The Experts below are selected from a list of 174 Experts worldwide ranked by ideXlab platform
Libia Sanz - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics of Bitis species reveals large intragenus venom toxin composition variation: application to taxonomy of congeneric taxa.
Journal of proteome research, 2007Co-Authors: José Escolano, Libia SanzAbstract:The protein composition of the venoms of the West African Gaboon viper (Bitis Gabonica rhinoceros), the rhinoceros viper (Bitis nasicornis), and the horned puff adder (Bitis caudalis) were analyzed...
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Snake venomics of Bitis Gabonica Gabonica. Protein family composition, subunit organization of venom toxins, and characterization of dimeric disintegrins Bitisgabonin-1 and Bitisgabonin-2.
Journal of proteome research, 2007Co-Authors: Cezary Marcinkiewicz, Libia SanzAbstract:The protein composition of the venom of the East African Gaboon viper (Bitis Gabonica Gabonica) was analyzed using RP-HPLC, N-terminal sequencing, MALDI-TOF peptide mass fingerprinting, and CID−MS/...
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Snake Venomics of Bitis Species Reveals Large Intragenus Venom Toxin Composition Variation: Application to Taxonomy of
2007Co-Authors: Congeneric Taxa, Juan J. Calvete, José Escolano, Libia SanzAbstract:The protein composition of the venoms of the West African Gaboon viper (Bitis Gabonica rhinoceros), the rhinoceros viper (Bitis nasicornis), and the horned puff adder (Bitis caudalis) were analyzed by RP-HPLC, N-terminal sequencing, SDS-PAGE, MALDI-TOF peptide mass fingerprinting, and CID-MS/ MS. In line with previous proteomic and transcriptomic analyses showing that snake venom proteins belong to only a few major protein families, the venom proteomes of Bitis Gabonica rhinoceros, Bitis nasicornis, and Bitis caudalis comprise, respectively, toxins from 11, 9, and 8 toxin families. Dimeric disintegrins, PLA2 molecules, serine proteinases, a CRISP, C-type lectin-like proteins, L-amino acid oxidases, and snake venom metalloproteases are present in the three Bitis snake venoms, though they depart from each other in the composition and the relative abundance of their toxins. The venom composition appears to keep information on the evolutionary history of congeneric taxa. Protein similarity coefficients used to estimate the similarity of venom proteins of the Bitis taxa sampled here and in previous studies (eg. Bitis arietans and Bitis Gabonica Gabonica) support the monophyly of the three West African taxa (B.g. Gabonica, B.g. rhinoceros, and B. nasicornis) based on genetic distance reconstructions, the lack of alliances between B. arietans and any other Bitis species, and are consistent with the taxonomic association of Bitis caudalis within the differentiated group of small Bitis species. The low level of venom toxin composition similarity between the two conventionally recognized subspecies of Bitis Gabonica, B. g. Gabonica and B. g. rhinoceros, supports the consideration by some authors of B. g. rhinoceros as a separate species, Bitis rhinoceros. Moreover, our proteomic data fit better to a weighted phylogram based on overall genetic distances than to an unweighted maximum-parsimony tree
Jonathan M Gibbins - One of the best experts on this subject based on the ideXlab platform.
