7 results on '"Tityus cambridgei"'
Search Results
2. Amino acid sequence and function of a new α-toxin from the Amazonian scorpion Tityus cambridgei
- Author
-
Murgia, Anna Rosa, Batista, Cesar V.F., Prestipino, Gianfranco, and Possani, Lourival D.
- Subjects
- *
SCORPION venom , *TOXINS , *AMINO acids , *PATCH-clamp techniques (Electrophysiology) - Abstract
A toxic peptide earlier denominated Tc48b [Toxicon 40 (2002) 557] was purified to homogeneity and its amino acid sequence determined. It has 64 amino acid residues stabilized by four disulfide bridges with a molecular weight of 7,385.2 atomic mass units (a.m.u.). It affects Na+-permeability in pituitary GH3 cells in culture, in a similar fashion as those reported for α-scorpion toxins, contrary to most of the New World scorpion toxins that are β-toxins. [Copyright &y& Elsevier]
- Published
- 2004
- Full Text
- View/download PDF
3. Proteomics of the venom from the Amazonian scorpion Tityus cambridgei and the role of prolines on mass spectrometry analysis of toxins
- Author
-
Batista, Cesar V.F., del Pozo, Luis, Zamudio, Fernando Z., Contreras, Sandra, Becerril, Baltazar, Wanke, Enzo, and Possani, Lourival D.
- Subjects
- *
SCORPIONS , *POISONOUS animals , *VENOM , *PEPTIDES , *BIOLOGICAL membranes , *AMINO acids , *TOXINS , *IMMUNOGLOBULINS - Abstract
Scorpion venom are complex mixtures of peptides, known to cause impairment of ion-channel function in biological membranes. This report describes the separation of approximately 60 different components by high performance liquid chromatography and the characterization by Edman degradation and mass spectrometry of 26 peptides from the soluble venom of the Amazonian scorpion Tityus cambridgei. One of these peptides, named Tc48a, was fully characterized. It contains 65 amino acid residues, the C-terminal residue is amidated and it affects Na+-channels with a Kd of about 82 nM. Furthermore, this report shows the thermo-instability of scorpion toxins subjected to electron spray ionization-mass spectrometry (ESI-MS). When a proline residue is located near the N-terminal region of the toxin, not stabilized by disulfide bridges, artificial components are generated by the mass spectrometer conditions, due to the cleavage of the peptide bond at the proline positions. This phenomenon was confirmed by using four model proteins (variable regions of immunoglobulins) studied by ESI-MS and matrix assisted laser desorption ionization–time of flight (MALDI–TOF)/MS. [Copyright &y& Elsevier]
- Published
- 2004
- Full Text
- View/download PDF
4. Scorpion toxins from Tityus cambridgei that affect Na+-channels
- Author
-
Batista, Cesar V.F., Zamudio, Fernando Z., Lucas, Sylvia, Fox, Jay W., Frau, Andrea, Prestipino, Gianfranco, and Possani, Lourival D.
