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Report of the 1st International Electronic Conference on Toxins (IECT2021), 16–31 January 2021
Article

Short Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2

1
Department of Biomedical Sciences, University of Padova, Via U. Bassi, 58/B, 35131 Padova, Italy
2
CNR of Italy, Neuroscience Institute, viale G. Colombo 3, 35131 Padova, Italy
*
Author to whom correspondence should be addressed.
Received: 8 March 2021 / Revised: 14 April 2021 / Accepted: 16 April 2021 / Published: 20 April 2021
Snake venom phospholipases A2 (PLA2s) have sequences and structures very similar to those of mammalian group I and II secretory PLA2s, but they possess many toxic properties, ranging from the inhibition of coagulation to the blockage of nerve transmission, and the induction of muscle necrosis. The biological properties of these proteins are not only due to their enzymatic activity, but also to protein–protein interactions which are still unidentified. Here, we compare sequence alignments of snake venom and mammalian PLA2s, grouped according to their structure and biological activity, looking for differences that can justify their different behavior. This bioinformatics analysis has evidenced three distinct regions, two central and one C-terminal, having amino acid compositions that distinguish the different categories of PLA2s. In these regions, we identified short linear motifs (SLiMs), peptide modules involved in protein–protein interactions, conserved in mammalian and not in snake venom PLA2s, or vice versa. The different content in the SLiMs of snake venom with respect to mammalian PLA2s may result in the formation of protein membrane complexes having a toxic activity, or in the formation of complexes whose activity cannot be blocked due to the lack of switches in the toxic PLA2s, as the motif recognized by the prolyl isomerase Pin1. View Full-Text
Keywords: snake venom phospholipases A2; neurotoxins; myotoxins; secretory phospholipases A2; PLA2G1B; PLA2G2A; sequence alignment; short linear motifs; prolyl isomerase; glycogen synthase kinase 3 snake venom phospholipases A2; neurotoxins; myotoxins; secretory phospholipases A2; PLA2G1B; PLA2G2A; sequence alignment; short linear motifs; prolyl isomerase; glycogen synthase kinase 3
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MDPI and ACS Style

Peggion, C.; Tonello, F. Short Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2. Toxins 2021, 13, 290. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13040290

AMA Style

Peggion C, Tonello F. Short Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2. Toxins. 2021; 13(4):290. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13040290

Chicago/Turabian Style

Peggion, Caterina, and Fiorella Tonello. 2021. "Short Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2" Toxins 13, no. 4: 290. https://0-doi-org.brum.beds.ac.uk/10.3390/toxins13040290

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