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Article

Primary Sequence and 3D Structure Prediction of the Plant Toxin Stenodactylin

1
Department of Biochemistry and Molecular Biology and Physiology, Faculty of Sciences, University of Valladolid, E−47011 Valladolid, Spain
2
Department of Experimental, Diagnostic and Specialty Medicine—DIMES, General Pathology Section, Alma Mater Studiorum—University of Bologna, Via S. Giacomo 14, 40126 Bologna, Italy
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Received: 23 July 2020 / Revised: 17 August 2020 / Accepted: 19 August 2020 / Published: 21 August 2020
(This article belongs to the Special Issue Toxin and Immunotoxin Based Therapeutic Approaches)
Stenodactylin is one of the most potent type 2 ribosome-inactivating proteins (RIPs); its high toxicity has been demonstrated in several models both in vitro and in vivo. Due to its peculiarities, stenodactylin could have several medical and biotechnological applications in neuroscience and cancer treatment. In this work, we report the complete amino acid sequence of stenodactylin and 3D structure prediction. The comparison between the primary sequence of stenodactylin and other RIPs allowed us to identify homologies/differences and the amino acids involved in RIP toxic activity. Stenodactylin RNA was isolated from plant caudex, reverse transcribed through PCR and the cDNA was amplificated and cloned into a plasmid vector and further analyzed by sequencing. Nucleotide sequence analysis showed that stenodactylin A and B chains contain 251 and 258 amino acids, respectively. The key amino acids of the active site described for ricin and most other RIPs are also conserved in the stenodactylin A chain. Stenodactylin amino acid sequence shows a high identity degree with volkensin (81.7% for A chain, 90.3% for B chain), whilst when compared with other type 2 RIPs the identity degree ranges from 27.7 to 33.0% for the A chain and from 42.1 to 47.7% for the B chain. View Full-Text
Keywords: 3D structure; plant toxin; primary sequence; ribosome-inactivating protein; stenodactylin; toxic lectin 3D structure; plant toxin; primary sequence; ribosome-inactivating protein; stenodactylin; toxic lectin
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MDPI and ACS Style

Iglesias, R.; Polito, L.; Bortolotti, M.; Pedrazzi, M.; Citores, L.; Ferreras, J.M.; Bolognesi, A. Primary Sequence and 3D Structure Prediction of the Plant Toxin Stenodactylin. Toxins 2020, 12, 538. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12090538

AMA Style

Iglesias R, Polito L, Bortolotti M, Pedrazzi M, Citores L, Ferreras JM, Bolognesi A. Primary Sequence and 3D Structure Prediction of the Plant Toxin Stenodactylin. Toxins. 2020; 12(9):538. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12090538

Chicago/Turabian Style

Iglesias, Rosario, Letizia Polito, Massimo Bortolotti, Manuela Pedrazzi, Lucía Citores, José M. Ferreras, and Andrea Bolognesi. 2020. "Primary Sequence and 3D Structure Prediction of the Plant Toxin Stenodactylin" Toxins 12, no. 9: 538. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins12090538

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