Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A2 Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation

Corina Vera-Gonzales; Carlos Alberto Arenas-Chávez; Luis A. Ponce-Soto; Aldo Alvarez-Risco; Shyla Del-Aguila-Arcentales; Neal M. Davies; Jaime A. Yáñez

doi:10.3390/pr10071428

Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A₂ Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation

Corina Vera-Gonzales, Carlos Alberto Arenas-Chávez, Luis A. Ponce-Soto, Aldo Alvarez-Risco, Shyla Del-Aguila-Arcentales, Neal M. Davies, Jaime A. Yáñez

Professional School of Pharmacy and Biochemistry

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

1 Scopus citations

Abstract

The fractionation of Crotalus durissus collilineatus whole venom through an HPLC chromatographic method enabled the purification of a new V-1 neurotoxin. Inter-CRO (V-1) presents similarity in its primary structure to crotoxin B (CB), suggesting another isoform of this toxin. The aim of this study was to compare V-1 to the crotoxin complex (CA/CB) and CB to elucidate aspects related to its functionality. The homogeneity of the purified protein was confirmed with a molecular mass of 1425.45 Da, further verified by mass spectrometry. The sequence of the protein showed high similarity to other viperid snake venom PLA₂ proteins. The results of this study report that V-1 is an uncharacterized novel toxin with different biological activities from CB. V-1 maintained catalytic activity but presented neurotoxic activity as observed by the 2.5-fold increase in twitch tension record compared to control values on isolated muscle cells.

Original language	English
Article number	1428
Journal	Processes
Volume	10
Issue number	7
DOIs	https://doi.org/10.3390/pr10071428
State	Published - Jul 2022

Keywords

Crotalus durissus collilineatus
Crotalus durissus terrificus
HPLC-RP
V-1
neurotoxin

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Vera-Gonzales, C., Arenas-Chávez, C. A., Ponce-Soto, L. A., Alvarez-Risco, A., Del-Aguila-Arcentales, S., Davies, N. M., & Yáñez, J. A. (2022). Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A₂ Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation. Processes, 10(7), Article 1428. https://doi.org/10.3390/pr10071428

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title = "Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A2 Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation",

abstract = "The fractionation of Crotalus durissus collilineatus whole venom through an HPLC chromatographic method enabled the purification of a new V-1 neurotoxin. Inter-CRO (V-1) presents similarity in its primary structure to crotoxin B (CB), suggesting another isoform of this toxin. The aim of this study was to compare V-1 to the crotoxin complex (CA/CB) and CB to elucidate aspects related to its functionality. The homogeneity of the purified protein was confirmed with a molecular mass of 1425.45 Da, further verified by mass spectrometry. The sequence of the protein showed high similarity to other viperid snake venom PLA2 proteins. The results of this study report that V-1 is an uncharacterized novel toxin with different biological activities from CB. V-1 maintained catalytic activity but presented neurotoxic activity as observed by the 2.5-fold increase in twitch tension record compared to control values on isolated muscle cells.",

keywords = "Crotalus durissus collilineatus, Crotalus durissus terrificus, HPLC-RP, V-1, neurotoxin",

author = "Corina Vera-Gonzales and Arenas-Ch{\'a}vez, {Carlos Alberto} and Ponce-Soto, {Luis A.} and Aldo Alvarez-Risco and Shyla Del-Aguila-Arcentales and Davies, {Neal M.} and Y{\'a}{\~n}ez, {Jaime A.}",

note = "Publisher Copyright: {\textcopyright} 2022 by the authors.",

year = "2022",

month = jul,

doi = "10.3390/pr10071428",

language = "English",

volume = "10",

journal = "Processes",

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Vera-Gonzales, C, Arenas-Chávez, CA, Ponce-Soto, LA, Alvarez-Risco, A, Del-Aguila-Arcentales, S, Davies, NM & Yáñez, JA 2022, 'Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A₂ Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation', Processes, vol. 10, no. 7, 1428. https://doi.org/10.3390/pr10071428

Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A₂ Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation. / Vera-Gonzales, Corina; Arenas-Chávez, Carlos Alberto; Ponce-Soto, Luis A. et al.
In: Processes, Vol. 10, No. 7, 1428, 07.2022.

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

TY - JOUR

T1 - Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A2 Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation

AU - Vera-Gonzales, Corina

AU - Arenas-Chávez, Carlos Alberto

AU - Ponce-Soto, Luis A.

AU - Alvarez-Risco, Aldo

AU - Del-Aguila-Arcentales, Shyla

AU - Davies, Neal M.

AU - Yáñez, Jaime A.

PY - 2022/7

Y1 - 2022/7

N2 - The fractionation of Crotalus durissus collilineatus whole venom through an HPLC chromatographic method enabled the purification of a new V-1 neurotoxin. Inter-CRO (V-1) presents similarity in its primary structure to crotoxin B (CB), suggesting another isoform of this toxin. The aim of this study was to compare V-1 to the crotoxin complex (CA/CB) and CB to elucidate aspects related to its functionality. The homogeneity of the purified protein was confirmed with a molecular mass of 1425.45 Da, further verified by mass spectrometry. The sequence of the protein showed high similarity to other viperid snake venom PLA2 proteins. The results of this study report that V-1 is an uncharacterized novel toxin with different biological activities from CB. V-1 maintained catalytic activity but presented neurotoxic activity as observed by the 2.5-fold increase in twitch tension record compared to control values on isolated muscle cells.

AB - The fractionation of Crotalus durissus collilineatus whole venom through an HPLC chromatographic method enabled the purification of a new V-1 neurotoxin. Inter-CRO (V-1) presents similarity in its primary structure to crotoxin B (CB), suggesting another isoform of this toxin. The aim of this study was to compare V-1 to the crotoxin complex (CA/CB) and CB to elucidate aspects related to its functionality. The homogeneity of the purified protein was confirmed with a molecular mass of 1425.45 Da, further verified by mass spectrometry. The sequence of the protein showed high similarity to other viperid snake venom PLA2 proteins. The results of this study report that V-1 is an uncharacterized novel toxin with different biological activities from CB. V-1 maintained catalytic activity but presented neurotoxic activity as observed by the 2.5-fold increase in twitch tension record compared to control values on isolated muscle cells.

KW - Crotalus durissus collilineatus

KW - Crotalus durissus terrificus

KW - HPLC-RP

KW - V-1

KW - neurotoxin

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U2 - 10.3390/pr10071428

DO - 10.3390/pr10071428

M3 - Article

AN - SCOPUS:85137209556

SN - 2227-9717

VL - 10

JO - Processes

JF - Processes

IS - 7

M1 - 1428

ER -

Vera-Gonzales C, Arenas-Chávez CA, Ponce-Soto LA, Alvarez-Risco A, Del-Aguila-Arcentales S, Davies NM et al. Purification and Characterization of a Novel Factor of Crotoxin Inter-CRO (V-1), a New Phospholipase A₂ Isoform from Crotalus durissus collilineatus Snake Venom Using an In Vitro Neuromuscular Preparation. Processes. 2022 Jul;10(7):1428. doi: 10.3390/pr10071428