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Purification and Functional Characterisation of Rhinocerase, a Novel Serine Protease from the Venom of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Andrew B. Bicknell, Jonathan M GibbinsAbstract:Background: Serine proteases are a major component of viper venoms and are thought to disrupt several distinct elements of the blood coagulation system of envenomed victims. A detailed understanding of the functions of these enzymes is important both for acquiring a fuller understanding of the pathology of envenoming and because these venom proteins have shown potential in treating blood coagulation disorders. Methodology/Principal Findings: In this study a novel, highly abundant serine protease, which we have named rhinocerase, has been isolated and characterised from the venom of Bitis Gabonica rhinoceros using liquid phase isoelectric focusing and gel filtration. Like many viper venom serine proteases, this enzyme is glycosylated; the estimated molecular mass of the native enzyme is approximately 36kDa, which reduces to 31kDa after deglycosylation. The partial amino acid sequence shows similarity to other viper venom serine proteases, but is clearly distinct from the sequence of the only other sequenced serine protease from Bitis Gabonica. Other viper venom serine proteases have been shown to exert distinct biological effects, and our preliminary functional characterization of rhinocerase suggest it to be multifunctional. It is capable of degrading a and b chains of fibrinogen, dissolving plasma clots and of hydrolysing a kallikrein substrate. Conclusions/Significance: A novel multifunctional viper venom serine protease has been isolated and characterised. The activities of the enzyme are consistent with the known in vivo effects of Bitis Gabonica envenoming, including bleedin
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Evolutionary Analysis of Novel Serine Proteases in the Venom Gland Transcriptome of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, E. GailAbstract:Background: Serine proteases are major components of viper venom and target various stages of the blood coagulation system in victims and prey. A better understanding of the diversity of serine proteases and other enzymes present in snake venom will help to understand how the complexity of snake venom has evolved and will aid the development of novel therapeutics for treating snake bites. Methodology and Principal Findings: Four serine protease-encoding genes from the venom gland transcriptome of Bitis Gabonica rhinoceros were amplified and sequenced. Mass spectrometry suggests the four enzymes corresponding to these genes are present in the venom of B. g. rhinoceros. Two of the enzymes, rhinocerases 2 and 3 have substitutions to two of the serine protease catalytic triad residues and are thus unlikely to be catalytically active, though they may have evolved other toxic functions. The other two enzymes, rhinocerases 4 and 5, have classical serine protease catalytic triad residues and thus are likely to be catalytically active, however they have glycine rather than the more typical aspartic acid at the base of the primary specificity pocket (position 189). Based on a detailed analysis of these sequences we suggest that alternative splicing together with individual amino acid mutations may have been involved in their evolution. Changes within amino acid segments which were previously proposed to undergo accelerated change in venom serine proteases have also been observed
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Sequence alignment of rhinocerase with other VVSPs.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Jonathan M Gibbins, Andrew B. Bicknell, Gail HutchinsonAbstract:The rhinocerase sequence obtained by Edman degradation was aligned with BGSP, the only known serine protease sequence from Bitis Gabonica (NCBI accession number: AAR24534) and two other VVSP sequences; bothrombin (NCBI accession number: P81661) and ancrod (NCBI accession number: AAA49195). The sequence identified by Q-TOF is underlined. ★ indicates conserved residues, : indicates biochemically more related residues and. indicates biochemically less related residues.
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Phylogenetic tree showing relationship between serine protease homologues and serine proteases from the same snakes.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:65 amino acid sequences from 10 snakes were included together with bovine α-chymotrypsinogen (NCBI accession number: P00766) which was used as an outgroup. The alignment was generated using ClustalW [12] within MEGA 4 [16] using a gap opening penalty of 10 and a gap extension penalty of 0.1 for the initial pairwise alignment, gap opening penalty of 3 and gap extension penalty of 1.8 for the multiple alignment and the Gonnet protein weight matrix. The phylogenetic tree was generated from this within MEGA 4 using the neighbour-joining method and the Jones-Taylor-Thornton substitution model. The bootstrap test was done using 2000 replications. In the diagram sequences are identified using a code which consists of up to 3 characters representing the snake name, (TG: Trimeresurus gramineus; VS: Viridovipera stejnegeri; TJ: Trimeresurus jerdonii; BJu: Bothrops jararacussu ; ML: Macrovipera lebetina; EO: Echis ocellatus; BG: Bitis Gabonica; Bja: Bothrops jararaca; TF: Trimeresurus flavoviridis; BAs: Bothrops asper) followed by a dash and then up to 5 characters representing the protein name. Where possible NCBI accession numbers are also included. ML-P3 and ML-P4 sequences were obtained directly from the sequences named VLP3 and VLP4 in [5]. Red circles indicate the sequences with mutations to the catalytic triad.
