Purification and biological effects of C-type lectin isolated from Bothrops insularis venom

Braga, Marcus Davis Machado; Martins, Alice Maria Costa; Amora, Daniela Nascimento; Menezes, Dalgimar Beserra de; Toyama, Marcos Hikari; Toyama, Daniela O.; Marangoni, Sérgio; Barbosa, Paula; Alves, Renata; Fonteles, M. C.; Monteiro, Helena Serra Azul

doi:10.1016/j.toxicon.2006.02.016

Cited by 20 publications

(15 citation statements)

References 34 publications

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“…The degree of purity of the lectin-like substance was assayed using two dimensional (2D) and mass spectrometry. SDS-PAGE using 12% acrylamide tricine gels confirmed the homogeneity of the fraction (22) …”

Section: Venommentioning

confidence: 66%

“…Analysis of the amino acid sequence of the RC-protein, and that of the enzymatically or chemically digested fragments, was performed with an Applied Biosystems model Procise f gas-liquid protein sequencer® (USA). The phenylthiohydantoin (PTH) derivatives of the amino acids were identified with an Applied Biosystems model 450 microgradient PTH-analyser® (USA) (22,23). The resulting primary structure of BmLec was aligned with homologous sequences obtained from the NCBI database (http://www.ncbi.nlm.nih.gov) using the algorithm BLAST.…”

Section: Characterization Of Lectin Isolated From B Moojeni Venommentioning

confidence: 99%

See 1 more Smart Citation

Purification and biological effects of a C-type lectin isolated from Bothrops moojeni

Barbosa¹,

Martins²,

Toyama³

et al. 2010

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

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Snake venom proteins from the C-type lectin family have very distinct biological activities despite their highly conserved primary structure, which is homologous to the carbohydrate recognition region of true C-type lectins. We purified a lectin-like protein (BmLec) from Bothrops moojeni venom and investigated its effect on platelet aggregation, insulin secretion, antibacterial activity, and isolated kidney cells. The BmLec was purified using two chromatographic steps: affinity chromatography and reverse phase high performance liquid chromatography (HPLC). BmLec showed a dose-dependent platelet aggregation and significantly decreased the bacterial growth rate in approximately 15%. During scanning electron microscopy, the profile of Xanthomonas axonopodis pv. passiflorae treated with lectin disclosed a high vesiculation and membrane rupture. BmLec induced a strong and significant increase in insulin secretion at 2.8 and 16.7 mM glucose concentrations, and this effect was seen in the presence of EGTA in both experiments. BmLec (10 µg/mL) increased the perfusion pressure, renal vascular resistance and urinary flow. The glomerular filtration rate and percentages of sodium, potassium and chloride tubular transport were reduced at 60 minutes of perfusion. Renal alterations caused by BmLec were completely inhibited by indomethacin in all evaluated parameters. In conclusion, the C-type lectin isolated from Bothrops moojeni affected platelet aggregation, insulin secretion, antibacterial activity and isolated kidney function

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Section: Venommentioning

confidence: 66%

Section: Characterization Of Lectin Isolated From B Moojeni Venommentioning

confidence: 99%

Purification and biological effects of a C-type lectin isolated from Bothrops moojeni

Barbosa¹,

Martins²,

Toyama³

et al. 2010

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

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show abstract

“…Recently, isolation of lectins from various sources has been described using numerous sugars, such as lactose (Almanza et al, 2004;Braga et al, 2006;Fujii et al, 2011;Hamako et al, 2007;Kawsar et al, 2009;Mendonça-Franqueiro et al, 2011;Naeem et al, 2007b;Pohleven et al, 2009;Rocha et al, 2009;Silva et al, 2007), sucrose and glucose (Pohleven et al, 2011), galactose (Konami et al, 1991;Lavanya Latha et al, 2006;Mo et al, 2000;Moreira et al, 1998;Naeem et al, 2007b;Nagata, 2005), mannose (Andon et al, 2003;Ooi et al, 2010;Suseelan et al, 2002), fucose (Cammarata et al, 2007;Mansour & Abdul-Salam, 2009), L-rhamnose (Jimbo et al, 2007;Watanabe et al, 2008), and sugars with 2'-acetamido groups N-acetylgalactosamine (Gerlach et al, 2005;Perçin et al, 2009;Qureshi et al, 2006), N-acetylglucosamine (Kaur et al, 2005;Kim et al, 2006;Maheswari et al, 2002;Wang & Ng, 2003), and N,N'-diacetylchitobiose (Konami et al, 1991;Koyama et al, 2002).…”

Section: Mono-and Disaccharidesmentioning

confidence: 99%

Affinity Chromatography of Lectins

Pohleven¹,

Štrukelj²,

Kos³

2012

Affinity Chromatography

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“…Some purified Bothrops toxins are able to reproduce the renal effects obtained with whole venom. Studies on the isolated perfused rat kidney have shown that L-amino acid oxidase (Braga et al, 2008), C-type lectins (Braga et al, 2006), phospholipase A2 myotoxins (Barbosa et al, 2005;Evangelista et al, 2010) and thrombin-like enzyme (Braga et al, 2007) from Bothrops venoms can alter renal function. The isolated perfused kidney technique also confirmed the direct acute tubular nephrotoxicity of Bothrops venoms and showed that platelet activating factor might play a role in some renal functional disturbances such as the decreased in glomerular filtration rate (Monteiro and Fonteles, 1999).…”

Section: Bothrops Venommentioning

confidence: 99%