Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin
The Australian jellyfish Chironex fleckeri, belongs to a family of cubozoan jellyfish known for their potent venoms. CfTX-1 and -2 are two highly abundant toxins in the venom, but there is no structural data available for these proteins. Structural information on toxins is integral to the understand...
Main Authors: | , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2018-06-01
|
Series: | Marine Drugs |
Subjects: | |
Online Access: | http://www.mdpi.com/1660-3397/16/6/201 |
id |
doaj-19583137a91b418999b008f36e37443c |
---|---|
record_format |
Article |
spelling |
doaj-19583137a91b418999b008f36e37443c2020-11-24T23:44:01ZengMDPI AGMarine Drugs1660-33972018-06-0116620110.3390/md16060201md16060201Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 ToxinAthena Andreosso0Paramjit S. Bansal1Michael J. Smout2David Wilson3Jamie E. Seymour4Norelle L. Daly5Centre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD 4878, AustraliaThe Australian jellyfish Chironex fleckeri, belongs to a family of cubozoan jellyfish known for their potent venoms. CfTX-1 and -2 are two highly abundant toxins in the venom, but there is no structural data available for these proteins. Structural information on toxins is integral to the understanding of the mechanism of these toxins and the development of an effective treatment. Two regions of CfTX-1 have been predicted to have helical structures that are involved with the mechanism of action. Here we have synthesized peptides corresponding to these regions and analyzed their structures using NMR spectroscopy. The peptide corresponding to the predicted N-terminal amphiphilic helix appears unstructured in aqueous solution. This lack of structure concurs with structural disorder predicted for this region of the protein using the Protein DisOrder prediction System PrDOS. Conversely, a peptide corresponding to a predicted transmembrane region is very hydrophobic, insoluble in aqueous solution and predicted to be structured by PrDOS. In the presence of SDS-micelles both peptides have well-defined helical structures showing that a membrane mimicking environment stabilizes the structures of both peptides and supports the prediction of the transmembrane region in CfTX-1. This is the first study to experimentally analyze the structure of regions of a C. fleckeri protein.http://www.mdpi.com/1660-3397/16/6/201Chironex fleckeri venomCfTX-1cubozoan toxinspore-forming toxins |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Athena Andreosso Paramjit S. Bansal Michael J. Smout David Wilson Jamie E. Seymour Norelle L. Daly |
spellingShingle |
Athena Andreosso Paramjit S. Bansal Michael J. Smout David Wilson Jamie E. Seymour Norelle L. Daly Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin Marine Drugs Chironex fleckeri venom CfTX-1 cubozoan toxins pore-forming toxins |
author_facet |
Athena Andreosso Paramjit S. Bansal Michael J. Smout David Wilson Jamie E. Seymour Norelle L. Daly |
author_sort |
Athena Andreosso |
title |
Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin |
title_short |
Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin |
title_full |
Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin |
title_fullStr |
Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin |
title_full_unstemmed |
Structural Characterisation of Predicted Helical Regions in the Chironex fleckeri CfTX-1 Toxin |
title_sort |
structural characterisation of predicted helical regions in the chironex fleckeri cftx-1 toxin |
publisher |
MDPI AG |
series |
Marine Drugs |
issn |
1660-3397 |
publishDate |
2018-06-01 |
description |
The Australian jellyfish Chironex fleckeri, belongs to a family of cubozoan jellyfish known for their potent venoms. CfTX-1 and -2 are two highly abundant toxins in the venom, but there is no structural data available for these proteins. Structural information on toxins is integral to the understanding of the mechanism of these toxins and the development of an effective treatment. Two regions of CfTX-1 have been predicted to have helical structures that are involved with the mechanism of action. Here we have synthesized peptides corresponding to these regions and analyzed their structures using NMR spectroscopy. The peptide corresponding to the predicted N-terminal amphiphilic helix appears unstructured in aqueous solution. This lack of structure concurs with structural disorder predicted for this region of the protein using the Protein DisOrder prediction System PrDOS. Conversely, a peptide corresponding to a predicted transmembrane region is very hydrophobic, insoluble in aqueous solution and predicted to be structured by PrDOS. In the presence of SDS-micelles both peptides have well-defined helical structures showing that a membrane mimicking environment stabilizes the structures of both peptides and supports the prediction of the transmembrane region in CfTX-1. This is the first study to experimentally analyze the structure of regions of a C. fleckeri protein. |
topic |
Chironex fleckeri venom CfTX-1 cubozoan toxins pore-forming toxins |
url |
http://www.mdpi.com/1660-3397/16/6/201 |
work_keys_str_mv |
AT athenaandreosso structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin AT paramjitsbansal structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin AT michaeljsmout structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin AT davidwilson structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin AT jamieeseymour structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin AT norelleldaly structuralcharacterisationofpredictedhelicalregionsinthechironexfleckericftx1toxin |
_version_ |
1725500469687615488 |