Tags

Type your tag names separated by a space and hit enter

Modulation of insect Ca(v) channels by peptidic spider toxins.
Toxicon. 2007 Mar 15; 49(4):513-30.T

Abstract

Insects have a much smaller repertoire of voltage-gated calcium (Ca(V)) channels than vertebrates. Drosophila melanogaster harbors only a single ortholog of each of the vertebrate Ca(V)1, Ca(V)2, and Ca(V)3 subtypes, although its basal inventory is expanded by alternative splicing and editing of Ca(V) channel transcripts. Nevertheless, there appears to be little functional plasticity within this limited panel of insect Ca(V) channels, since severe loss-of-function mutations in genes encoding the pore-forming alpha1 subunits in Drosophila are embryonic lethal. Since the primary role of spider venom is to paralyze or kill insect prey, it is not surprising that most, if not all, spider venoms contain peptides that potently modify the activity of these functionally critical insect Ca(V) channels. Unfortunately, it has proven difficult to determine the precise ion channel subtypes recognized by these peptide toxins since insect Ca(V) channels have significantly different pharmacology to their vertebrate counterparts, and cloned insect Ca(V) channels are not available for electrophysiological studies. However, biochemical and genetic studies indicate that some of these spider toxins might ultimately become the defining pharmacology for certain subtypes of insect Ca(V) channels. This review focuses on peptidic spider toxins that specifically target insect Ca(V) channels. In addition to providing novel molecular tools for ion channel characterization, some of these toxins are being used as leads to develop new methods for controlling insect pests.

Authors+Show Affiliations

Division of Chemical and Structural Biology, Institute for Molecular Bioscience, University of Queensland, Brisbane Qld. 4072, Australia. glenn.king@imb.uq.edu.au

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review

Language

eng

PubMed ID

17197008

Citation

King, Glenn F.. "Modulation of Insect Ca(v) Channels By Peptidic Spider Toxins." Toxicon : Official Journal of the International Society On Toxinology, vol. 49, no. 4, 2007, pp. 513-30.
King GF. Modulation of insect Ca(v) channels by peptidic spider toxins. Toxicon. 2007;49(4):513-30.
King, G. F. (2007). Modulation of insect Ca(v) channels by peptidic spider toxins. Toxicon : Official Journal of the International Society On Toxinology, 49(4), 513-30.
King GF. Modulation of Insect Ca(v) Channels By Peptidic Spider Toxins. Toxicon. 2007 Mar 15;49(4):513-30. PubMed PMID: 17197008.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Modulation of insect Ca(v) channels by peptidic spider toxins. A1 - King,Glenn F, Y1 - 2006/11/28/ PY - 2006/10/30/received PY - 2006/11/17/accepted PY - 2007/1/2/pubmed PY - 2007/5/4/medline PY - 2007/1/2/entrez SP - 513 EP - 30 JF - Toxicon : official journal of the International Society on Toxinology JO - Toxicon VL - 49 IS - 4 N2 - Insects have a much smaller repertoire of voltage-gated calcium (Ca(V)) channels than vertebrates. Drosophila melanogaster harbors only a single ortholog of each of the vertebrate Ca(V)1, Ca(V)2, and Ca(V)3 subtypes, although its basal inventory is expanded by alternative splicing and editing of Ca(V) channel transcripts. Nevertheless, there appears to be little functional plasticity within this limited panel of insect Ca(V) channels, since severe loss-of-function mutations in genes encoding the pore-forming alpha1 subunits in Drosophila are embryonic lethal. Since the primary role of spider venom is to paralyze or kill insect prey, it is not surprising that most, if not all, spider venoms contain peptides that potently modify the activity of these functionally critical insect Ca(V) channels. Unfortunately, it has proven difficult to determine the precise ion channel subtypes recognized by these peptide toxins since insect Ca(V) channels have significantly different pharmacology to their vertebrate counterparts, and cloned insect Ca(V) channels are not available for electrophysiological studies. However, biochemical and genetic studies indicate that some of these spider toxins might ultimately become the defining pharmacology for certain subtypes of insect Ca(V) channels. This review focuses on peptidic spider toxins that specifically target insect Ca(V) channels. In addition to providing novel molecular tools for ion channel characterization, some of these toxins are being used as leads to develop new methods for controlling insect pests. SN - 0041-0101 UR - https://www.unboundmedicine.com/medline/citation/17197008/Modulation_of_insect_Ca_v__channels_by_peptidic_spider_toxins_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0041-0101(06)00430-2 DB - PRIME DP - Unbound Medicine ER -