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Juan J. Calvete - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus
Journal of proteomics, 2011Co-Authors: Carlos Corrêa-netto, Libia Sanz, Inácio De L. M. Junqueira-de-azevedo, Débora Andrade Silva, Moema Leitão-de-araujo, Maria Lucia Machado Alves, Debora Foguel, Russolina B. Zingali, Juan J. CalveteAbstract:Abstract The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris . The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 ( M. altirostris ) and 10 ( M. corallinus ) 3FTxs, and 3 ( M. altirostris ) and 1 ( M. corallinus ) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris ; serine proteinase in M. corallinus ) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to Peripheral Paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus , venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti- Micrurus ( corallinus and frontalis ) antivenom produced by Instituto Butantan quantitatively immunodepleted the minor toxins from M. altirostris and M. corallinus venoms but showed impaired crossreactivity towards their major 3FTx and PLA 2 molecules. The structural diversity of 3FTxs among Micrurus sp. may underlay the impaired cross-immunoreactivity of the Butantan antivenom towards M. altirostris and M. corallinus toxins, hampering the possibility to raise an antivenom against a simple venom mixture exhibiting paraspecific neutralization of other Micrurus venoms.
Carlos Corrêa-netto - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus
Journal of proteomics, 2011Co-Authors: Carlos Corrêa-netto, Libia Sanz, Inácio De L. M. Junqueira-de-azevedo, Débora Andrade Silva, Moema Leitão-de-araujo, Maria Lucia Machado Alves, Debora Foguel, Russolina B. Zingali, Juan J. CalveteAbstract:Abstract The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris . The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 ( M. altirostris ) and 10 ( M. corallinus ) 3FTxs, and 3 ( M. altirostris ) and 1 ( M. corallinus ) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris ; serine proteinase in M. corallinus ) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to Peripheral Paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus , venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti- Micrurus ( corallinus and frontalis ) antivenom produced by Instituto Butantan quantitatively immunodepleted the minor toxins from M. altirostris and M. corallinus venoms but showed impaired crossreactivity towards their major 3FTx and PLA 2 molecules. The structural diversity of 3FTxs among Micrurus sp. may underlay the impaired cross-immunoreactivity of the Butantan antivenom towards M. altirostris and M. corallinus toxins, hampering the possibility to raise an antivenom against a simple venom mixture exhibiting paraspecific neutralization of other Micrurus venoms.
Libia Sanz - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus
Journal of proteomics, 2011Co-Authors: Carlos Corrêa-netto, Libia Sanz, Inácio De L. M. Junqueira-de-azevedo, Débora Andrade Silva, Moema Leitão-de-araujo, Maria Lucia Machado Alves, Debora Foguel, Russolina B. Zingali, Juan J. CalveteAbstract:Abstract The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris . The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 ( M. altirostris ) and 10 ( M. corallinus ) 3FTxs, and 3 ( M. altirostris ) and 1 ( M. corallinus ) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris ; serine proteinase in M. corallinus ) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to Peripheral Paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus , venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti- Micrurus ( corallinus and frontalis ) antivenom produced by Instituto Butantan quantitatively immunodepleted the minor toxins from M. altirostris and M. corallinus venoms but showed impaired crossreactivity towards their major 3FTx and PLA 2 molecules. The structural diversity of 3FTxs among Micrurus sp. may underlay the impaired cross-immunoreactivity of the Butantan antivenom towards M. altirostris and M. corallinus toxins, hampering the possibility to raise an antivenom against a simple venom mixture exhibiting paraspecific neutralization of other Micrurus venoms.