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evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis Gabonica rhinoceros
PLOS ONE, 2011Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:Our study provides further insight into the diversity of serine protease isoforms present within snake venom and discusses their possible functions and how they may have evolved. These multiple serine protease isoforms with different substrate specificities may enhance the envenomation effects and help the snake to adapt to new habitats and diets. Our findings have potential for helping the future development of improved therapeutics for snake bites.
Robert A. Harrison - One of the best experts on this subject based on the ideXlab platform.
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Purification and Functional Characterisation of Rhinocerase, a Novel Serine Protease from the Venom of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Andrew B. Bicknell, Jonathan M GibbinsAbstract:Background: Serine proteases are a major component of viper venoms and are thought to disrupt several distinct elements of the blood coagulation system of envenomed victims. A detailed understanding of the functions of these enzymes is important both for acquiring a fuller understanding of the pathology of envenoming and because these venom proteins have shown potential in treating blood coagulation disorders. Methodology/Principal Findings: In this study a novel, highly abundant serine protease, which we have named rhinocerase, has been isolated and characterised from the venom of Bitis Gabonica rhinoceros using liquid phase isoelectric focusing and gel filtration. Like many viper venom serine proteases, this enzyme is glycosylated; the estimated molecular mass of the native enzyme is approximately 36kDa, which reduces to 31kDa after deglycosylation. The partial amino acid sequence shows similarity to other viper venom serine proteases, but is clearly distinct from the sequence of the only other sequenced serine protease from Bitis Gabonica. Other viper venom serine proteases have been shown to exert distinct biological effects, and our preliminary functional characterization of rhinocerase suggest it to be multifunctional. It is capable of degrading a and b chains of fibrinogen, dissolving plasma clots and of hydrolysing a kallikrein substrate. Conclusions/Significance: A novel multifunctional viper venom serine protease has been isolated and characterised. The activities of the enzyme are consistent with the known in vivo effects of Bitis Gabonica envenoming, including bleedin
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Evolutionary Analysis of Novel Serine Proteases in the Venom Gland Transcriptome of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, E. GailAbstract:Background: Serine proteases are major components of viper venom and target various stages of the blood coagulation system in victims and prey. A better understanding of the diversity of serine proteases and other enzymes present in snake venom will help to understand how the complexity of snake venom has evolved and will aid the development of novel therapeutics for treating snake bites. Methodology and Principal Findings: Four serine protease-encoding genes from the venom gland transcriptome of Bitis Gabonica rhinoceros were amplified and sequenced. Mass spectrometry suggests the four enzymes corresponding to these genes are present in the venom of B. g. rhinoceros. Two of the enzymes, rhinocerases 2 and 3 have substitutions to two of the serine protease catalytic triad residues and are thus unlikely to be catalytically active, though they may have evolved other toxic functions. The other two enzymes, rhinocerases 4 and 5, have classical serine protease catalytic triad residues and thus are likely to be catalytically active, however they have glycine rather than the more typical aspartic acid at the base of the primary specificity pocket (position 189). Based on a detailed analysis of these sequences we suggest that alternative splicing together with individual amino acid mutations may have been involved in their evolution. Changes within amino acid segments which were previously proposed to undergo accelerated change in venom serine proteases have also been observed
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Sequence alignment of rhinocerase with other VVSPs.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Jonathan M Gibbins, Andrew B. Bicknell, Gail HutchinsonAbstract:The rhinocerase sequence obtained by Edman degradation was aligned with BGSP, the only known serine protease sequence from Bitis Gabonica (NCBI accession number: AAR24534) and two other VVSP sequences; bothrombin (NCBI accession number: P81661) and ancrod (NCBI accession number: AAA49195). The sequence identified by Q-TOF is underlined. ★ indicates conserved residues, : indicates biochemically more related residues and. indicates biochemically less related residues.
