Isolation and Molecular Characterization of Two Lectins from Dwarf Elder Sambucus ebulus L. Blossoms Related to the Sam n1 AllergenReportar como inadecuado




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1

Nutrition and Food Science, Faculty of Medicine and CINAD Center for Research in Nutrition, Food and Dietetics; Lucia Building-Science Park, University of Valladolid, Valladolid E-47005, Spain

2

Pharmacy and Pharmaceutical Technology, Faculty of Pharmacy and IUFI Institute of Industrial Pharmacy, CAD Center for Research in Nutrition, Food and Dietomplutense University of Madrid, Madrid E-28040, Spain





*

Author to whom correspondence should be addressed.



Abstract Sambucus species contain a number of lectins with and without antiribosomal activity. Here, we show that dwarf elder Sambucus ebulus L. blossoms express two D-galactose-binding lectins that were isolated and purified by affinity chromatography and gel filtration. These proteins, which we named ebulin blo A-B toxin and SELblo B-B lectin—blo from blossoms—were subjected to molecular characterization and analysis by MALDI-TOF mass spectrometry and tryptic peptide fingerprinting. Both lectins share a high degree of amino acid sequence homology with Sambucus lectins related to the Sam n1 allergen. Ebulin blo, but not SELblo, was highly toxic by nasal instillation to mice. Overall, our results suggested that both lectins would belong to an allergen family exemplified by Sam n1 and could trigger allergy responses. Furthermore, they raise a concern about ebulin blo toxicity. View Full-Text

Keywords: Sambucus ebulus; blossoms; lectin; ebulin; ricin; ribosome-inactivating protein Sambucus ebulus; blossoms; lectin; ebulin; ricin; ribosome-inactivating protein





Autor: Pilar Jimenez 1, Patricia Cabrero 1, José E. Basterrechea 1, Jesús Tejero 1, Damian Cordoba-Diaz 2 and Tomas Girbes 1,*

Fuente: http://mdpi.com/



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