Aryl sulfatase from <i>Naja nigricolis</i> venom: Characterization and possible contribution in the pathology of snake poisoning

Nok, Andrew J.; Abubakar, M.S.; Adaudi, A O; Balogun, E.O.

doi:10.1002/jbt.10061

Cited by 8 publications

(2 citation statements)

References 10 publications

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“…Aryl sulfatase was purified from N. nigricollis venom [48]. The enzyme catalyzed the hydrolysis of the fluorescent compound methyumbelliferyl-sulfate chondroitin-4-sulfate.…”

Section: Other Hydrolasesmentioning

confidence: 99%

Non-Lethal Polypeptide Components in Cobra Venom

Utkin

Osipov²

2007

CPD

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Snakes from several genera (mostly from Naja genus) belonging to the Elapidae family are usually named cobras. The effect of cobra bites is mainly neurotoxic. This is explained by the presence of highly potent alpha-neurotoxin in their venoms. The other two highly toxic components of cobra venoms are cytotoxins and phospholipases A(2). These three types of toxins constitute a major part of cobra venom. They have attracted the attention of researchers for many years and have been very well studied and thoroughly described. However cobra venoms contain also many other less abundant components which possess very low toxicity or even are not toxic at all. These components, mostly proteins, belong to different structural and functional types, and the reason for their presence in the venom is not always evident. Some of them are known for many years (e.g., nerve growth factor and cobra venom factor); others (e.g., cysteine rich secretory proteins, CRISPs) were discovered only recently. There are non-lethal proteins with unique biological activities that can be used as biochemical tools, while others may be regarded as potential leads for drug design. This review is the first attempt to systemize the available data on non-lethal components of cobra venom.

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“…Aryl sulfatase was purified from N. nigricollis venom [48]. The enzyme catalyzed the hydrolysis of the fluorescent compound methyumbelliferyl-sulfate chondroitin-4-sulfate.…”

Section: Other Hydrolasesmentioning

confidence: 99%

Non-Lethal Polypeptide Components in Cobra Venom

Utkin

Osipov²

2007

CPD

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“…By modifying the sulphation state of their substrates, sulphatases play a key role in the control of physiological processes, including cellular degradation, cell signalling and hormone regulation (Diez‐Roux & Ballabio, 2005). The venom of the black‐necked spitting cobra Naja nigricollis was found to contain a high level of the enzyme arylsulphatase (Nok et al. , 2003).…”

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confidence: 99%

Insights into the venom composition of the ectoparasitoid wasp Nasonia vitripennis from bioinformatic and proteomic studies

Graaf

Aerts

Brunain

et al. 2010

Insect Molecular Biology

179

237

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With the Nasonia vitripennis genome sequences available, we attempted to determine the proteins present in venom by two different approaches. First, we searched for the transcripts of venom proteins by a bioinformatic approach using amino acid sequences of known hymenopteran venom proteins. Second, we performed proteomic analyses of crude N. vitripennis venom removed from the venom reservoir, implementing both an off-line two-dimensional liquid chromatography matrix-assisted laser desorption/ionization time-of-flight (2D-LC-MALDI-TOF) mass spectrometry (MS) and a two-dimensional liquid chromatography electrospray ionization Founer transform ion cyclotron resonance (2D-LC-ESI-FT-ICR) MS setup. This combination of bioinformatic and proteomic studies resulted in an extraordinary richness of identified venom constituents. Moreover, half of the 79 identified proteins were not yet associated with insect venoms: 16 proteins showed similarity only to known proteins from other tissues or secretions, and an additional 23 did not show similarity to any known protein. Serine proteases and their inhibitors were the most represented. Fifteen nonsecretory proteins were also identified by proteomic means and probably represent so-called ‘venom trace elements’. The present study contributes greatly to the understanding of the biological diversity of the venom of parasitoid wasps at the molecular level.

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