The anti-inflamatory effect of Andira anthelmia lectin in rats involves inhibition of the prostanoid pathway, TNF-α and lectin domain.

OBJECTIVE: To investigate the effect and mechanisms of Andira anthelmia lectin in rat models of acute inflammation. MATERIAL: AAL anti-inflammatory activity was evaluated in Wistar rat models of paw edema and peritonitis. METHODS: AAL (0.01-1 mg/kg i.v.) was injected 30 min before stimulation with carrageenan and with initial and late phase inflammatory mediators into the animals paw or peritoneum for evaluation of cell migration (optical and intravital microscopy), paw edema (plethysmometry and histopathology); hyperalgesia (analgesimetry). RESULTS: AAL inhibited leukocyte migration induced by carrageenan, mainly neutrophils to the peritoneal fluid, decreasing leukocyte adhesion. In the peritoneal fluid, AAL reduced the gene expression of TNF-α and cyclooxygenase, as well the levels of PGE2. AAL inhibited the paw edema induced by carrageenan, serotonin, histamine, TNF-α, PLA2 and PGE2, but not by L-arginine. In this model, AAL also inhibited mechanical hypernociception induced by TNF-α, PGE2, db-cAMP and capsaicin, and the activity of myeloperoxidase in the paw tissues. CONCLUSION: AAL presents anti-inflammatory effect in acute models of rat inflammation involving the participation of prostaglandins, TNF-α and lectin domain.

Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.

CaBo is a mannose/glucose-specific lectin purified from seeds of Canavalia bonariensis. In the present work, we report the CaBo crystal structure determined to atomic resolution in the presence of X-man, a specific ligand. Similar to the structural characteristics of other legume lectins, CaBo presented the jellyroll motif, a metal binding site occupied by calcium and manganese ions close to the carbohydrate-recognition domain (CRD). In vitro test of CaBo cytotoxicity against glioma cells demonstrated its ability to decrease the cellular viability and migration by induction of autophagy and cell death. Molecular docking simulations corroborate previous data indicating that the lectin's biological activities occur mostly through interactions with glycoproteins since the lectin interacted favorably with several N-glycans, especially those of the high-mannose type. Together, these results suggest that CaBo interacts with glycosylated cell targets and elicits a remarkable antiglioma activity.

Purification of a thermostable antinociceptive lectin isolated from Andira anthelmia.

Andira anthelmia (tribe Dalbergieae), a plant from Brazilian Amazon, possesses a seed lectin that was purified by affinity chromatography in sepharose-mannose. This novel Dalbergieae lectin, named AAL, agglutinated rabbit erythrocytes treated with trypsin. The hemagglutinating activity of AAL was maintained after incubation at a wide range of temperature (40 to 70 °C) and pH, was shown to be dependent on divalent cations, and was inhibited by d-mannose and d-sucrose. AAL showed an electrophoretic profile in sodium dodecyl sulfate-polyacrylamide gel electrophoresis similar to other lectins of the tribe Dalbergieae, presenting a double band of molecular weight with approximately 20 kDa and other minor bands of 17, 15, and 13 kDa, being the smaller fragment glycosylated. AAL injected by intravenous route in mice showed antinociceptive activity in two behavioral tests (writhing and formalin). In the writhing test induced by acetic acid, AAL showed inhibitory effect at 0.01 mg/kg (68%), 0.1 mg/kg (46%) and 1 mg/kg (74%). In the formalin test, AAL (0.1 mg/kg) inhibited by 48% the licking time in the inflammatory phase, an effect that was recovered by the lectin association with mannose. In conclusion, AAL presents analgesic effect involving the lectin domain via peripheral mechanisms of inflammatory nociception. This activity highlights the importance of lectins as tools to be used for understanding the interaction of protein-carbohydrate in processes associated to inflammatory pain. Copyright © 2015 John Wiley & Sons, Ltd.