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Phylogenetic tree showing relationship between serine protease homologues and serine proteases from the same snakes.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:65 amino acid sequences from 10 snakes were included together with bovine α-chymotrypsinogen (NCBI accession number: P00766) which was used as an outgroup. The alignment was generated using ClustalW [12] within MEGA 4 [16] using a gap opening penalty of 10 and a gap extension penalty of 0.1 for the initial pairwise alignment, gap opening penalty of 3 and gap extension penalty of 1.8 for the multiple alignment and the Gonnet protein weight matrix. The phylogenetic tree was generated from this within MEGA 4 using the neighbour-joining method and the Jones-Taylor-Thornton substitution model. The bootstrap test was done using 2000 replications. In the diagram sequences are identified using a code which consists of up to 3 characters representing the snake name, (TG: Trimeresurus gramineus; VS: Viridovipera stejnegeri; TJ: Trimeresurus jerdonii; BJu: Bothrops jararacussu ; ML: Macrovipera lebetina; EO: Echis ocellatus; BG: Bitis Gabonica; Bja: Bothrops jararaca; TF: Trimeresurus flavoviridis; BAs: Bothrops asper) followed by a dash and then up to 5 characters representing the protein name. Where possible NCBI accession numbers are also included. ML-P3 and ML-P4 sequences were obtained directly from the sequences named VLP3 and VLP4 in [5]. Red circles indicate the sequences with mutations to the catalytic triad.
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evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis Gabonica rhinoceros
PLOS ONE, 2011Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:Our study provides further insight into the diversity of serine protease isoforms present within snake venom and discusses their possible functions and how they may have evolved. These multiple serine protease isoforms with different substrate specificities may enhance the envenomation effects and help the snake to adapt to new habitats and diets. Our findings have potential for helping the future development of improved therapeutics for snake bites.
Sakthivel Vaiyapuri - One of the best experts on this subject based on the ideXlab platform.
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Purification and Functional Characterisation of Rhinocerase, a Novel Serine Protease from the Venom of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Andrew B. Bicknell, Jonathan M GibbinsAbstract:Background: Serine proteases are a major component of viper venoms and are thought to disrupt several distinct elements of the blood coagulation system of envenomed victims. A detailed understanding of the functions of these enzymes is important both for acquiring a fuller understanding of the pathology of envenoming and because these venom proteins have shown potential in treating blood coagulation disorders. Methodology/Principal Findings: In this study a novel, highly abundant serine protease, which we have named rhinocerase, has been isolated and characterised from the venom of Bitis Gabonica rhinoceros using liquid phase isoelectric focusing and gel filtration. Like many viper venom serine proteases, this enzyme is glycosylated; the estimated molecular mass of the native enzyme is approximately 36kDa, which reduces to 31kDa after deglycosylation. The partial amino acid sequence shows similarity to other viper venom serine proteases, but is clearly distinct from the sequence of the only other sequenced serine protease from Bitis Gabonica. Other viper venom serine proteases have been shown to exert distinct biological effects, and our preliminary functional characterization of rhinocerase suggest it to be multifunctional. It is capable of degrading a and b chains of fibrinogen, dissolving plasma clots and of hydrolysing a kallikrein substrate. Conclusions/Significance: A novel multifunctional viper venom serine protease has been isolated and characterised. The activities of the enzyme are consistent with the known in vivo effects of Bitis Gabonica envenoming, including bleedin
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Evolutionary Analysis of Novel Serine Proteases in the Venom Gland Transcriptome of Bitis Gabonica rhinoceros
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, E. GailAbstract:Background: Serine proteases are major components of viper venom and target various stages of the blood coagulation system in victims and prey. A better understanding of the diversity of serine proteases and other enzymes present in snake venom will help to understand how the complexity of snake venom has evolved and will aid the development of novel therapeutics for treating snake bites. Methodology and Principal Findings: Four serine protease-encoding genes from the venom gland transcriptome of Bitis Gabonica rhinoceros were amplified and sequenced. Mass spectrometry suggests the four enzymes corresponding to these genes are present in the venom of B. g. rhinoceros. Two of the enzymes, rhinocerases 2 and 3 have substitutions to two of the serine protease catalytic triad residues and are thus unlikely to be catalytically active, though they may have evolved other toxic functions. The other two enzymes, rhinocerases 4 and 5, have classical serine protease catalytic triad residues and thus are likely to be catalytically active, however they have glycine rather than the more typical aspartic acid at the base of the primary specificity pocket (position 189). Based on a detailed analysis of these sequences we suggest that alternative splicing together with individual amino acid mutations may have been involved in their evolution. Changes within amino acid segments which were previously proposed to undergo accelerated change in venom serine proteases have also been observed
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Sequence alignment of rhinocerase with other VVSPs.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Jonathan M Gibbins, Andrew B. Bicknell, Gail HutchinsonAbstract:The rhinocerase sequence obtained by Edman degradation was aligned with BGSP, the only known serine protease sequence from Bitis Gabonica (NCBI accession number: AAR24534) and two other VVSP sequences; bothrombin (NCBI accession number: P81661) and ancrod (NCBI accession number: AAA49195). The sequence identified by Q-TOF is underlined. ★ indicates conserved residues, : indicates biochemically more related residues and. indicates biochemically less related residues.
