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The venom of Vipera ammodytes ammodytes: proteomics, neurotoxic effect and neutralization by antivenom

ABSTRACT: Snake venoms have a very complex and chemically heterogeneous composition, in which the most abundant proteins and peptides play an important role in the immobilization and digestion of prey. It is obvious that the variability in the composition of the venom has a decisive influence on the designing of antivenoms. In this context, proteomic analyses are of great importance as they provide fundamental knowledge about the components of the venom. Therefore, the aim of the study was to investigate the proteomic profile of Vipera ammodytes ammodytes venom.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Vipera Ammodytes Ammodytes

TISSUE(S): Venom

SUBMITTER: Dina Rešetar Maslov

LAB HEAD: Vladimir Mrljak

PROVIDER: PXD056495 | Pride | 2025-05-07

REPOSITORIES: Pride

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			Action	DRS
	Sample_list.xlsx	Xlsx
	checksum.txt	Txt
	fraction_0.mgf	Mgf
	fraction_0.raw	Raw
	fraction_0A_Peptide_groups_PeptideGroups.txt	Txt

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The Venom of Vipera ammodytes ammodytes: Proteomics, Neurotoxic Effect and Neutralization by Antivenom.

Ivanović Saša R SR Rešetar Maslov Dina D Rubić Ivana I Mrljak Vladimir V Živković Irena I Borozan Nevena N Grujić-Milanović Jelica J Borozan Sunčica S

Veterinary sciences 20241128 12

Deep proteomic analyses identified, in total, 159 master proteins (with 1% FDR and 2 unique peptides) from 26 protein families in the venom of Vipera ammodytes ammodytes (Vaa). Data are available via ProteomeXchange with the identifier PXD056495. The relative abundance of PLA2s is 11.60% of the crude venom, of which 4.35% are neurotoxic Ammodytoxins (Atxs). The neurotoxicity of the venom of Vaa and the neutralizing effect of the antivenom were tested on the neuromuscular preparatio ...[more]

PMID: 39728945

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