Biochemical and functional characterization of a C-type lectin (BpLec) from Bothrops pauloensis snake venom

Snake venom galactoside-binding lectins: a structural and functional overview

“…All SVgalLs are homodimeric proteins composed of disulfide-linked monomers presenting molecular mass varying from 14 to 16.2 kDa. The primary structures of 12 SVgalLs were determined, and presented from 134 to 136 amino acid residues as described for the following lectins: RSL—rattlesnake lectin from Crotalus atrox [ 23 ], ApL— Agkistrodon piscivorus piscivorus lectin [ 15 ], BaL— Bitis arietans lectin [ 13 ], CrL— Crotalus ruber lectin [ 18 ], BiL— Bothrops insularis lectin [ 16 ], BmLec— Bothrops moojeni lectin [ 24 ], BpalL— Bothrops pauloensis lectin [ 21 ], BJcuL— Bothrops jararacussu lectin [ 25 ], BpirL— Bothrops pirajai lectin [ 17 ], LmL— Lachesis muta stenophrys lectin [ 26 ], ToL— Trimeresurus okinavensis lectin [ 27 ] and TsL— Trimeresurus stejnegeri lectin [ 28 ]. Amino acid sequence analysis among the referenced SVgalLs using BLAST searching tool [ 29 ] showed an identity degree from 82 to 97 % among them, indicating a high primary structural similarity within these lectins.…”

“…So far, with the exception of the mannose-binding lectin isolated from Oxyuranus scutellatus crude venom [ 37 ], most snake venom glycan-binding lectins present the ability to interact specifically with sugars via terminal galactoside residues [ 6 ]. Interestingly, this similarity of galactose recognition patterns is reflected in several aspects among SVgalLs, such as the purification procedure which, for most snake lectins, is performed by single step liquid chromatography using affinity resins with a matrix composed of lactose- or galactose-based components [ 8 – 21 , 38 – 41 ].…”

“…Considering that during the infection process pathogen adhesion to the host cell involves protein-glycan interactions [ 63 , 64 ], glycoconjugates from the pathogen cell surface represents a potential target for SVgalLs. Castanheira et al [ 21 ] showed that BpalL, a lectin isolated from Bothrops pauloensis venom, induced agglutination but not toxicity of promastigote forms of Leishmania amazonesis through interaction with galactoside glycoconjugates on the parasite membrane. The effects of BpalL on bacteria were also evaluated, where the lectin inhibited gram-positive Staphylococcus aureus growth, but not gram-negative E.coli [ 21 ].…”

“…Since then, several reports on purification and both the structural and functional characterization of snake venom lectins have been described from the snake families Viperidae and Elapidae, including from the genera Bothrops , Crotalus , Bitis , Agkistrodon , Lachesis , Dendroaspis and Trimeresurus . Most snake venom glycan-binding lectins are members of the C-type galactoside-binding proteins due to their ability to interact with terminal galactoside residues in a calcium-dependent manner [ 8 – 21 ]. The lectin isolated from Lachesis muta stenophrys (LmL) was first classified as lectin-like by the authors [ 10 ].…”

Porifera Lectins: Diversity, Physiological Roles and Biotechnological Potential

“…These results suggest that L. chagasi promastigotes have specific glycosylated receptors for these lectins on the cell membrane of the parasite. Specificities of parasite receptors have extensively been studied, especially for trypanosomatids [ 152 , 153 , 154 , 155 ]. These lectins may represent valuable tools for the detection and fight against the protozoan parasites.…”