The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F

Rossella Pellizzari; Silvia Mason; Clifford Shone; Cesare Montecucco

doi:10.1016/S0014-5793(97)00482-1

The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F

Rossella Pellizzari
, Silvia Mason
, Clifford Shone
, Cesare Montecucco^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

40 Citations (Scopus)

Abstract

Botulinum neurotoxins type D and F are zinc-endopeptidases with a unique specificity for VAMP/synaptobrevin, an essential component of the exocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with tetanus and botulinum B and G neurotoxins. Here, we show that V1 plays a major role in VAMP recognition by botulinum neurotoxins D and P and that V2 is also involved in F binding. Site-directed mutagenesis of V1 and V2 indicates that different residues are the determinants of the VAMP interaction with the two endopeptidases. The study of the VAMP-neurotoxins interaction suggest a pairing of the V1 and V2 segments.

Original language	English
Pages (from-to)	339-342
Number of pages	4
Journal	FEBS Letters
Volume	409
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(97)00482-1
Publication status	Published - 16 Jun 1997

Bibliographical note

Funding Information:
We would like to thank S. Censini and J. Telford for the synthesis of oligonucleotides and P. Washbourne for critically reading the manuscript. This study was supported by Telethon-Italia Grant 763 and by CNR.

Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.

Keywords

Botulism
Neurotoxin
SNARE motif
Tetanus
VAMP
Zinc-endopeptidase

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10.1016/S0014-5793(97)00482-1

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title = "The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F",

abstract = "Botulinum neurotoxins type D and F are zinc-endopeptidases with a unique specificity for VAMP/synaptobrevin, an essential component of the exocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with tetanus and botulinum B and G neurotoxins. Here, we show that V1 plays a major role in VAMP recognition by botulinum neurotoxins D and P and that V2 is also involved in F binding. Site-directed mutagenesis of V1 and V2 indicates that different residues are the determinants of the VAMP interaction with the two endopeptidases. The study of the VAMP-neurotoxins interaction suggest a pairing of the V1 and V2 segments.",

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author = "Rossella Pellizzari and Silvia Mason and Clifford Shone and Cesare Montecucco",

note = "Funding Information: We would like to thank S. Censini and J. Telford for the synthesis of oligonucleotides and P. Washbourne for critically reading the manuscript. This study was supported by Telethon-Italia Grant 763 and by CNR. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.",

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doi = "10.1016/S0014-5793(97)00482-1",

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AU - Pellizzari, Rossella

AU - Mason, Silvia

AU - Shone, Clifford

AU - Montecucco, Cesare

N1 - Funding Information: We would like to thank S. Censini and J. Telford for the synthesis of oligonucleotides and P. Washbourne for critically reading the manuscript. This study was supported by Telethon-Italia Grant 763 and by CNR. Copyright: Copyright 2007 Elsevier B.V., All rights reserved.

PY - 1997/6/16

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N2 - Botulinum neurotoxins type D and F are zinc-endopeptidases with a unique specificity for VAMP/synaptobrevin, an essential component of the exocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with tetanus and botulinum B and G neurotoxins. Here, we show that V1 plays a major role in VAMP recognition by botulinum neurotoxins D and P and that V2 is also involved in F binding. Site-directed mutagenesis of V1 and V2 indicates that different residues are the determinants of the VAMP interaction with the two endopeptidases. The study of the VAMP-neurotoxins interaction suggest a pairing of the V1 and V2 segments.

AB - Botulinum neurotoxins type D and F are zinc-endopeptidases with a unique specificity for VAMP/synaptobrevin, an essential component of the exocytosis apparatus. VAMP contains two copies of a nine residue motif, termed V1 and V2, which are determinants of the interaction with tetanus and botulinum B and G neurotoxins. Here, we show that V1 plays a major role in VAMP recognition by botulinum neurotoxins D and P and that V2 is also involved in F binding. Site-directed mutagenesis of V1 and V2 indicates that different residues are the determinants of the VAMP interaction with the two endopeptidases. The study of the VAMP-neurotoxins interaction suggest a pairing of the V1 and V2 segments.

KW - Botulism

KW - Neurotoxin

KW - SNARE motif

KW - Tetanus

KW - VAMP

KW - Zinc-endopeptidase

UR - https://www.scopus.com/pages/publications/0030787389

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DO - 10.1016/S0014-5793(97)00482-1

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C2 - 9224685

AN - SCOPUS:0030787389

SN - 0014-5793

VL - 409

SP - 339

EP - 342

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F

Abstract

Bibliographical note

Keywords

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