Seaweeds early development: detrimental effects of desiccation and attenuation by algal extracts.

The effects of desiccation on the early development stages of Mazzaella laminarioides, Scytosiphon lomentaria and Lessonia nigrescens, algal species with different patterns of distribution across the intertidal zone, were examined in the laboratory. In addition, the protective effect against desiccation was evaluated using algal extracts, including those from Porphyra columbina, a macroalga tolerant to desiccation that lives in the uppermost part of the intertidal zone. Our results showed that M.

Expression of Jug r 1, the 2S albumin allergen from walnut (Juglans regia), as a correctly folded and functional recombinant protein.

Jug r 1, the 2S albumin allergen from walnut, was isolated from ripe nuts as a native allergen and expressed in Escherichia coli using the Gateway technology as a recombinant allergen. The recombinant Jug r 1 (15 kDa) differs from the native allergen by the absence of cleavage of the polypeptide chain in two covalently associated light (3.5 kDa) and heavy (8 kDa) chains.

IgE-binding epitopic peptide mapping on a three-dimensional model built for the 13S globulin allergen of buckwheat (Fagopyrum esculentum).

The three-dimensional model built for the 13S globulin allergen of buckwheat (Fagopyrum esculentum) consists of three protomers exhibiting the cupin motif, arranged in a homotrimer around a three-fold symmetry axis. Using the SPOT technique, 11 continuous IgE-binding epitopic peptides were characterized on the molecular surface of the 13S globulin allergen of buckwheat. Except for one of them, they all correspond to well exposed regions containing electropositiveley and/or electronegatively charged residues, which cover up to 40% of the molecular surface of the allergen.

Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes.

Surface-exposed IgE-binding epitopes of close overall conformation were characterized on the molecular surface of three-dimensional models built for the vicilin allergens of peanut (Ara h 1), walnut (Jug r 2), hazelnut (Cor a 11) and cashew nut (Ana o 1). They correspond to linear stretches of conserved amino acid sequences mainly located along the C-terminus of the polypeptide chains. A glyco-epitope corresponding to an exposed N-glycosylation site could also interfere with the IgE-binding epitopes.

Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts.

Linear IgE-binding epitopes identified in legumin allergens of peanut (Ara h 3) and other allergenic tree nuts (Jug r 4 of walnut, Cor a 9 of hazelnut, Ana o 2 cashew nut) were mapped on three-dimensional models of the proteins built up by homology modelling. A conformational analysis revealed that consensual surface-exposed IgE-binding epitopes exhibited some structural homology susceptible to account for the IgE-binding cross-reactivity observed among peanut and tree nut allergens. This structurally related cross-reactivity seems irrespective of the botanical origin of the allergens and thus demands that persons allergic to peanut avoid other three nuts to prevent possible allergic reactions.