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Title: δ/ω-Plectoxin-Pt1a: An Excitatory Spider Toxin with Actions on both Ca(2+) and Na(+) Channels.
Name(s): Zhou, Yi, author
Zhao, Mingli, author
Fields, Gregg B., author
Wu, Chun-Fang, author
Branton, W., author
Type of Resource: text
Genre: Text
Issuance: serial
Date Issued: 2013
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: The venom of spider Plectreurys tristis contains a variety of peptide toxins that selectively target neuronal ion channels. O-palmitoylation of a threonine or serine residue, along with a characteristic and highly constrained disulfide bond structure, are hallmarks of a family of toxins found in this venom. Here, we report the isolation and characterization of a new toxin, δ/ω-plectoxin-Pt1a, from this spider venom. It is a 40 amino acid peptide containing an O-palmitoylated Ser-39. Analysis of δ/ω-plectoxin-Pt1a cDNA reveals a small precursor containing a secretion signal sequence, a 14 amino acid N-terminal propeptide, and a C-terminal amidation signal. The biological activity of δ/ω-plectoxin-Pt1a is also unique. It preferentially blocks a subset of Ca(2+) channels that is apparently not required for neurotransmitter release; decreases threshold for Na(+) channel activation; and slows Na(+) channel inactivation. As δ/ω-plectoxin-Pt1a enhances synaptic transmission by prolonging presynaptic release of neurotransmitter, its effects on Na(+) and Ca(2+) channels may act synergistically to sustain the terminal excitability.
Identifier: FSU_migr_biomed_faculty_publications-0044 (IID)
Subject(s): Biochemistry
Molecular biology
Persistent Link to This Record:
Host Institution: FSU
Is Part of Series: Department of Biomedical Sciences Faculty Publications.
Is Part Of: PLoS One.
Issue: 5, 8

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Zhou, Y., Zhao, M., Fields, G. B., Wu, C. -F., & Branton, W. (2013). δ/ω-Plectoxin-Pt1a: An Excitatory Spider Toxin with Actions on both Ca(2+) and Na(+) Channels. Plos One. Retrieved from