Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent

Araújo, Regina Maria Sousa de; Ferreira, Rodrigo S.; Napoleão, Thiago Henrique; Carneiro-da-Cunha, Maria das Graças; Coelho, Luana Cassandra Breitenbach Barroso; Correia, Maria Tereza dos Santos; Oliva, Maria Luiza Vilela

doi:10.1016/j.plantsci.2011.10.018

Cited by 37 publications

(43 citation statements)

References 43 publications

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“…C. tapia is known by Northeast Brazilian people as “paudalho” or “tapiá” and its bark is largely used in the folk medicine for the treatment of diabetes. Recently, a lectin with a molecular weight of 40 kDa (CrataBL) was purified from the aqueous extract of Crataeva tapia bark [2]. Lectins are carbohydrate binding proteins, of nonimmunogenic origin, that bind specifically and reversibly to different types of carbohydrates or glycoproteins and can be obtained from several sources, mainly from vegetal [3].…”

Section: Introductionmentioning

confidence: 99%

Lectin fromCrataeva tapiaBark Improves Tissue Damages and Plasma Hyperglycemia in Alloxan-Induced Diabetic Mice

Rocha

Araújo²,

Fonseca³

et al. 2013

Evidence-Based Complementary and Alternative Medicine

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Crataeva tapia is a plant popularly used for diabetes treatment, in Brazil. Progressive decline in renal and hepatic functions has been described in patients with diabetes mellitus, and mortality rate is increased in patients with chronic liver and renal disease. This study aimed to evaluate whether Crataeva tapia bark lectin (CrataBL) improves hyperglycemia and renal and hepatic damage in diabetic mice. CrataBL was purified by ion exchange chromatography on CM-cellulose, and intraperitoneal administration of CrataBL to alloxan-induced diabetic mice at dose of 10 mg/Kg/day and 20 mg/Kg/day for 10 days significantly reduced serum glucose levels by 14.9% and 55.9%, respectively. Serum urea, creatinine, aspartate aminotransferase, and alanine aminotransferase were also significantly reduced after treatment with both doses of CrataBL. Furthermore, histological analysis of liver, kidney, and pancreas revealed an improvement in the tissue morphology upon treatment with CrataBL. The results suggest that CrataBL has a beneficial hypoglycemic activity and improves the renal and hepatic complications of diabetes. Therefore, this lectin may be a promising agent for the treatment of diabetes, and this might be the basis for its use in the folk medicine as an alternative treatment to manage diabetes-related complications such as hyperglycemia and tissue damage.

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Section: Introductionmentioning

confidence: 99%

Lectin fromCrataeva tapiaBark Improves Tissue Damages and Plasma Hyperglycemia in Alloxan-Induced Diabetic Mice

Rocha

Araújo²,

Fonseca³

et al. 2013

Evidence-Based Complementary and Alternative Medicine

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“…12 A number of biological properties associated with CrataBL have been characterized, including anti-inflammatory, analgesic, anti-tumor, 13 and insecticidal activities. 12 A recent study showed that CrataBL delayed clot formation by impairing the intrinsic pathway of coagulation cascade, suggesting this protein might interact with heparin. 14 Heparin and heparin-derived low molecular weight heparins (LMWHs) are the most widely used clinical anticoagulants.…”

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confidence: 99%

Structural Studies of the Interaction of Crataeva tapia Bark Protein with Heparin and Other Glycosaminoglycans