- Subjects
- *
SCORPION venom , *AMINO acid sequence , *TOXINS , *HIGH performance liquid chromatography - Abstract
By means of high performance liquid chromatography (HPLC) the soluble venom of the Amazonian scorpion Tityus cambridgei was fractionated into over 50 different components. Four toxic and/or lethal peptides to mice were obtained in pure form and sequenced. Mass spectrometry analysis showed molecular weights of 7310, 7151, 7259 and 7405, respectively, for toxins Tc48a, Tc49a, Tc54 and Tc49b. The N-terminal amino acid sequence was obtained for the three first toxins mentioned, whereas the full primary structure was determined for Tc49b. It contains 64 amino acid residues, closely packed by four disulfide bridges. Sequence comparison analysis showed similarities around 50% with other toxins from scorpions of the genus Tityus of Brazil. It is lethal to mice at doses of 20 μg per 20 g mouse. The toxin was shown to affect the Na+-currents permeability of rat cerebellum granular cells in culture. Almost a complete elimination of current was observed with 100 nM toxin concentration. This effect was partially reversible. Furthermore, this toxin does not modify the function of the Shaker B K+-channels expressed on Sf9 cells, nor does it modify the Na+-channel function in a similar manner as those reported for the alpha-scorpion toxins purified from other scorpions. [Copyright &y& Elsevier]
- Published
- 2002
- Full Text
- View/download PDF
5. Tc1, from Tityus cambridgei , is the first member of a new subfamily of scorpion toxin that blocks K+ -channels
- Author
-
Lourival D. Possani, Froylan Gómez-Lagunas, Sylvia M. Lucas, and Cesar Vicente Ferreira Batista
- Subjects
Potassium Channels ,Subfamily ,Molecular Sequence Data ,Neurotoxins ,Biophysics ,Scorpion ,Scorpion Venoms ,Peptide ,Venom ,Spodoptera ,Tityus cambridgei ,complex mixtures ,Biochemistry ,Cell Line ,Scorpions ,Mice ,Structural Biology ,biology.animal ,Potassium Channel Blockers ,Genetics ,Animals ,Amino Acid Sequence ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,K+-channel ,Scorpion toxin ,biology ,Chemistry ,Cell Biology ,Amino acid ,Shaker Superfamily of Potassium Channels ,Peptides ,Synaptosomes - Abstract
A new peptide, Tc1, containing only 23 amino acids closely packed by three disulfide bridges was isolated from the Amazonian scorpion Tityus cambridgei. It blocks reversibly the Shaker B K+-channels with a Kd of 65 nM and displaces binding of noxiustoxin to mouse brain synaptosome membranes. It is the shortest known peptide from scorpion venom that recognizes K+-channels and constitutes a new structural subfamily of toxin, classified as alphaKTx 13.1.
- Published
- 2000
- Full Text
- View/download PDF
6. Aspectos epidemiológicos e clínicos do escorpionismo na região de Santarém, Estado do Pará, Brasil
- Author
-
Erik Jennings, Joseana Silva de Oliveira Pardal, Maria Rita de Cassia Costa Monteiro, Pedro Pereira de Oliveira Pardal, and Lívia Correa Castro
- Subjects
Microbiology (medical) ,medicine.medical_specialty ,lcsh:Arctic medicine. Tropical medicine ,Animais venenosos ,lcsh:RC955-962 ,Pará - Estado ,Escorpionismo ,Tityus cambridgei ,Escorpião ,medicine ,Envenomation ,Gynecology ,business.industry ,Scorpionism ,Santarém ,Surgery ,Envenenamento ,Comportamento clínico ,Infectious Diseases ,Neurological ,Aspecto clínico ,Parasitology ,business ,Neurológico ,Santarém - PA ,Aspecto epidemiológico - Abstract
Este trabalho é um estudo prospectivo e descritivo dos aspectos epidemiológicos e clínicos de 72 envenenamentos por escorpiões admitidos no Hospital Municipal de Santarém, Estado do Pará, Brasil, entre fevereiro de 2000 a fevereiro de 2001. Trouxeram o animal 8,3% das vítimas, os quais foram identificados como T. cambridgei. O sexo masculino foi acometido em 83,3%. A idade das vítimas e o tempo para o socorro médico foram respectivamente de 33,6±18,3 anos e 4,6±3,2 horas em média. Os membros superiores foram acometidos em 51,5% dos casos. As manifestações locais estiveram presentes em 91,7% e as sistêmicas em 98,6% dos envenenamentos. Entre os sintomas locais encontramos: parestesia em 79,2%, dor em 52,8%, e edema em 26,4% dos casos. Nas manifestações sistêmicas