Identification of Bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta

Castro, Helena C.; Fernandes, Márcio; Zingali, Russolina B.

doi:10.1016/s0041-0101(99)00087-2

Cited by 31 publications

(16 citation statements)

References 34 publications

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“…Nausea, hypotension, bradycardia, shock, and even death due to hemorrhagic, coagulant, and neurotoxic activities comprise the envenoming features ( Jorge et al 1997) and are probably a consequence of the direct action of the few molecules already characterized from L. muta. They are common pit viper toxins, such as serine proteases (Weinberg et al 2004), snake venom metalloproteases (SVMPs) , phospholipases A2 (PLA2s) (Damico et al 2005), and a C-type lectin (Castro et al 1999). …”

mentioning

confidence: 99%

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

et al. 2006

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Efforts to describe toxins from the two major families of venomous snakes (Viperidae and Elapidae) usually reveal proteins belonging to few structural types, particular of each family. Here we carried on an effort to determine uncommon cDNAs that represent possible new toxins from Lachesis muta (Viperidae). In addition to nine classes of typical toxins, atypical molecules never observed in the hundreds of Viperidae snakes studied so far are highly expressed: a diverging C-type lectin that is related to Viperidae toxins but appears to be independently originated; an ohanin-like toxin, which would be the third member of the most recently described class of Elapidae toxins, related to human butyrophilin and B30.2 proteins; and a 3FTx-like toxin, a new member of the widely studied three-finger family of proteins, which includes major Elapidae neurotoxins and CD59 antigen. The presence of these common and uncommon molecules suggests that the repertoire of toxins could be more conserved between families than has been considered, and their features indicate a dynamic process of venom evolution through molecular mechanisms, such as multiple recruitments of important scaffolds and domain exchange between paralogs, always keeping a minimalist nature in most toxin structures in opposition to their nontoxin counterparts.

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confidence: 99%

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

et al. 2006

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“…Los antivenenos se mostraron efectivos en la neutralización de la actividad hemorrágica, lo que indica la neutralización de las metaloproteinasas (hemorraginas o reprolisinas) del veneno. Esto era de esperar dada la alta similitud entre las diferentes metaloproteinasas (Bjarnasson y Fox 1994) y al hecho de que para este veneno se han descrito componentes hemorrágicos (Pessatti et al 1995) que presentan relación antigénica con la bothrojaragina de B. jararaca (Castro et al 1999).…”

Section: Discussionunclassified

“…Se describió también que posee baja cantidad de componentes con actividad de fosfolipasa A 2 y poca actividad miotóxica (Moura da Silva et al 1990Silva et al , 1991 y una alta actividad de L-aminoácido-oxidasa (Pessatti et al 1995). También se ha visto que posee una fracción altamente hemorrágica (Pessatti et al 1995) la cual tiene alta reactividad inmunoquímica con la bothrojaracina de Bothrops jararaca (Castro et al 1999). Sin embargo, no se dispone de datos de la toxicidad global del mismo así como de la neutralización de sus diferentes actividades tóxicas por antivenenos de uso terapéutico.…”

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Características biológicas e inmunológicas del veneno de Bothrops cotiara (Serpentes: Viperidae)

Roodt

Estévez²,

Dolab

et al. 2013

RBT

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Biological and immunological characteristics of the poison of Bothrops cotiara (Serpentes: Viperidae).Bothrops cotiara is a venomous snake sporadically found in the province of Misiones in Argentina, South of Brazil and Paraguay. Data on the clinics of the envenomation produced by its bite and on its venom are scarce. There is no information on the neutralizing capacity of the antivenoms available. In this study, the lethal potency, hemorrhagic, necrotizing, coagulant and thrombin-like, defibrinogenating, indirect hemolytic and fibrinolytic activities of the venom of B. cotiara specimens from the province of Misiones were determined. The toxic activities were within the range of those described for the other Bothrops species from Argentina, and the electrophoretic and chromatographic studies showed similarities with those described for the other bothropic venoms. The immunochemical reactivity of six South American anti Viper antivenoms (ELISA) have a strong reactivity with all the antivenoms studied. The neutralizing capacity of three of these therapeutic antivenoms against the lethal potency and hemorrhagic, necrotizing, coagulant, thrombin-like and hemolytic activities showed a very close neutralizing capacity. Our data strongly suggest that the antivenoms for therapeutic use available in this area of South America are useful to neutralize the toxic and enzymatic activities of the venom of this uncommon specie of Bothrops. Rev. Biol. Trop. 54 (3): 889-901. Epub 2006 Sept. 29.

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“…Proexosite I blockage decreases cleavage of prothrombin by FXa-FVa complex or prothrombinase complex [20]. BJC-like proteins are present in other Bothrops species and Lachesis muta venom, such as bothroalternin, a less potent human thrombin inhibitor, from Bothrops alternatus venom [21].…”

Section: Thrombin Inhibitorsmentioning

confidence: 99%

Snake Venom Proteins Affecting Platelets and Their Applications to Anti-Thrombotic Research

Clemetson

Lu²,

Clemetson

2007

CPD

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Snake venoms are very complex mixtures of biologically active proteins and peptides that may affect hemostasis in many ways, by activating or inhibiting coagulant factors or platelets, or by disrupting endothelium. They have been classified into various families, including serine proteases, metalloproteinases, C-type lectins, disintegrins and phospholipases. The various members of a particular family act selectively on different blood coagulation factors, blood cells or tissues. Venom proteins affect platelet function in particular by binding to and blocking or clustering and activating receptors or by cleaving receptors or von Willebrand factor. They may also activate protease-activated receptors or modulate ADP release or thromboxane A2 formation. L-amino acid oxidases activate platelets by producing H2O2. Many of these purified components are valuable tools in platelet research, providing new information about receptor function and signaling.

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Identification of Bothrojaracin-like proteins in snake venoms from Bothrops species and Lachesis muta

Cited by 31 publications

References 34 publications

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

Lachesis muta (Viperidae) cDNAs Reveal Diverging Pit Viper Molecules and Scaffolds Typical of Cobra (Elapidae) Venoms: Implications for Snake Toxin Repertoire Evolution

Características biológicas e inmunológicas del veneno de Bothrops cotiara (Serpentes: Viperidae)

Snake Venom Proteins Affecting Platelets and Their Applications to Anti-Thrombotic Research

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