plants are essential for humans as they serve as a source of food, fuel, medicine, oils, and more. The major elements that are utilized for our needs exist in storage organs, such as seeds. These seeds are rich in proteins, show a broad spectrum of physiological roles, and are classified based on their sequence, structure, and conserved motifs. With the improvements to our knowledge of the basic sequence and our structural understanding, we have acquired better insights into seed proteins and their role. However, we still lack a systematic analysis towards understanding the functional diversity associated within each family and their associations with allergy. This review puts together the information about seed proteins, their classification, and diverse functional roles along with their associations with allergy.

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Section: Structural Studies On Seed Storage Proteinsmentioning

confidence: 99%

Seed Storage Protein, Functional Diversity and Association with Allergy

Jain

2023

Allergies

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“…This sequence conservation translates into a high similarity of the structural fold and function within other members of the profilin family [ 5 ]. Conversely, it also results in a broad IgE cross-reactivity of profilin allergic patients to other inhalant and nutritive allergen sources [ 6 ]. However, their sensitizing capabilities remain unclear.…”

Section: Introductionmentioning

confidence: 99%

Two Distinct Conformations in Bet v 2 Determine Its Proteolytic Resistance to Cathepsin S

Soh

Briza

Dall

et al. 2017

IJMS

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Birch pollen allergy affects more than 20% of the European allergic population. On a molecular level, birch pollen allergy can be linked to the two dominant allergens Bet v 1 and Bet v 2. Bet v 2 belongs to the profilin family, which is abundant in the plant kingdom. Importantly, the homologous plant profilins have a conserved cysteine motif with a currently unknown functional relevance. In particular, it is unknown whether the motif is relevant for disulfide formation and to what extent it would affect the profilins’ structural, functional and immunological properties. Here we present crystal structures of Bet v 2 in the reduced and the oxidized state, i.e., without and with a disulfide bridge. Despite overall structural similarity, the two structures distinctly differ at their termini which are stabilized to each other in the oxidized, i.e., disulfide-linked state. These structural differences translate into differences in their proteolytic resistance. Whereas the oxidized Bet v 2 is rather resistant towards the endolysosomal protease cathepsin S, it is rapidly degraded in the reduced form. By contrast, both Bet v 2 forms exhibit similar immunological properties as evidenced by their binding to IgE antibodies from birch pollen allergic patients and by their ability to trigger histamine release in a humanized rat basophilic leukemia cells (RBL) assay, independent of the presence or absence of the disulfide bridge. Taken together our findings suggest that the oxidized Bet v 2 conformation should be the relevant species, with a much longer retention time to trigger immune responses.

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