predominou as queixas neurológicas em 97,2% das vítimas, sendo o sintoma de sensação de "choque elétrico" pelo corpo (88,9%) o mais freqüente. No exame neurológico os sinais mais encontrados foram: mioclonias (93,0%), dismetria (86,1%), disartria (80,6%) e ataxia de marcha (70,8%). Classificou-se como moderados 76,4% dos envenenamentos, sem nenhum caso grave. Deixaram de realizar a soroterapia 32,7% dos casos moderados, por ausência de soro específico no momento do atendimento. O escorpionismo da região de Santarém mostra um comportamento clínico regional diferente daqueles descritos no Brasil e de outros locais da Amazônia e, apresenta uma clínica predominantemente neurológica, ainda não descrita na literatura brasileira. This is a descriptive and prospective study on epidemiological and clinical aspects of 72 scorpion accidents admitted to Santarém Municipal Hospital, state of Pará, Brazil, from February 2000 to February 2001. Only 8.3% brought the animal with them, identified as T. cambridgei. The majority of victims were male (83.3%). The mean age and the time of the medical help were respectively 33.6±18.3 years and 4.6±3.2 hours. The parts of the body most affected were the superior members (51.5%). Local symptoms occurred in 91.7% cases and systemic manifestations in 98.6% of the accidents. The local symptoms included: paresthesia in 79.2% cases, pain in 52.8% and edema in 26.4%. Among the systemic manifestations neurological disorders predominated in 97.2%, and the symptom of "electric shock" occurred in 88.9% patients. The most common neurological signs were: myoclonia (93%), dysmetria (86.1%), dysarthria (80.6%), and ataxia (70.8%). The accidents were classified as moderate in 76.4% without any serious cases. The specific anti-venom serum was not administered in 32.7% of the moderate cases, due to non-availability of the anti-venom serum at the time of attendance. The victims of scorpion envenomation notified at Santarém, present a different clinical and regional behavior from previous reports in Brazil and Amazonia regions. The predominantly neurological picture has not previously been described in the Brazilian literature.
- Published
- 2003
7. Molecular dynamics simulations of a K+ channel blocker: Tc1 toxin from Tityus cambridgei
- Author
-
Alessandro Grottesi and Mark S.P. Sansom
- Subjects
Models, Molecular ,Protein Folding ,Charybdotoxin ,Protein Conformation ,Neurotoxins ,Biophysics ,Scorpion Venoms ,Biology ,010402 general chemistry ,medicine.disease_cause ,01 natural sciences ,Biochemistry ,Homology (biology) ,Scorpions ,03 medical and health sciences ,Molecular dynamics ,Structural Biology ,Genetics ,medicine ,Potassium Channel Blockers ,Animals ,Channel blocker ,Computer Simulation ,Molecular Biology ,030304 developmental biology ,K channels ,0303 health sciences ,Protein fold class ,Voltage-gated ion channel ,Toxin ,Cell Biology ,0104 chemical sciences ,Protein Structure, Tertiary ,Crystallography ,Molecular simulation ,Tityus cambridgei ,Essential dynamics ,Conotoxins ,Voltage-gated channel - Abstract
Toxins that block voltage-gated potassium (Kv) channels provide a possible template for improved homology models of the Kv pore. In assessing the interactions of Kv channels and their toxins it is important to determine the dynamic flexibility of the toxins. Multiple 10 ns duration molecular dynamics simulations combined with essential dynamics analysis have been used to explore the flexibility of four different Kv channel-blocking toxins. Three toxins (Tc1, AgTx and ChTx) share a common fold. They also share a common pattern of conformational dynamics, as revealed by essential dynamics analysis of the simulation results. This suggests that some aspects of dynamic behaviour are conserved across a single protein fold class. In each of these three toxins, the residue exhibiting minimum flexibility corresponds to a conserved lysine residue that is suggested to interact with the filter domain of the channel. Thus, comparative simulations reveal functionally important conservation of molecular dynamics as well as protein fold across a family of related toxins.
- Published
- 2003
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.