Lebectin and lebecetin, two C-type lectins from snake venom, inhibit alpha5beta1 and alphaV-containing integrins

Abstract : Integrins are essential protagonists in the complex multistep process of cancer progression and metastasis. We recently reported that lebectin, a novel C-type lectin from Macrovipera lebetina venom, displays an anti-integrin activity. In this study, we extend this observation to lebecetin, a second C-type lectin isolated from the same venom and previously reported as a potent inhibitor of platelet aggregation. Both venom lectins appear to exert their effect on cell adhesion, migration, invasion and proliferation by inhibiting α5β1 and αv-containing integrins. Moreover, the inhibition of α5β1 and αv integrins is likely due to the binding of venom peptides, as both lebectin and lebecetin co-immunoprecipitate with these integrins. Lebectin and lebecetin are thus the first examples of venom C-type lectins inhibiting an integrin other than the collagen receptor α2β1.
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Submitted on : Tuesday, February 19, 2019 - 10:41:41 AM
Last modification on : Wednesday, August 21, 2019 - 1:19:06 AM

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Sameh Sarray, Estelle Delamarre, Jacques Marvaldi, Mohamed El Ayeb, Naziha Marrakchi, et al.. Lebectin and lebecetin, two C-type lectins from snake venom, inhibit alpha5beta1 and alphaV-containing integrins. Matrix Biology, Elsevier, 2007, 26 (4), pp.306-313. ⟨10.1016/j.matbio.2007.01.001⟩. ⟨pasteur-02024416⟩

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