Mass spectrometry-based top-down and bottom-up approaches for proteomic analysis of the Moroccan Buthus occitanus scorpion venom.
Buthus occitanus scorpion
bottom-up
top-down
toxins
venom
venomic
Journal
FEBS open bio
ISSN: 2211-5463
Titre abrégé: FEBS Open Bio
Pays: England
ID NLM: 101580716
Informations de publication
Date de publication:
07 2021
07 2021
Historique:
revised:
18
02
2021
received:
29
12
2020
accepted:
11
03
2021
pubmed:
15
3
2021
medline:
1
4
2022
entrez:
14
3
2021
Statut:
ppublish
Résumé
Buthus occitanus (B. occitanus) is one of the most dangerous scorpions in the world. Despite the involvement of B. occitanus scorpion in severe cases of envenomation in Morocco, no study has focused yet on the proteomic composition of the Moroccan B. occitanus scorpion venom. Mass spectrometry-based proteomic techniques are commonly used in the study of scorpion venoms. The implementation of top-down and bottom-up approaches for proteomic analyses facilitates screening by allowing a global view of the structural aspects of such complex matrices. Here, we provide a partial overview of the venom of B. occitanus scorpion, in order to explore the diversity of its toxins and hereafter understand their effects. To this end, a combination of top-down and bottom-up approaches was applied using nano-high liquid chromatography coupled to nano-electrospray tandem mass spectrometry (nano-LC-ESI MS/MS). The LC-MS results showed that B. occitanus venom contains around 200 molecular masses ranging from 1868 to 16 720 Da, the most representative of which are those between 5000 and 8000 Da. Interestingly, combined top-down and bottom-up LC-MS/MS results allowed the identification of several toxins, which were mainly those acting on ion channels, including those targeting sodium (NaScTxs), potassium (KScTxs), chloride (ClScTxs), and calcium channels (CaScTx), as well as antimicrobial peptides (AMPs), amphipathic peptides, myotropic neuropeptides, and hypothetical secreted proteins. This study reveals the molecular diversity of B. occitanus scorpion venom and identifies components that may have useful pharmacological activities.
Identifiants
pubmed: 33715301
doi: 10.1002/2211-5463.13143
pmc: PMC8255848
doi:
Substances chimiques
Scorpion Venoms
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1867-1892Informations de copyright
© 2021 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
Références
Arch Biochem Biophys. 2001 Jul 15;391(2):197-206
pubmed: 11437351
Toxins (Basel). 2019 Apr 10;11(4):
pubmed: 30974767
Eur J Biochem. 1998 May 15;254(1):44-9
pubmed: 9652392
J Proteome Res. 2013 Jul 5;12(7):3460-70
pubmed: 23731212
Sci Data. 2017 Jul 11;4:170090
pubmed: 28696408
Toxicon. 1996 Sep;34(9):987-1001
pubmed: 8896191
J Venom Anim Toxins Incl Trop Dis. 2017 Oct 18;23:44
pubmed: 29075288
Am J Physiol. 1993 Feb;264(2 Pt 1):C361-9
pubmed: 8383429
Glia. 2002 Aug;39(2):162-73
pubmed: 12112367
