Open AccessCharacterization of Three Venom Peptides from the Spitting Spider Scytodes thoracica
Author(s) -
Nathanial K. Ariki,
Lisa E. Muñoz,
Elizabeth L. Armitage,
Francesca R. Goodstein,
Kathryn G. George,
V. Anne Smith,
Irina Vetter,
Volker Herzig,
Glenn F. King,
Nikolaus M. Loening
Publication year - 2016
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0156291
Subject(s) - venom , peptide , biology , spider , peptide sequence , receptor , thoracica , biochemistry , zoology , crustacean , barnacle , gene
We present the solution-state NMR structures and preliminary functional characterizations of three venom peptides identified from the spitting spider Scytodes thoracica . Despite little sequence identity to other venom peptides, structural characterization reveals that these peptides contain an inhibitor cystine knot motif common to many venom peptides. These are the first structures for any peptide or protein from spiders of the Scytodidae family. Many venom peptides target neuronal ion channels or receptors. However, we have not been able to determine the target of these Scytodes peptides so we can only state with certainty the channels and receptors that they do not target.