et al. 2013

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CrataBL, a protein isolated from Crataeva tapia bark, which is both a serine protease inhibitor and a lectin, has been previously shown to exhibit a number of interesting biological properties, including anti-inflammatory, analgesic, anti-tumor, and insecticidal activities. Using a glycan array we have now shown that only sulfated carbohydrates are effectively bound by CrataBL. Since this protein was recently shown to delay clot formation by impairing the intrinsic pathway of coagulation cascade, we considered that its natural ligand might be heparin. Heparin is a glycosaminoglycan (GAG) that interacts with a number of proteins including thrombin and antithrombin III, which have a critical, essential pharmacological role in regulating blood coagulation. We have thus employed surface plasmon resonance to better understand the binding interaction between the heparin polysaccharide and CrataBL. Kinetic analysis shows that CrataBL displays strong heparin-binding affinity (KD= 49 nM). Competition studies using different size heparin-derived oligosaccharides showed that the binding of CrataBL to heparin is chain length dependent. Full chain heparin with 40 saccharides, or large oligosaccharides, having 16 to 18 saccharide residues, show strong binding affinity for CrataBL. Heparin-derived disaccharides through tetradecasaccharides show considerably lower binding affinity. Other highly sulfated GAGs including chondroitin sulfate E and dermatan 4,6-disulfate showed comparable CrataBL binding affinity to heparin. Less highly sulfated GAGs, heparan sulfate, chondroitin sulfate A and C and dermatan sulfate displayed modest binding affinity as did chondroitin sulfate D. Studies using chemically modified heparin show that N-sulfo and 6-O-sulfo groups on heparin are essential for CrataBL- heparin interaction.

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“…Toxic activity of CrataBL on the caste of soldiers and workers of N. corniger insect (termite) was previously reported. 14 …”

Section: Resultsmentioning

confidence: 99%

“…9,11 Such interactions can subsequently trigger other responses, including antimicrobial, anti-tumor, mitogenic, and insecticidal activity. 12–14 It has been reported that some plant lectins are toxic to insects belonging to the orders of Coleoptera, Diptera, Lepidoptera, and Isoptera. 15-20 …”

Section: Introductionmentioning

confidence: 99%

“…22 CrataBL exhibits binding specificity to N-acetyl glucosamine, 23 glucose, and galactose. 14 It was already demonstrated that this protein has several important biological functions including changes in the intrinsic pathway of the coagulation cascade proteins leading to the delay time of formation of the blood clot, 24 as well as thrombus formation. 25 In addition, CrataBL was shown to exhibit analgesic and anti-inflammatory, 26–27 anti-tumoral, 22,26 and insecticidal (against Nasutitermes corniger 14 ) properties.…”

Section: Introductionmentioning

confidence: 99%

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Potential of the Lectin/Inhibitor Isolated from Crataeva tapia Bark (CrataBL) for Controlling Callosobruchus maculatus Larva Development

Nunes

Ferreira

Silva-Lucca

et al. 2015

J. Agric. Food Chem.

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Callosobruchus maculatus is an important predator of cowpeas. Due to infestation during storage, this insect affects the quality of seed and crop yield. This study aimed to investigate the effects of CrataBL, a multifunction protein isolated from Crataeva tapia bark, on C. maculatus larvae development. The protein, which is stable even in extreme pH conditions, showed toxic activity reducing the larval mass 45% and 70% at concentrations of 0.25% and 1.0% (w/w), respectively. Acting as inhibitor, CrataBL decreased by 39% the activity of cysteine proteinases from larval gut. Conversely, the activity of serine proteinases was increased about 8-fold. The toxic properties of CrataBL may also be attributed to its capacity of binding to glycoproteins or glycosaminoglycans. Such binding interferes with larval metabolism, since CrataBL-FITC was found in the fat body, Malpighian tubules, and in the feces of larvae. These results demonstrate the potential of this protein for controlling larvae development.

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Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent

Cited by 37 publications

References 43 publications

Lectin fromCrataeva tapiaBark Improves Tissue Damages and Plasma Hyperglycemia in Alloxan-Induced Diabetic Mice

Lectin fromCrataeva tapiaBark Improves Tissue Damages and Plasma Hyperglycemia in Alloxan-Induced Diabetic Mice

Structural Studies of the Interaction of Crataeva tapia Bark Protein with Heparin and Other Glycosaminoglycans

Potential of the Lectin/Inhibitor Isolated from Crataeva tapia Bark (CrataBL) for Controlling Callosobruchus maculatus Larva Development

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