Comparison of the partial proteomes of the venoms of Brazilian spiders of the genus Phoneutria

Richardson, Michael; Pimenta, Adriano M.C.; Bemquerer, Marcelo P.; Santoro, Marcelo M.; Beirão, Paulo Sérgio Lacerda; Lima, Maria Elena de; Figueiredo, Suely G.; Bloch, Carlos; Vasconcelos, Érico Augusto Rosas de; Campos, Francisco; Gomes, Paulo César; Cordeiro, Marta N.

doi:10.1016/j.cbpc.2005.09.010

Cited by 97 publications

(100 citation statements)

References 95 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We conclude that, in OtTx, as well as in OxyTx, the three core ICK disulfides (C ; the latter is in fact part of the ESM and is found in most spider toxins containing eight cysteine residues). Lower similarity (~38% identical residues in OtTx1) is noted with the Tx3-6 [29] and PRTx23C2 [30] toxins from the Brazilian spiders Phoneutria nigriventer and Phoneutria reidyi (Ctenidae) that are thought to target calcium channels. Interestingly, a sixth disulfide bridge is found in these Phoneutria toxins.…”

Section: Ottx Sequence Analysismentioning

confidence: 99%

Spider toxins comprising disulfide‐rich and linear amphipathic domains: a new class of molecules identified in the lynx spider Oxyopes takobius

et al. 2013

View full text Add to dashboard Cite

In addition to the conventional neurotoxins and cytotoxins, venom of the lynx spider Oxyopes takobius was found to contain two-domain modular toxins named spiderines: OtTx1a, 1b, 2a and 2b. These toxins show both insecticidal activity (a median lethal dose against flesh fly larvae of 75 lgÁg À1) and potent antimicrobial effects (minimal inhibitory concentrations in the range 0.1-10 lM). Full sequences of the purified spiderines were established by a combination of Edman degradation, mass spectrometry and cDNA cloning. They are relatively large molecules (~110 residues, 12.0-12.5 kDa) and consist of two distinct modules separated by a short linker. The N-terminal part (~40 residues) contains no cysteine residues, is highly cationic, forms amphipathic a-helical structures in a membrane-mimicking environment, and shows potent cytolytic effects on cells of various origins. The C-terminal part (~60 residues) is disulfide-rich (five S-S bonds), and contains the inhibitor cystine knot (ICK/knottin) signature. The N-terminal part of spiderines is very similar to linear cytotoxic peptides found in various organisms, whereas the C-terminal part corresponds to the usual spider neurotoxins. We synthesized the modules of OtTx1a and compared their activity to that of full-length mature toxin produced recombinantly, highlighting the importance of the N-terminal part, which retained full-length toxin activity in both insecticidal and antimicrobial assays. The unique structure of spiderines completes the range of two-domain spider toxins. DatabaseThe protein sequences of the spiderines (OtTx) reported in this paper have been submitted to the UniProt Knowledgebase (UniProtKB) under accession numbers P86716-P86719, and the nucleotide sequences encoding OtTx have been submitted to the GenBank under accession numbers JX134894-JX134897.

show abstract

Section: Ottx Sequence Analysismentioning

confidence: 99%

Spider toxins comprising disulfide‐rich and linear amphipathic domains: a new class of molecules identified in the lynx spider Oxyopes takobius

et al. 2013

View full text Add to dashboard Cite

show abstract

“…While enzymes are present in the majority of venoms [18][19][20][21][22][23][24][25][26][27][28], their number in invertebrates is very limited compared to that in snake venoms. As ArachnoServer and ConoServer deal with invertebrate proteins, data on enzymes are either limited, or nonexistent.…”

Section: Enzymesmentioning

confidence: 99%

Animal Toxins: How is Complexity Represented in Databases?

Jungo¹,

Estreicher

Bairoch

et al. 2010

Toxins

View full text Add to dashboard Cite

Peptide toxins synthesized by venomous animals have been extensively studied in the last decades. To be useful to the scientific community, this knowledge has been stored, annotated and made easy to retrieve by several databases. The aim of this article is to present what type of information users can access from each database. ArachnoServer and ConoServer focus on spider toxins and cone snail toxins, respectively. UniProtKB, a generalist protein knowledgebase, has an animal toxin-dedicated annotation program that includes toxins from all venomous animals. Finally, the ATDB metadatabase compiles data and annotations from other databases and provides toxin ontology.

show abstract

“…The term "seizure" refers to a crisis with predominant motor manifestations (45 after ischemia induced in vitro (53)(54)(55)(56)(57)(58)(59)(60). There is evidence that PnTx3-3 and PnTx3-4 also offer neuroprotection in vivo, which suggests that these molecules may be used for studies on neurodegenerative diseases, such as epilepsy (61).…”

Section: Peptides With Antiepileptic Effectsmentioning

confidence: 99%

“…Animal venoms or purified toxins evoke complex effects on ion channels, mainly sodium, potassium and calcium channels (56,66,(122)(123)(124)(125)(126)(127) Spider venoms are composed of distinct proteins, peptides and biologically active molecules, most of them neurotoxins (56). These venoms have been described as potentially useful for future discovery and development of new biologically active molecules with medical application (66,115,116,122).…”

Section: Peptides That Potentiate Erectile Functionmentioning

confidence: 99%

Some arachnidan peptides with potential medical application

Lima¹,

Borges²,

Verano‐Braga³

et al. 2010

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

View full text Add to dashboard Cite

ABSTRACT:The search for new active drugs that can alleviate or cure different diseases is a constant challenge to researchers in the biological area and to the pharmaceutical industry. Historically, research has focused on the study of substances from plants. More recently, however, animal venoms have been attracting attention and studies have been successful in addressing treatment of accidents. Furthermore, venoms and their toxins have been considered good tools for prospecting for new active drugs or models for new therapeutic drugs. In this review, we discuss some possibilities of using different toxins, especially those from arachnid venoms, which have shown some potential application in diseases involving pain, hypertension, epilepsy and erectile dysfunction. A new generation of drugs is likely to emerge from peptides, including those found in animal venoms.

show abstract

Comparison of the partial proteomes of the venoms of Brazilian spiders of the genus Phoneutria

Cited by 97 publications

References 95 publications

Spider toxins comprising disulfide‐rich and linear amphipathic domains: a new class of molecules identified in the lynx spider Oxyopes takobius

Spider toxins comprising disulfide‐rich and linear amphipathic domains: a new class of molecules identified in the lynx spider Oxyopes takobius

Animal Toxins: How is Complexity Represented in Databases?

Some arachnidan peptides with potential medical application

Contact Info

Product

Resources

About