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. laminarioides displayed the highest resistance to daily desiccation, followed by S. lomentaria, whereas L. nigrescens was the most susceptible. Spores from L. nigrescens exposed to desiccation, although being able to germinate, ceased further post-germination development. In addition, our results showed that all species exposed to extracts from desiccated P. columbina successfully completed their development and strongly suggest the occurrence of compounds with protective properties that help in attenuating the stress caused by desiccation. Finally, our results indicate that the magnitude of the effects generated by desiccation on the early algal development is related to the position of the species in the intertidal zone, and that the protective effects of P. columbina extracts reveal an exceptional metabolism of this species under desiccation stress.

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. Some of these epitopes come in close contact to probably create more extended discontinuous epitopes, especially those located on the edge of the 13S globulin homotrimer. Half of the identified epitope peptides remain unaltered in a core structure protected against hydrolysis by digestive proteases and are thus assumed to promote the allergenicity of the 13S globulin. In addition, a few of these epitopes coincide with sequential IgE-binding epitopes previously characterized in soybean 11S globulins, that could account for the IgE-binding cross-reactions observed between soybean and buckwheat in Western blot experiments.