bassianolide and Food-Hypersensitivity

Parvalbumin (PV) is the most common allergen in fish. Some patients with fish allergy are allergic to only one species of fish but are tolerant to others; however, the underlying mechanism has not been identified. This study showed that three types of glycated fishes' PV showed a similar decrease in immunoglobulin E (IgE) binding. Glycosylation could improve the simulated gastric fluid (SGF) and simulated intestinal fluid (SIF) digestion resistance of fishes' PV. We also discovered that the cross-reactivity between eel and turbot was weaker than that of bass; glycosylation can reduce cross-reactivity between eel/bass and turbot by downregulating Th2 cytokines and upregulating Th1 cytokines as well as downregulating the expression of G-T PV, G-E PV, G-B PV of IL-4 (94.31 ± 3.16, 73.26 ± 0.91, 94.95 ± 3.03 ng/mL), and IL-13 (38.84 ± 0.75, 33.77 ± 0.71, 36.51 ± 0.50 ng/mL) and upregulating the expression of IFN-γ (318.01 ± 3.46, 387.15 ± 3.30, 318.01 ± 4.21 ng/mL) compared with T PV, respectively. This study showed that glycosylation affected sensitization by regulating the cross-reactivity of parvalbumins.

Topics: Allergens; Animals; Bass; Cytokines; Eels; Flatfishes; Food Hypersensitivity; Glycosylation; Parvalbumins

Fish allergy is a common food allergy, with prevalence rates in the general population ranging between 0.2% and 2.3%. In both adults and children fish ranks in the top eight foods known to cause IgE mediated food allergy. Fish allergy is rarely outgrown and individuals with fish allergy may be allergic to some but not all species of fish. Whilst fish allergy occurs around the world, the characterization of allergenic components of individual species of fish has been largely confined to Northern hemisphere and European fish species. To date allergy to commonly consumed fish in the Asian-Pacific region including barramundi (Asian seabass; Lates calcarifer) have been less well investigated. The aim of this study was to identify and characterize allergenic proteins from barramundi in both fish allergic adult and pediatric patients. Serum from 17 fish allergic adults and children from Australia were characterized by immunoblotting and enzyme linked immunosorbent assays (ELISA) against raw and heated barramundi. Molecular analysis of identified allergens included genetic sequencing and generation of recombinant isoallergens. Two novel parvalbumin isoforms of the β-type were identified as the only allergens in barramundi and subsequently designated as Lat c 1.0101 and Lat c 1.0201 by the International Union of Immunological Societies. These two isoallergens do not differ in their ability to bind IgE antibodies, but are differentially expressed in barramundi tissue. This study characterized two novel heat stable parvalbumin allergens from barramundi, with differential IgE binding capacity between adults and pediatric patients.

Topics: Adult; Allergens; Amino Acid Sequence; Animals; Bass; Child; Female; Fish Proteins; Food Hypersensitivity; Humans; Immunoglobulin E; Male; Models, Molecular; Molecular Sequence Data; Parvalbumins; Protein Binding; Protein Conformation; Sequence Homology, Amino Acid