Expression of recombinant human antibody fragments capable of inhibiting the phospholipase and myotoxic activities of Bothrops jararacussu venom

Tamarozzi, M. B.; Soares, Sandro G.; Marcussi, Silvana; Giglio, José Roberto; Barbosa, José Elpídio

doi:10.1016/j.bbagen.2006.04.008

Cited by 39 publications

(36 citation statements)

References 28 publications

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“…A promising future alternative for treatment with specific monoclonal or humanized antibodies is likely (24,(43)(44)(45)(46). The production of humanized antibodies like single-chain Fv expressed in philamentous phage could replace heterologous antisera, thereby reducing the probability of adverse reaction (47). Studies identifying toxicity factors and the similarity among toxin structures allow the production of antibodies that confer cross neutralization and are a good starting point to develop monoclonal therapy and vaccines (48,49).…”

Section: Reaction)mentioning

confidence: 99%

Snake antivenoms: adverse reactions and production technology

Morais¹,

Massaldi²

2009

J. Venom. Anim. Toxins incl. Trop. Dis

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Antivenoms have been widely used for more than a century for treating snakebites and other accidents with poisonous animals. Despite their efficacy, the use of heterologous antivenoms involves the possibility of adverse reactions due to activation of the immune system. In this paper, alternatives for antivenom production already in use were evaluated in light of their ability to minimize the occurrence of adverse reactions. These effects were classified according to their molecular mechanism as: anaphylactic reactions mediated by IgE, anaphylactoid reactions caused by complement system activation, and pyrogenic reactions produced mainly by the presence of endotoxins in the final product. In the future, antivenoms may be replaced by humanized antibodies, specific neutralizing compounds or vaccination. Meanwhile, improvements in antivenom quality will be focused on the obtainment of a more purified and specific product in compliance with good manufacturing practices and at an affordable cost.

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Section: Reaction)mentioning

confidence: 99%

Snake antivenoms: adverse reactions and production technology

Morais¹,

Massaldi²

2009

J. Venom. Anim. Toxins incl. Trop. Dis

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“…A modified kinetic indirect hemolytic assay, standardized in our laboratory (Tamarozzi et al, 2006), was performed to measure PLA 2 activity. We used egg yolk as a substrate to develop a turbidimetric assay based on the capacity of snake venom PLA 2 s to hydrolyze egg phosphatidylcholine, producing lysophosphatidylcholine and fatty acids.…”

Section: Hemolytic Activitymentioning

confidence: 99%

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

Campos

Pucca

Roncolato

et al. 2013

Toxicon

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In various types of snake venom, the major toxic components are proteinases and members of the phospholipase A2 family, although other enzymes also contribute to the toxicity. In this study, we evaluated the proteolytic, phospholipase, and L-Amino acid oxidase activities in the venom of five Bothrops species-Bothrops jararaca, Bothrops jararacussu, Bothrops moojeni, Bothrops neuwiedi, and Bothrops alternatus-all of which are used in the production of commercial antivenom, prepared in horses. The enzymatic activities of each species' venom were classified as high, moderate, or low. B. moojeni venom demonstrated the highest enzymatic activity profile, followed by the venom of B. neuwiedi, B. jararacussu, B. jararaca, and B. alternatus. To our knowledge, this is the first study to compare all of these enzymes from multiple species, which is significant in view of the activity of L-amino acid oxidase across Bothrops species.

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“…Snake venoms are complex mixtures of proteins including phospholipases A2, myotoxins, hemorrhagic metalloproteases and other proteolytic enzymes, cytotoxins, cardiotoxins and others [17]. In spite of the fact that viperid venoms may contain well over 100 protein components, venom proteins belong to only a few major protein families, including enzymes (serine proteinases, Zn 2 C-metalloproteases, Lamino acid oxidase, group II PLA2) and proteins without enzymatic activity (ohanin, disintegrins, C-type lectins, natriuretic peptides, myotoxins, cysteine-rich secretory protein (CRISP) toxins, nerve and vascular endothelium growth factors, cystatin, and Kunitz-type protease inhibitors) (reviewed in [18]).…”

Section: Sweet-venommentioning

confidence: 99%

Venom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins

Soares¹,

Oliveira²

2009

PPL

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Protein glycosylation represents one of the most important post-translational events, and is a mean of diversifying a protein without recourse to the genome. The venoms produced by snakes contain an abundance of glycoproteins with N-linked carbohydrates. N-linked glycosylation can ensure the correct folding of important functional domains. Characterization of carbohydrates structures aids in development of human therapeutics by snake venom toxins.

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Expression of recombinant human antibody fragments capable of inhibiting the phospholipase and myotoxic activities of Bothrops jararacussu venom

Cited by 39 publications

References 28 publications

Snake antivenoms: adverse reactions and production technology

Snake antivenoms: adverse reactions and production technology

In vitro comparison of enzymatic effects among Brazilian Bothrops spp. venoms

Venom-Sweet-Venom: N-Linked Glycosylation in Snake Venom Toxins

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