The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3

Stefan Zorn; Enrico Leipold; Alfred Hansel; Grzegorz Bulaj; Baldomero M Olivera; Heinrich Terlau; Stefan H Heinemann

doi:10.1016/j.febslet.2006.01.057

The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3

Stefan Zorn, Enrico Leipold, Alfred Hansel, Grzegorz Bulaj, Baldomero M Olivera, Heinrich Terlau, Stefan H Heinemann

Friedrich Schiller University Jena

Abstract

Several families of peptide toxins from cone snails affect voltage-gated sodium (Na(V)) channels: mu-conotoxins block the pore, delta-conotoxins inhibit channel inactivation, and muO-conotoxins inhibit Na(V) channels by an unknown mechanism. The only currently known muO-conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (Na(V)1.4) and brain (Na(V)1.2) sodium channels in mammalian cells. A systematic domain-swapping strategy identified the C-terminal pore loop of domain-3 as the major determinant for Na(V)1.4 being more potently blocked than Na(V)1.2 channels. muO-conotoxins therefore show an interaction pattern with Na(V) channels that is clearly different from the related mu- and delta-conotoxins, indicative of a distinct molecular mechanism of channel inhibition.

Original language	English
Journal	FEBS Letters
Volume	580
Issue number	5
Pages (from-to)	1360-4
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2006.01.057
Publication status	Published - 20.02.2006

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10.1016/j.febslet.2006.01.057

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title = "The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3",

abstract = "Several families of peptide toxins from cone snails affect voltage-gated sodium (Na(V)) channels: mu-conotoxins block the pore, delta-conotoxins inhibit channel inactivation, and muO-conotoxins inhibit Na(V) channels by an unknown mechanism. The only currently known muO-conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (Na(V)1.4) and brain (Na(V)1.2) sodium channels in mammalian cells. A systematic domain-swapping strategy identified the C-terminal pore loop of domain-3 as the major determinant for Na(V)1.4 being more potently blocked than Na(V)1.2 channels. muO-conotoxins therefore show an interaction pattern with Na(V) channels that is clearly different from the related mu- and delta-conotoxins, indicative of a distinct molecular mechanism of channel inhibition.",

author = "Stefan Zorn and Enrico Leipold and Alfred Hansel and Grzegorz Bulaj and Olivera, {Baldomero M} and Heinrich Terlau and Heinemann, {Stefan H}",

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T1 - The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3

AU - Zorn, Stefan

AU - Leipold, Enrico

AU - Hansel, Alfred

AU - Bulaj, Grzegorz

AU - Olivera, Baldomero M

AU - Terlau, Heinrich

AU - Heinemann, Stefan H

PY - 2006/2/20

Y1 - 2006/2/20

N2 - Several families of peptide toxins from cone snails affect voltage-gated sodium (Na(V)) channels: mu-conotoxins block the pore, delta-conotoxins inhibit channel inactivation, and muO-conotoxins inhibit Na(V) channels by an unknown mechanism. The only currently known muO-conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (Na(V)1.4) and brain (Na(V)1.2) sodium channels in mammalian cells. A systematic domain-swapping strategy identified the C-terminal pore loop of domain-3 as the major determinant for Na(V)1.4 being more potently blocked than Na(V)1.2 channels. muO-conotoxins therefore show an interaction pattern with Na(V) channels that is clearly different from the related mu- and delta-conotoxins, indicative of a distinct molecular mechanism of channel inhibition.

AB - Several families of peptide toxins from cone snails affect voltage-gated sodium (Na(V)) channels: mu-conotoxins block the pore, delta-conotoxins inhibit channel inactivation, and muO-conotoxins inhibit Na(V) channels by an unknown mechanism. The only currently known muO-conotoxins MrVIA and MrVIB from Conus marmoreus were applied to cloned rat skeletal muscle (Na(V)1.4) and brain (Na(V)1.2) sodium channels in mammalian cells. A systematic domain-swapping strategy identified the C-terminal pore loop of domain-3 as the major determinant for Na(V)1.4 being more potently blocked than Na(V)1.2 channels. muO-conotoxins therefore show an interaction pattern with Na(V) channels that is clearly different from the related mu- and delta-conotoxins, indicative of a distinct molecular mechanism of channel inhibition.

U2 - 10.1016/j.febslet.2006.01.057

DO - 10.1016/j.febslet.2006.01.057

M3 - Journal articles

C2 - 16458302

SN - 0014-5793

VL - 580

SP - 1360

EP - 1364

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3

Abstract

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