Comparison and characterization of the venoms of three Parabuthus scorpion species occurring in southern Africa

Debont, Tom; Swerts, An; Walt, J. J. Van der; Müller, G; Verdonck, Fons; Daenens, Paul; Tytgat, Jan

doi:10.1016/s0041-0101(97)00099-8

Cited by 29 publications

(19 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…16 -18 Traditionally, these peptides have been isolated and identified using a series of chromatographic steps followed by amino acid sequencing. Typification of venoms usually employs gel-based chromatographic fingerprint profiles 19 or ELISA methods. 20,21 Chromatography is, however, time consuming whereas ELISA selectivity is limited and fine differentiation among species is normally not feasible.…”

Section: Introductionmentioning

confidence: 99%

Peptide fingerprinting of snake venoms by direct infusion nano‐electrospray ionization mass spectrometry: potential use in venom identification and taxonomy

et al. 2008

View full text Add to dashboard Cite

Fingerprinting by mass spectrometry has been increasingly used to study venom variations and for taxonomic analyses based on venom components. Most of these studies have concentrated on components heavier than 3 kDa, but Bothrops snake venoms contain many biologically active peptides, principally C-type natriuretic peptides and bradykinin-potentiating peptides (BPPs). In this work, we have examined the peptide profile of Bothrops venoms (B. alternatus, B. erythromelas, B. insularis, B. jararaca, B. jararacussu, B. leucurus and B. moojeni) using direct infusion nano-electrospray ionization mass spectrometry (nano-ESI-MS) subjecting the data further to principal components analysis (PCA) to assess whether the peptide distributions are reliable in distinguishing the venoms. ESI-MS of a low molar mass fraction obtained by ultrafiltration of each venom (5 kDa nominal cutoff filters) revealed that the venoms have a variety of peptides in common but that each venom also contains taxonomic marker peptides not shared with other venoms. One BPP peptide, QGGWPRPGPEIPP, was found to be common to the seven Bothrops species examined. This peptide may represent a specific marker for this genus since it was not found in the venom of the South American rattlesnake, Crotalus durissus terrificus. PCA on the ESI-MS data reveals a close relationship between B. jararaca, B. jararacussu and B. moojeni venoms, with B. leucurus and B. erythromelas being more distant from these three; B. alternatus and B. insularis were also located distant from these five species, as was C. d. terrificus. These results agree partially with established phylogenetic relationships among these species and suggest that ESI-MS peptide fingerprinting of snake venoms coupled with PCA is a useful tool for identifying venoms and for taxonomic analyses.

show abstract

Section: Introductionmentioning

confidence: 99%

Peptide fingerprinting of snake venoms by direct infusion nano‐electrospray ionization mass spectrometry: potential use in venom identification and taxonomy

et al. 2008

View full text Add to dashboard Cite

show abstract

“…There have been several mass fingerprinting studies of scorpion venoms from New World scorpions (see inter alia ,5, 7, 12, 18, 30–34) and two from African Old World scorpions 15, 35. This study is the first such report on an Old World Asian scorpion.…”

Section: Resultsmentioning

confidence: 76%

Mass fingerprinting of toxic fractions from the venom of the Indian red scorpion,Mesobuthus tamulus: biotope‐specific variation in the expression of venom peptides

Newton

Clench

Deshmukh

et al. 2007

Rapid Comm Mass Spectrometry

View full text Add to dashboard Cite

The red scorpion, Mesobuthus tamulus, is found in two distinct biotopes within the Indian state of Maharastra-a tropical, sea-level biotope and a semi-arid biotope, up to 600 m. Scorpions from these two geographical areas show marked differences in toxicity. Using mass spectrometry, we have shown biotope-specific variation in the expression of peptides from scorpions collected from these two distinct areas. Matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOFMS) and reversed-phase liquid chromatography/electrospray ionisation mass spectrometry (LC/ESI-MS) were assessed as techniques for obtaining mass fingerprint data. On line LC/ ESI-MS was judged to be the method of choice and unique biotope-specific mass fingerprints, with key diagnostic markers, were obtained.

show abstract

“…Because of the evidently high reproducibility of MS peaks in the range of m/z values characteristic for the long‐chain Na + channel toxins, this group was chosen as the basis for constructing the venom profiles for categorizing the 16 Parabuthus species. Typical α‐effects that correlate with these toxins were described for Parabuthus by Badenhorst 36,. 38,, 40…”

Section: Resultsmentioning

confidence: 93%

“…The venom composition of scorpions of southern Africa is largely unknown, and its analysis has only recently been started for some species of the Parabuthus genus 15,. 36 Because the severity of scorpion envenomation, ranging from local pain to generalized neurological symptoms and death, varies between scorpion families, genera and species, the composition of the venom and quantity of different groups of toxins are expected to vary. Figure 1 illustrates a comparison of the mass spectral patterns for two important scorpion families in southern Africa: Buthidae, with the medically most important genus Parabuthus ( P. schlechteri shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Determination of species‐specific components in the venom of Parabuthus scorpions from southern Africa using matrix‐assisted laser desorption time‐of‐flight mass spectrometry

Dyason

Brandt

Prendini

et al. 2002

Rapid Comm Mass Spectrometry

Self Cite

View full text Add to dashboard Cite

The aim of the present study was to analyze mass spectra of scorpions belonging to the genus Parabuthus (Pocock 1890) by means of matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOFMS) and to construct a species-specific venom code for species identification. The venom compositions of sixteen Parabuthus species, occurring in southern Africa, were characterized using representative peaks in the molecular mass range of 6400-8400 Da. This mass range is characteristic for the typical long-chain neurotoxins influencing sodium channels. Only a few of these peptides have been sequenced up to now. The impetus for development of these species-specific profiles was the observation of unique, highly reproducible mass spectral peaks within a specific species. An identification label for all the different species could be found using a minimum number of peaks. MALDI-TOFMS is therefore proposed as a complementary method to morphological and behavioural characteristics for species and ultimately subspecies discrimination.

show abstract

Comparison and characterization of the venoms of three Parabuthus scorpion species occurring in southern Africa

Cited by 29 publications

References 22 publications

Peptide fingerprinting of snake venoms by direct infusion nano‐electrospray ionization mass spectrometry: potential use in venom identification and taxonomy

Peptide fingerprinting of snake venoms by direct infusion nano‐electrospray ionization mass spectrometry: potential use in venom identification and taxonomy

Mass fingerprinting of toxic fractions from the venom of the Indian red scorpion,Mesobuthus tamulus: biotope‐specific variation in the expression of venom peptides

Determination of species‐specific components in the venom of Parabuthus scorpions from southern Africa using matrix‐assisted laser desorption time‐of‐flight mass spectrometry

Contact Info

Product

Resources

About