Structural and biological characterization of a crotapotin isoform isolated from Crotalus durissus cascavella venom

Oliveira, Daniela Garcia de; Toyama, Marcos H.; Martins, Alice Maria Costa; Havt, Alexandre; Nobre, Arlandia Cristina Lima; Marangoni, Sérgio; Câmara, Paula Rs; Antunes, Edson; Nucci, Gilberto De; Beliam, Luis O.S; Fonteles, M. C.; Monteiro, Helena Serra Azul

doi:10.1016/s0041-0101(03)00100-4

Cited by 26 publications

(17 citation statements)

References 24 publications

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“…Determination of the N-terminal sequence of sPLA 2 was performed following the protocol described by de Oliveira et al (2003). Briefly, 10 mg of purified protein was dissolved in 200 mL of 6 M guanidine chloride (Merck, Darmstadt, Germany) containing 0.4 mM Tris-HCl and 2 mM EDTA (final pH 8.15).…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

Renal and cardiovascular effects of Bothrops marajoensis venom and phospholipase A2

Evangelista

Martins

Nascimento

et al. 2010

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Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

Renal and cardiovascular effects of Bothrops marajoensis venom and phospholipase A2

Evangelista

Martins

Nascimento

et al. 2010

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“…The N-terminal sequence of LAAO was determined following published protocols (15). Briefly, 10 mg of purified protein was dissolved in 200 µL of 6 M guanidine (final pH 8.15).…”

Section: N-terminal Amino Acid Sequencementioning

confidence: 99%

Antimicrobial activity of an L-amino acid oxidase isolated from Bothrops leucurus snake venom

Torres¹,

Dantas²,

Menezes³

et al. 2010

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

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Some snake venom proteins present enzymatic activities, such as L-amino acid oxidase (LAAO). The aim of this paper was to investigate the effect of Bothrops leucurus total venom (BleuTV) and its fraction LAAO (BleuLAAO) on bacteria, yeast, and promastigote forms of Leishmania amazonensis and Leishmania chagasi, and epimastigote forms of Trypanosoma cruzi. BleuTV was isolated with a Protein Pack 5PW® (Waters Corporation, USA), and several fractions were obtained. BleuLAAO was purified to high molecular homogeneity, and its N-terminal amino acid sequence shared a high degree of amino acid conservation with other LAAOs. BleuTV inhibited Staphylococcus aureus growth in a dose-dependent manner, with a minimum inhibitory concentration (MIC) of 25 μg/mL, which corresponded to its minimum lethal concentration (MLC). BleuTV also inhibited the growth of promastigote forms of L. chagasi and L. amazonensis, with respective IC50 values of 1.94 μg/mL and 5.49 μg/mL. Furthermore, it repressed T. cruzi growth with an IC50 of 1.14 μg/mL. However, BleuLAAO did not inhibit the growth of the microorganisms studied and was not toxic to macrophages. BleuTV had low toxicity against macrophages at the concentrations studied. In conclusion, whole venom from Bothrops leucurus inhibited the growth of some microorganisms, including S. aureus, Leishmania sp., and T. cruzi

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“…Some other CB variants (e.g. CB3; Table 2) were, however, identified in special geographic samples of C. d. terrificus [39,40]. The basic subunit of canebraxin (from neurotoxic population of C. horridus) has its N-terminal sequence identical with that of CB1 but has a distinct mass of 14.154 kDa.…”

Section: Phylogeography and Evolution Of Venom N6-pla 2 Smentioning

confidence: 99%

“…Although the toxicities of sistruxin and canebraxin are as potent as crotoxin (Table 5), their contents in the venom are relatively low (5-12 %). Thus envenomings by Pigmy rattlers or Timber rattlers usually do not show neurotoxic symptoms like those by Mojave or neotropical rattlers, which contain crotoxin up to 50 % of the total venom content [35,39].…”

Section: Phylogeography and Evolution Of Venom N6-pla 2 Smentioning

confidence: 99%

Molecular evolution and structure–function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms

Chen

Wang

Hseu

et al. 2004

Biochemical Journal

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Some myotoxic or neurotoxic PLA 2 s (phospholipases A 2 ) from pit viper venoms contain characteristic N6 substitutions. Our survey of the venoms of more than ten pit viper genera revealed that N6-PLA 2 s exist only in limited Asian pit vipers of two genera, Protobothrops and Gloydius, and exist as either monomers or the basic subunits of heterodimers in some New World pit vipers. For the newly identified N6-PLA 2 s, the neuromuscular blocking activities were assayed with the chick biventer cervicis neuromuscular tissue, whereas the increased serum creatine kinase level assessed their myotoxicities. The purified N6-PLA 2 s from Protobothrops mangshanensis and Gloydius intermedius saxatilis were found to be presynaptic neurotoxins. In contrast, all N6-PLA 2 s from the venoms of Sistrurus miliarius strackeri, S. m. barbouri, Crotalus viridis viridis, C. lepidus lepidus, Cerrophidion godmani and Bothreichis schlegelii were myotoxins without neurotoxicity even in the presence of crotoxin A. Crotoxin-like complexes were for the first time purified from the venoms of Sitrurus catenatus tergeminus, C. mitchelli mitchelli, C. horridus atricaudatus, C. basiliscus and C. durissus cumanensis. The cDNAs encoding six novel N6-PLA 2 s and subunits of the crotoxin-like complex from S. c. tergeminus were cloned and fully sequenced. Phylogeny analysis showed that two structural subtypes of N6-PLA 2 s with either F24 or S24 substitution have been evolved in parallel, possibly descended respectively from species related to present-day Protobothrops and Gloydius. Calmodulin binds all the N6-PLA 2 s but crotoxin A may inhibit its binding to crotoxin B and to other neurotoxic N6-PLA 2 s. Structure-activity relationships at various regions of the PLA 2 molecules were extensively discussed.

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Structural and biological characterization of a crotapotin isoform isolated from Crotalus durissus cascavella venom

Cited by 26 publications

References 24 publications

Renal and cardiovascular effects of Bothrops marajoensis venom and phospholipase A2

Renal and cardiovascular effects of Bothrops marajoensis venom and phospholipase A2

Antimicrobial activity of an L-amino acid oxidase isolated from Bothrops leucurus snake venom

Molecular evolution and structure–function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms

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