Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development

Research output: Contribution to journalJournal article

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Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development. / Laustsen, Andreas Hougaard; Lomonte, Bruno; Lohse, Brian; Fernandez, Julian; Gutiérrez, José María.

In: Journal of Proteomics, Vol. 119, 2015, p. 126–142.

Research output: Contribution to journalJournal article

Harvard

Laustsen, AH, Lomonte, B, Lohse, B, Fernandez, J & Gutiérrez, JM 2015, 'Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development', Journal of Proteomics, vol. 119, pp. 126–142. https://doi.org/10.1016/j.jprot.2015.02.002

APA

Laustsen, A. H., Lomonte, B., Lohse, B., Fernandez, J., & Gutiérrez, J. M. (2015). Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development. Journal of Proteomics, 119, 126–142. https://doi.org/10.1016/j.jprot.2015.02.002

Vancouver

Laustsen AH, Lomonte B, Lohse B, Fernandez J, Gutiérrez JM. Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development. Journal of Proteomics. 2015;119:126–142. https://doi.org/10.1016/j.jprot.2015.02.002

Author

Laustsen, Andreas Hougaard ; Lomonte, Bruno ; Lohse, Brian ; Fernandez, Julian ; Gutiérrez, José María. / Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development. In: Journal of Proteomics. 2015 ; Vol. 119. pp. 126–142.

Bibtex

@article{82c712185b004a3dae1cc11f6c908c28,
title = "Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development",
abstract = "The venom proteome of the black mamba, Dendroaspis polylepis, from Eastern Africa, was, for the first time, characterized. Forty- different proteins and one nucleoside were identified or assigned to protein families. The most abundant proteins were Kunitz-type proteinase inhibitors, which include the unique mamba venom components ‘dendrotoxins’, and α-neurotoxins and other representatives of the three-finger toxin family. In addition, the venom contains lower percentages of proteins from other families, including metalloproteinase, hyaluronidase, prokineticin, nerve growth factor, vascular endothelial growth factor, phospholipase A2, 5′-nucleotidase, and phosphodiesterase. Assessment of acute toxicity revealed that the most lethal components were α-neurotoxins and, to a lower extent, dendrotoxins. This venom also contains a relatively high concentration of adenosine, which might contribute to toxicity by influencing the toxin biodistribution. ELISA immunoprofiling and preclinical assessment of neutralization showed that polyspecific antivenoms manufactured in South Africa and India were effective in the neutralization of D. polylepis venom, albeit showing different potencies. Antivenoms had higher antibody titers against α-neurotoxins than against dendrotoxins, and displayed high titers against less toxic proteins of high molecular mass. Our results reveal the complexity of D. polylepis venom, and provide information for the identification of its most relevant toxins to be neutralized by antivenoms.",
keywords = "Faculty of Health and Medical Sciences, Dendroaspis polylepis, Antivenoms, Immunoprofiling, Snake venom: proteomics, Black mamba",
author = "Laustsen, {Andreas Hougaard} and Bruno Lomonte and Brian Lohse and Julian Fernandez and Guti{\'e}rrez, {Jos{\'e} Mar{\'i}a}",
year = "2015",
doi = "10.1016/j.jprot.2015.02.002",
language = "English",
volume = "119",
pages = "126–142",
journal = "Journal of Proteomics",
issn = "1874-3919",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Unveiling the nature of black mamba (Dendroaspis polylepis) venom through venomics and antivenom immunoprofiling: Identification of key toxin targets for antivenom development

AU - Laustsen, Andreas Hougaard

AU - Lomonte, Bruno

AU - Lohse, Brian

AU - Fernandez, Julian

AU - Gutiérrez, José María

PY - 2015

Y1 - 2015

N2 - The venom proteome of the black mamba, Dendroaspis polylepis, from Eastern Africa, was, for the first time, characterized. Forty- different proteins and one nucleoside were identified or assigned to protein families. The most abundant proteins were Kunitz-type proteinase inhibitors, which include the unique mamba venom components ‘dendrotoxins’, and α-neurotoxins and other representatives of the three-finger toxin family. In addition, the venom contains lower percentages of proteins from other families, including metalloproteinase, hyaluronidase, prokineticin, nerve growth factor, vascular endothelial growth factor, phospholipase A2, 5′-nucleotidase, and phosphodiesterase. Assessment of acute toxicity revealed that the most lethal components were α-neurotoxins and, to a lower extent, dendrotoxins. This venom also contains a relatively high concentration of adenosine, which might contribute to toxicity by influencing the toxin biodistribution. ELISA immunoprofiling and preclinical assessment of neutralization showed that polyspecific antivenoms manufactured in South Africa and India were effective in the neutralization of D. polylepis venom, albeit showing different potencies. Antivenoms had higher antibody titers against α-neurotoxins than against dendrotoxins, and displayed high titers against less toxic proteins of high molecular mass. Our results reveal the complexity of D. polylepis venom, and provide information for the identification of its most relevant toxins to be neutralized by antivenoms.

AB - The venom proteome of the black mamba, Dendroaspis polylepis, from Eastern Africa, was, for the first time, characterized. Forty- different proteins and one nucleoside were identified or assigned to protein families. The most abundant proteins were Kunitz-type proteinase inhibitors, which include the unique mamba venom components ‘dendrotoxins’, and α-neurotoxins and other representatives of the three-finger toxin family. In addition, the venom contains lower percentages of proteins from other families, including metalloproteinase, hyaluronidase, prokineticin, nerve growth factor, vascular endothelial growth factor, phospholipase A2, 5′-nucleotidase, and phosphodiesterase. Assessment of acute toxicity revealed that the most lethal components were α-neurotoxins and, to a lower extent, dendrotoxins. This venom also contains a relatively high concentration of adenosine, which might contribute to toxicity by influencing the toxin biodistribution. ELISA immunoprofiling and preclinical assessment of neutralization showed that polyspecific antivenoms manufactured in South Africa and India were effective in the neutralization of D. polylepis venom, albeit showing different potencies. Antivenoms had higher antibody titers against α-neurotoxins than against dendrotoxins, and displayed high titers against less toxic proteins of high molecular mass. Our results reveal the complexity of D. polylepis venom, and provide information for the identification of its most relevant toxins to be neutralized by antivenoms.

KW - Faculty of Health and Medical Sciences

KW - Dendroaspis polylepis

KW - Antivenoms

KW - Immunoprofiling

KW - Snake venom: proteomics

KW - Black mamba

U2 - 10.1016/j.jprot.2015.02.002

DO - 10.1016/j.jprot.2015.02.002

M3 - Journal article

C2 - 25688917

VL - 119

SP - 126

EP - 142

JO - Journal of Proteomics

JF - Journal of Proteomics

SN - 1874-3919

ER -

ID: 134704827