Inácio De L. M. Junqueira-de-azevedo - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus
Journal of proteomics, 2011Co-Authors: Carlos Corrêa-netto, Libia Sanz, Inácio De L. M. Junqueira-de-azevedo, Débora Andrade Silva, Moema Leitão-de-araujo, Maria Lucia Machado Alves, Debora Foguel, Russolina B. Zingali, Juan J. CalveteAbstract:Abstract The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris . The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 ( M. altirostris ) and 10 ( M. corallinus ) 3FTxs, and 3 ( M. altirostris ) and 1 ( M. corallinus ) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris ; serine proteinase in M. corallinus ) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to Peripheral Paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus , venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti- Micrurus ( corallinus and frontalis ) antivenom produced by Instituto Butantan quantitatively immunodepleted the minor toxins from M. altirostris and M. corallinus venoms but showed impaired crossreactivity towards their major 3FTx and PLA 2 molecules. The structural diversity of 3FTxs among Micrurus sp. may underlay the impaired cross-immunoreactivity of the Butantan antivenom towards M. altirostris and M. corallinus toxins, hampering the possibility to raise an antivenom against a simple venom mixture exhibiting paraspecific neutralization of other Micrurus venoms.
Débora Andrade Silva - One of the best experts on this subject based on the ideXlab platform.
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Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus
Journal of proteomics, 2011Co-Authors: Carlos Corrêa-netto, Libia Sanz, Inácio De L. M. Junqueira-de-azevedo, Débora Andrade Silva, Moema Leitão-de-araujo, Maria Lucia Machado Alves, Debora Foguel, Russolina B. Zingali, Juan J. CalveteAbstract:Abstract The venom proteomes of Micrurus altirostris and M. corallinus were analyzed by combining snake venomics and venom gland transcriptomic surveys. In both coral snake species, 3FTx and PLA 2 were the most abundant and diversified toxin families. 33 different 3FTxs and 13 PLA 2 proteins, accounting respectively for 79.5% and 13.7% of the total proteins, were identified in the venom of M. altirostris . The venom of M. corallinus comprised 10 3FTx (81.7% of the venom proteome) and 4 (11.9%) PLA 2 molecules. Transcriptomic data provided the full-length amino acid sequences of 18 ( M. altirostris ) and 10 ( M. corallinus ) 3FTxs, and 3 ( M. altirostris ) and 1 ( M. corallinus ) novel PLA 2 sequences. In addition, venom from each species contained single members of minor toxin families: 3 common (PIII-SVMP, C-type lectin-like, L-amino acid oxidase) and 4 species-specific (CRISP, Kunitz-type inhibitor, lysosomal acid lipase in M. altirostris ; serine proteinase in M. corallinus ) toxin classes. The finding of a lipase (LIPA) in the venom proteome and in the venom gland transcriptome of M. altirostris supports the view of a recruitment event predating the divergence of Elapidae and Viperidae more than 60 Mya. The toxin profile of both M. altirostris and M. corallinus venoms points to 3FTxs and PLA 2 molecules as the major players of the envenoming process. In M. altirostris venom, all major, and most minor, 3FTxs display highest similarity to type I α-neurotoxins, suggesting that these postsynaptically acting toxins may play the predominant role in the neurotoxic effect leading to Peripheral Paralysis, respiratory arrest, and death. M. corallinus venom posesses both, type I α-neurotoxins and a high-abundance (26% of the venom proteome) protein of subfamily XIX of 3FTxs, exhibiting similarity to bucandin from Malayan krait, Bungarus candidus , venom, which enhances acetylcholine release presynaptically. This finding may explain the presynaptic neurotoxicity of M. corallinus venom and the lack of this effect in M. altirostris venom. The anti- Micrurus ( corallinus and frontalis ) antivenom produced by Instituto Butantan quantitatively immunodepleted the minor toxins from M. altirostris and M. corallinus venoms but showed impaired crossreactivity towards their major 3FTx and PLA 2 molecules. The structural diversity of 3FTxs among Micrurus sp. may underlay the impaired cross-immunoreactivity of the Butantan antivenom towards M. altirostris and M. corallinus toxins, hampering the possibility to raise an antivenom against a simple venom mixture exhibiting paraspecific neutralization of other Micrurus venoms.