J Proteomics. 2016 Sep 2;146:148-64
pubmed: 27318176
Am J Trop Med Hyg. 2000 Feb;62(2):277-83
pubmed: 10813485
J Immunol. 1997 Jun 1;158(11):5120-8
pubmed: 9164927
Toxicon. 2008 Oct;52(5):611-8
pubmed: 18718845
Eur J Biochem. 1997 Jan 15;243(1-2):93-9
pubmed: 9030726
Toxicon. 2013 Mar 1;63:44-54
pubmed: 23182832
J Venom Anim Toxins Incl Trop Dis. 2013 Mar 28;19(1):5
pubmed: 23849043
J Neurosci. 2002 Mar 15;22(6):2023-34
pubmed: 11896142
Drug Des Devel Ther. 2012;6:165-73
pubmed: 22826633
Toxicon. 2005 Dec 15;46(8):831-44
pubmed: 16274721
PLoS One. 2012;7(7):e40135
pubmed: 22792229
Proteomics. 2006 Jun;6(12):3718-27
pubmed: 16705749
Biochimie. 2001 Sep;83(9):883-9
pubmed: 11698110
Cell Mol Life Sci. 2008 Oct;65(19):3081-92
pubmed: 18726072
Heliyon. 2017 Jan 05;3(1):e00221
pubmed: 28124029
Anal Chem. 2016 Jan 5;88(1):95-121
pubmed: 26558748
Toxicon. 2011 Jan;57(1):84-92
pubmed: 20969885
J Proteome Res. 2020 Apr 3;19(4):1731-1749
pubmed: 32073270
Toxicon. 2018 Jul;149:26-36
pubmed: 28712915
Toxins (Basel). 2013 Dec 13;5(12):2456-87
pubmed: 24351712
J Venom Anim Toxins Incl Trop Dis. 2014 Nov 03;20(1):48
pubmed: 25414725
Toxins (Basel). 2019 Apr 30;11(5):
pubmed: 31052267
Bioorg Khim. 1985 Nov;11(11):1445-56
pubmed: 4091860
Peptides. 2012 Jun;35(2):291-9
pubmed: 22484288
Eur J Biochem. 1987 Feb 2;162(3):589-99
pubmed: 3104036
Protein Cell. 2011 Jun;2(6):437-44
pubmed: 21748593
Mol Cancer. 2014 Aug 13;13:191
pubmed: 25128329
Acta Trop. 2016 Jan;153:70-8
pubmed: 26477848
Mol Cell Proteomics. 2016 Jul;15(7):2423-34
pubmed: 27178327
Toxicon. 2013 Nov;74:193-207
pubmed: 23998939
Insect Biochem Mol Biol. 2004 Nov;34(11):1141-6
pubmed: 15522610
Mol Pharmacol. 2012 Sep;82(3):372-82
pubmed: 22622363
Toxicon. 2006 May;47(6):676-87
pubmed: 16626777
Anal Chem. 1996 Mar 1;68(5):850-8
pubmed: 8779443
Rapid Commun Mass Spectrom. 2019 May;33 Suppl 1:20-27
pubmed: 30076652
Toxins (Basel). 2018 Apr 18;10(4):
pubmed: 29670004
J Comp Neurol. 2005 Sep 12;490(1):57-71
pubmed: 16041719
PLoS One. 2015 Feb 06;10(2):e0117188
pubmed: 25659089
Toxicon. 2018 Sep 1;151:47-62
pubmed: 29964058
Toxicon. 1997 Mar;35(3):365-82
pubmed: 9080593
Toxicon. 2007 Sep 1;50(3):428-37
pubmed: 17559900
Biochem Biophys Res Commun. 2008 Jul 4;371(3):515-20
pubmed: 18445483
Nat Methods. 2012 Nov;9(11):1065-6
pubmed: 23132117
PLoS One. 2015 Jun 01;10(6):e0125908
pubmed: 26030072
Nat Methods. 2013 Mar;10(3):186-7
pubmed: 23443629
Proteomics. 2012 Jan;12(2):313-28
pubmed: 22121013
Toxins (Basel). 2019 Aug 27;11(9):
pubmed: 31461913
Toxicon. 2014 Nov;90:337-43
pubmed: 25218169
Toxins (Basel). 2014 Jun 12;6(6):1873-81
pubmed: 24926799
Toxicon. 2014 Mar;79:55-63
pubmed: 24418174
Rapid Commun Mass Spectrom. 2001;15(17):1562-72
pubmed: 11713783
Int J Mol Sci. 2019 Jan 31;20(3):
pubmed: 30709056
Biochem Biophys Res Commun. 2002 Dec 13;299(4):562-8
pubmed: 12459175
J Proteomics. 2018 Mar 20;175:3-4
pubmed: 28188863
Eur J Biochem. 1999 Sep;264(2):287-300
pubmed: 10491073