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   <subfield code="a">10.1007/s00425-014-2191-2</subfield>
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   <subfield code="a">Biological activities of the antiviral protein BE27 from sugar beet ( Beta vulgaris L.)</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Rosario Iglesias, Lucía Citores, Antimo Di Maro, José Ferreras]</subfield>
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   <subfield code="a">Main conclusion : The ribosome inactivating protein BE27 displays several biological activities in vitro that could result in a broad action against several types of pathogens. Beetin 27 (BE27), a ribosome-inactivating protein (RIP) from sugar beet (Beta vulgaris L.) leaves, is an antiviral protein induced by virus and signaling compounds such as hydrogen peroxide and salicylic acid. Its role as a defense protein has been attributed to its RNA polynucleotide:adenosine glycosidase activity. Here we tested other putative activities of BE27 that could have a defensive role against pathogens finding that BE27 displays rRNA N-glycosidase activity against yeast and Agrobacterium tumefaciens ribosomes, DNA polynucleotide:adenosine glycosidase activity against herring sperm DNA, and magnesium-dependent endonuclease activity against the supercoiled plasmid PUC19 (nicking activity). The nicking activity could be a consequence of an unusual conformation of the BE27 active site, similar to that of PD-L1, a RIP from Phytolacca dioica L. leaves. Additionally, BE27 possesses superoxide dismutase activity, thus being able to produce the signal compound hydrogen peroxide. BE27 is also toxic to COLO 320 cells, inducing apoptosis in these cells by either activating the caspase pathways and/or inhibiting protein synthesis. The combined effect of these biological activities could result in a broad action against several types of pathogens such as virus, bacteria, fungi or insects.</subfield>
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   <subfield code="a">Springer-Verlag Berlin Heidelberg, 2014</subfield>
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   <subfield code="a">Antifungal</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Apoptosis</subfield>
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   <subfield code="a">Caspase</subfield>
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   <subfield code="a">Endonuclease</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">N -glycosidase</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Superoxide dismutase</subfield>
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   <subfield code="a">NBT : 4-Nitro blue tetrazolium</subfield>
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   <subfield code="a">SOD : Superoxide dismutase</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">SRL : Sarcin ricin loop</subfield>
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   <subfield code="a">Iglesias</subfield>
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   <subfield code="u">Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain</subfield>
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   <subfield code="u">Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain</subfield>
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   <subfield code="u">Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, 81100, Caserta, Italy</subfield>
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   <subfield code="D">José</subfield>
   <subfield code="u">Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, 47011, Valladolid, Spain</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
   <subfield code="b">Springer special CC-BY-NC licence</subfield>
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