Dataset Information

Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effects.

ABSTRACT: Venom phospholipases A2 (PLA(2)) are associated with neurotoxic, myotoxic, cardiotoxic, platelet aggregation, and edema activities. A PLA(2) (Drs-PLA(2)) was purified from Daboia russelii siamensis venom by a two-step purification procedure consisting of size-exclusion, followed by anion exchange high performance liquid chromatography (HPLC). The molecular weight of the Drs-PLA(2) was 13,679Da, which was determined by MALDI-TOF mass spectrometry. Its N-terminal amino acid sequence was homologous to basic PLA(2)s of viperid snake venoms. The Drs-PLA(2) had indirect hemolytic and anticoagulant activities, cytotoxic activity with a CC(50) of 65.8nM, and inhibited SK-MEL-28 cell migration with an IC(50) of 25.6nM. In addition, the Drs-PLA(2) inhibited the colonization of B16F10 cells in lungs of BALB/c mice by ?65%.

SUBMITTER: Khunsap S

PROVIDER: S-EPMC3210966 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effects.

Khunsap Suchitra S Pakmanee Narumol N Khow Orawan O Chanhome Lawan L Sitprija Visith V Suntravat Montamas M Lucena Sara E SE Perez John C JC Sánchez Elda E EE

Journal of venom research 20111022

Venom phospholipases A2 (PLA(2)) are associated with neurotoxic, myotoxic, cardiotoxic, platelet aggregation, and edema activities. A PLA(2) (Drs-PLA(2)) was purified from Daboia russelii siamensis venom by a two-step purification procedure consisting of size-exclusion, followed by anion exchange high performance liquid chromatography (HPLC). The molecular weight of the Drs-PLA(2) was 13,679Da, which was determined by MALDI-TOF mass spectrometry. Its N-terminal amino acid sequence was homologous ...[more]

PMID: 22091349

Similar Datasets

Project description:BackgroundSnakebite in India results in over 58,000 fatalities and a vast number of morbidities annually. The majority of these clinically severe envenomings are attributed to Russell's viper (Daboia russelii), which has a near pan-India distribution. Unfortunately, despite its medical significance, the influence of biogeography on the composition and potency of venom from disparate D. russelii populations, and the repercussions of venom variation on the neutralisation efficacy of marketed Indian antivenoms, remain elusive.MethodsHere, we employ an integrative approach comprising proteomic characterisation, biochemical analyses, pharmacological assessment, and venom toxicity profiling to elucidate the influence of varying ecology and environment on the pan-Indian populations of D. russelii. We then conducted in vitro venom recognition experiments and in vivo neutralisation assays to evaluate the efficacy of the commercial Indian antivenoms against the geographically disparate D. russelii populations.FindingsWe reveal significant intraspecific variation in the composition, biochemical and pharmacological activities and potencies of D. russelii venoms sourced from five distinct biogeographic zones across India. Contrary to our understanding of the consequences of venom variation on the effectiveness of snakebite therapy, commercial antivenom exhibited surprisingly similar neutralisation potencies against the majority of the investigated populations, with the exception of low preclinical efficacy against the semi-arid population from northern India. However, the ability of Indian antivenoms to counter the severe morbid effects of Daboia envenoming remains to be evaluated.ConclusionThe concerning lack of antivenom efficacy against the north Indian population of D. russelii, as well as against two other 'big four' snake species in nearby locations, underscores the pressing need to develop pan-India effective antivenoms with improved efficacy in high snakebite burden locales.

Dataset Information

Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effects.

Publications

Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effects.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure