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Bitis gabonica rhinoceros, Snake Venom

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[#TXL1105-250] Bitis gabonica rhinoceros, Snake Venom

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TXL1105-250 | Bitis gabonica rhinoceros, Snake Venom, 250 mg.
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(1) Development of Equine IgG Antivenoms against Major Snake Groups in Mozambique.[TOP]

Pubmed ID :26730709
Publication Date : //
Snake envenoming is a significant public health problem in underdeveloped and developing countries. In sub-Saharan Africa, it is estimated that 90,000-400,000 envenomations occur each year, resulting in 3,500-32,000 deaths. Envenomings are caused by snakes from the Viperidae (Bitis spp. and Echis spp.) and Elapidae (Naja spp. and Dendroaspis spp.) families. The African continent has been suffering from a severe antivenom crisis and current antivenom production is only sufficient to treat 25% of snakebite cases. Our aim is to develop high-quality antivenoms against the main snake species found in Mozambique.

Authors : Guidolin Felipe Raimondi, Caricati Celso Pereira, Marcelino José Roberto, da Silva Wilmar Dias,



(2) New proline-rich oligopeptides from the venom of African adders: Insights into the hypotensive effect of the venoms.[TOP]

Pubmed ID :25688758
Publication Date : //
The snakes from the Bitis genus are some of the most medically important venomous snakes in sub Saharan Africa, however little is known about the composition and effects of these snake venom peptides. Considering that the victims with Bitis genus snakes have exacerbate hypotension and cardiovascular disorders, we investigated here the presence of angiotensin-converting enzyme modulators on four different species of venoms.

Authors : Kodama Roberto T, Cajado-Carvalho Daniela, Kuniyoshi Alexandre K, Kitano Eduardo S, Tashima Alexandre K, Barna Barbara F, Takakura Ana Carolina, Serrano Solange M T, Dias-Da-Silva Wilmar, Tambourgi Denise V, Portaro Fernanda V,



(3) African adders: partial characterization of snake venoms from three Bitis species of medical importance and their neutralization by experimental equine antivenoms.[TOP]

Pubmed ID :25643358
Publication Date : //
An alarming number of fatal accidents involving snakes are annually reported in Africa and most of the victims suffer from permanent local tissue damage and chronic disabilities. Envenomation by snakes belonging to the genus Bitis, Viperidae family, are common in Sub-Saharan Africa. The accidents are severe and the victims often have a poor prognosis due to the lack of effective specific therapies. In this study we have biochemically characterized venoms from three different species of Bitis, i.e., Bitis arietans, Bitis gabonica rhinoceros and Bitis nasicornis, involved in the majority of the human accidents in Africa, and analyzed the in vitro neutralizing ability of two experimental antivenoms.

Authors : Paixão-Cavalcante Danielle, Kuniyoshi Alexandre K, Portaro Fernanda C V, da Silva Wilmar Dias, Tambourgi Denise V,



(4) Non-contaminating camouflage: multifunctional skin microornamentation in the West African Gaboon viper (Bitis rhinoceros).[TOP]

Pubmed ID :24599379
Publication Date : //
The West African Gaboon viper (Bitis rhinoceros) has an extraordinary coloration of pale brown and velvety black markings. The velvety black appearance is caused by a unique hierarchical surface structures which was not found on the pale brown scales. In the present study we examined the wettability of the vipeŕs scales by measuring contact angles of water droplets. Velvet black scale surfaces had high static contact angles beyond 160° and low roll-off angles below 20° indicating an outstanding superhydrophobicity. Our calculations showed that the Cassie-Baxter model describes well wettability effects for these surfaces. Self-cleaning capabilities were determined by contaminating the scales with particles and fogging them until droplets formed. Black scales were clean after fogging, while pale scales stayed contaminated. Black scales feature multifunctional structures providing not only water-repellent but also self-cleaning properties. The pattern of nanoridges can be used as a model for surface-active technical surfaces.

Authors : Spinner Marlene, Gorb Stanislav N, Balmert Alexander, Bleckmann Horst, Westhoff Guido,



(5) Snake velvet black: hierarchical micro- and nanostructure enhances dark colouration in Bitis rhinoceros.[TOP]

Pubmed ID :23677278
Publication Date : //
The West African Gaboon viper (Bitis rhinoceros) is a master of camouflage due to its colouration pattern. Its skin is geometrically patterned and features black spots that purport an exceptional spatial depth due to their velvety surface texture. Our study shades light on micromorphology, optical characteristics and principles behind such a velvet black appearance. We revealed a unique hierarchical pattern of leaf-like microstructures striated with nanoridges on the snake scales that coincides with the distribution of black colouration. Velvet black sites demonstrate four times lower reflectance and higher absorbance than other scales in the UV-near IR spectral range. The combination of surface structures impeding reflectance and absorbing dark pigments, deposited in the skin material, provides reflecting less than 11% of the light reflected by a polytetrafluoroethylene diffuse reflectance standard in any direction. A view-angle independent black structural colour in snakes is reported here for the first time.

Authors : Spinner Marlene, Kovalev Alexander, Gorb Stanislav N, Westhoff Guido,



(6) Rhinocetin, a venom-derived integrin-specific antagonist inhibits collagen-induced platelet and endothelial cell functions.[TOP]

Pubmed ID :22689571
Publication Date : //
Snaclecs are small non-enzymatic proteins present in viper venoms reported to modulate hemostasis of victims through effects on platelets, vascular endothelial, and smooth muscle cells. In this study, we have isolated and functionally characterized a snaclec that we named "rhinocetin" from the venom of West African gaboon viper, Bitis gabonica rhinoceros. Rhinocetin was shown to comprise α and β chains with the molecular masses of 13.5 and 13 kDa, respectively. Sequence and immunoblot analysis of rhinocetin confirmed this to be a novel snaclec. Rhinocetin inhibited collagen-stimulated activation of human platelets in a dose-dependent manner but displayed no inhibitory effects on glycoprotein VI (collagen receptor) selective agonist, CRP-XL-, ADP-, or thrombin-induced platelet activation. Rhinocetin antagonized the binding of monoclonal antibodies against the α2 subunit of integrin α2β1 to platelets and coimmunoprecipitation analysis confirmed integrin α2β1 as a target for this venom protein. Rhinocetin inhibited a range of collagen-induced platelet functions such as fibrinogen binding, calcium mobilization, granule secretion, aggregation, and thrombus formation. It also inhibited integrin α2β1-dependent functions of human endothelial cells. Together, our data suggest rhinocetin to be a modulator of integrin α2β1 function and thus may provide valuable insights into the role of this integrin in physiological and pathophysiological scenarios, including hemostasis, thrombosis, and envenomation.

Authors : Vaiyapuri Sakthivel, Hutchinson E Gail, Ali Marfoua S, Dannoura Abeer, Stanley Ronald G, Harrison Robert A, Bicknell Andrew B, Gibbins Jonathan M,



(7) Evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis gabonica rhinoceros.[TOP]

Pubmed ID :21731776
Publication Date : //
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.

Authors : Vaiyapuri Sakthivel, Wagstaff Simon C, Harrison Robert A, Gibbins Jonathan M, Hutchinson E Gail,



(8) Purification and functional characterisation of rhiminopeptidase A, a novel aminopeptidase from the venom of Bitis gabonica rhinoceros.[TOP]

Pubmed ID :20706583
Publication Date : //
Snake bite is a major neglected public health issue within poor communities living in the rural areas of several countries throughout the world. An estimated 2.5 million people are bitten by snakes each year and the cost and lack of efficacy of current anti-venom therapy, together with the lack of detailed knowledge about toxic components of venom and their modes of action, and the unavailability of treatments in rural areas mean that annually there are around 125,000 deaths worldwide. In order to develop cheaper and more effective therapeutics, the toxic components of snake venom and their modes of action need to be clearly understood. One particularly poorly understood component of snake venom is aminopeptidases. These are exo-metalloproteases, which, in mammals, are involved in important physiological functions such as the maintenance of blood pressure and brain function. Although aminopeptidase activities have been reported in some snake venoms, no detailed analysis of any individual snake venom aminopeptidases has been performed so far. As is the case for mammals, snake venom aminopeptidases may also play important roles in altering the physiological functions of victims during envenomation. In order to further understand this important group of snake venom enzymes we have isolated, functionally characterised and analysed the sequence-structure relationships of an aminopeptidase from the venom of the large, highly venomous West African gaboon viper, Bitis gabonica rhinoceros.

Authors : Vaiyapuri Sakthivel, Wagstaff Simon C, Watson Kimberley A, Harrison Robert A, Gibbins Jonathan M, Hutchinson E Gail,



(9) Purification and functional characterisation of rhinocerase, a novel serine protease from the venom of Bitis gabonica rhinoceros.[TOP]

Pubmed ID :20300193
Publication Date : //
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.

Authors : Vaiyapuri Sakthivel, Harrison Robert A, Bicknell Andrew B, Gibbins Jonathan M, Hutchinson Gail,



(10) Inhibition of the myotoxic activities of three African Bitis venoms (B. rhinoceros, B. arietans and B. nasicornis) by a polyvalent antivenom.[TOP]

Pubmed ID :19857507
Publication Date : //
A murine model of venom-induced myotoxicity was used to assess the antimyotoxic capacity of a polyvalent antivenom (PAV), rich in F(ab')2 fragments, obtained from horses immunized with Bitis venoms. Intramuscular (i.m.) injection of Bitis rhinoceros, Bitis arietans or Bitis nasicornis into mice induced a time- and dose-dependent increase in plasma CK activity. The area under the plasma CK activity vs. time curve (AUC) between 0 and 48 h was used to quantify the data. Pre-incubation with PAV neutralized the venoms' myotoxicity, in a concentration-dependent manner: 80-100% neutralization occurred when the ratio of the PAV volume to the venom mass was 3-fold that recommended for use in human envenomation. Intravenous administration of PAV 1 h before the i.m. venom injection, afforded significant protection against myotoxicity, especially in the case of B. arietans. An antimyotoxic effect was also observed, albeit reduced, when the PAV treatment was applied 1 h after the venom injection. These data indicate that a PAV developed and manufactured in Brazil protects against the myotoxicity of the venoms of B. rhinoceros, B. arietans or B. nasicornis, which account for a large number of snakebite accidents in the African continent.

Authors : Ponte Cristiano Gonçalves, Nóbrega Eduardo Lira, Fernandes Vanessa Câmara, da Silva Wilmar Dias, Suarez-Kurtz Guilherme,