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Phylogenetic tree showing relationship between serine protease homologues and serine proteases from the same snakes.
2013Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:65 amino acid sequences from 10 snakes were included together with bovine α-chymotrypsinogen (NCBI accession number: P00766) which was used as an outgroup. The alignment was generated using ClustalW [12] within MEGA 4 [16] using a gap opening penalty of 10 and a gap extension penalty of 0.1 for the initial pairwise alignment, gap opening penalty of 3 and gap extension penalty of 1.8 for the multiple alignment and the Gonnet protein weight matrix. The phylogenetic tree was generated from this within MEGA 4 using the neighbour-joining method and the Jones-Taylor-Thornton substitution model. The bootstrap test was done using 2000 replications. In the diagram sequences are identified using a code which consists of up to 3 characters representing the snake name, (TG: Trimeresurus gramineus; VS: Viridovipera stejnegeri; TJ: Trimeresurus jerdonii; BJu: Bothrops jararacussu ; ML: Macrovipera lebetina; EO: Echis ocellatus; BG: Bitis Gabonica; Bja: Bothrops jararaca; TF: Trimeresurus flavoviridis; BAs: Bothrops asper) followed by a dash and then up to 5 characters representing the protein name. Where possible NCBI accession numbers are also included. ML-P3 and ML-P4 sequences were obtained directly from the sequences named VLP3 and VLP4 in [5]. Red circles indicate the sequences with mutations to the catalytic triad.
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evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis Gabonica rhinoceros
PLOS ONE, 2011Co-Authors: Sakthivel Vaiyapuri, Robert A. Harrison, Simon C Wagstaff, Jonathan M Gibbins, Gail E HutchinsonAbstract:Our study provides further insight into the diversity of serine protease isoforms present within snake venom and discusses their possible functions and how they may have evolved. These multiple serine protease isoforms with different substrate specificities may enhance the envenomation effects and help the snake to adapt to new habitats and diets. Our findings have potential for helping the future development of improved therapeutics for snake bites.
James M Neenan - One of the best experts on this subject based on the ideXlab platform.
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spondyloarthropathy in vertebrae of the aquatic cretaceous snake lunaophis aquaticus and its first recognition in modern snakes
Naturwissenschaften, 2018Co-Authors: Adriana M Albino, Bruce M Rothschild, Jorge D Carrillobriceno, James M NeenanAbstract:Inflammatory arthritis is documented for the first time in snakes. Ossification of the intervertebral capsule and zygapophyseal joints resulting in segmental vertebral fusion was observed in the aquatic Cretaceous snake Lunaophis aquaticus. Such pathologic alterations are pathognomonic for the spondyloarthropathy form of inflammatory arthritis. A survey of 2144 snakes in recent collections, performed to identify Holocene prevalence, revealed only two occurrences in extant snakes. The findings in Bitis Gabonica and Elaphe taeniura were indistinguishable from those noted in Lunaophis aquaticus and identical to those previously recognized in modern varanids. The pathology likely represents a form of reactive arthritis related to enteropathic infection. While the disease probably did not affect general locomotion, its vertebral column position may have compromised mating.