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Grass pollen allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Increasingly more sensitive analyses of complex allergen sources are being employed for standardizing allergen extracts [136,23]. Proteomic studies incorporating combinations of two-dimensional immunoelectrophoresis, mass spectrometry, and sophisticated computer software not only allow for the quantitation of specific isoforms of known allergens but also permit identification of the presence of additional IgE-reactive components in grass pollen. For example, a shotgun proteomic analysis of ryegrass pollen extract and immunoblotting pollen proteins separated by two-dimensional electrophoresis revealed the presence of novel IgE-reactive proteins that might be involved in polysensitization [137]. Cyclophilin (peptidyl-prolyl cis-trans isomerase), fructosyltransferase, an enzyme with invertase activity and multiple putative N-glycosylation sites, and legumin-like protein belonging to the Cupin superfamily were identified as potential allergens. Another proteomic study of timothy grass pollen allergens isolated from pollen and pollen cytoplasmic granules (PCGs) identified up to six novel IgE-binding proteins including ascorbate reductase and triosephosphate isomerase in pollen and PCGs; a ß-glucosidase in pollen only; and cinnamyl alcohol dehydrogenase, legumin-like protein, and UDP-glucose pyrophosphorylase in PCGs only [138]. The clinical significance of these IgE-reactive proteins is yet to be established.
Nutritional Attributes of Cereal Grains And Legumes as Functional Food: A Review
Published in Megh R. Goyal, Durgesh Nandini Chauhan, Plant- and Marine-Based Phytochemicals for Human Health, 2018
Vikas Dadwal, Himani Agrawal, Shriya Bhatt, Robin Joshi, Mahesh Gupta
Three main isoflavones present in soybean are: daidzein, genistein, and glycitein. Conjugated aglycones comprise esterified 6″-O-malonylβ-glycosides, 6″-O-acetyl-β-glycosides, and β-glycosides; and it includes a total of 12 isoflavones.83 Phytoestrogens present in it exhibit antiproliferative activities and also regulate the immune system.28, 85 Despite the presence of various bioactive compounds, it has anti-nutritional effects.127 Soybean is anti-allergic, affecting almost 0.4% of children and 0.25% of adults.135 The Food and Agriculture Organization has listed it as one of the eight most common allergenic foods.126 Soybean contains various allergenic glycol proteins that lead to various allergic symptoms such as eczema, atopic dermatitis, and asthma. Several soybean allergens have been classified into families such as cupin superfamily, prolamin superfamily, pathogenesis-related proteins, and profilins.5, 126, 153
Biomolecular and Clinical Aspects of Food Allergy
Published in Andreas L. Lopata, Food Allergy, 2017
At present, the cupin superfamily contains 57 families. The members of this superfamily possess one or more conserved cupin domain, a characteristic β-barrel (Latin cupa = barrel) that evolved in a prokaryotic organism and was then passed on into the plant kingdom (Khuri et al. 2001). The cupin domain is used for a large number of biological functions and is found in fungal spherulins that are produced upon spore formation, in proteins that bind saccharose, or in germins whose function depends on the binding of manganese ions by the cupin domain (Dunwell et al. 2000). Cupins are highly thermostable, a trait that has most likely evolved in thermophilic archaea and that can still be found in today’s plant food allergens. The cupin domain was duplicated in flowering plants giving rise to the so-called bicupin seed storage proteins (Dunwell and Gane 1998), the 7S and 11S globulins which are described as major allergens of peanut, tree nuts and various seeds (Mills et al. 2002, Radauer and Breiteneder 2007, Willison et al. 2014). The cupin seed storage proteins are primarily an energy source and provide amino acids during seed germination. In addition, they are also involved in the defense of many plant species against fungi and insects (Candido Ede et al. 2011).
The complex barnacle perfume: identification of waterborne pheromone homologues in Balanus improvisus and their differential expression during settlement
Published in Biofouling, 2019
Anna Abramova, Ulrika Lind, Anders Blomberg, Magnus Alm Rosenblad
Except for the relatively high sequence identity to WSP from B. amphitrite, the WSP homologues in B. improvisus did not have any reliable matches to other proteins in the databases. However, all B. improvisus WSP homologues contained a region with weak resemblance to the cupin_5 domain (PF06172) (Table S2). Cupin_5 is a domain of unknown function, and proteins containing this domain belong to the cupin superfamily (http://www.ebi.ac.uk/interpro/entry/IPR009327). In the Pfam database, for metazoans there are currently only 17 sequences from 10 species indicated to have a cupin_5 domain. Among these sequences, the scores for the predicted cupin_5 domain varied from 41.3 to 139.2 with the only two crustacean representatives having scores of 70.5 or 78.7, both coming from Daphnia (see Table S3 in Supplemental material). The Pfam cupin_5 domain scores for the B. improvisus WSP homologues varied between 19.8 and 36.3, with some of them thus being below the Pfam cupin_5 profile threshold score of 25.0 (Table S2). However, proteins with higher cupin_5 Pfam scores in both B. improvisus and B. amphitrite (with scores 45.4 and 46.0) were found, and these were named Bi_cupin and Ba_cupin, respectively. The Bi_cupin sequence was only 15% identical to Bi_WSP. Even if some of the WSP homologues in B. improvisus have a domain with weak similarity (slightly above the threshold score) to cupin_5, for the ease of the following discussion only proteins with high domain scores, ie Bi_cupin, Ba_cupin and Daphnia cupin_5, will be referred to as ‘cupin_5 proteins’ further in the text.