Multivalent human blood group ABH and Lewis glycotopes are key recognition factors for a lFuc>Man binding lectin from phytopathogenic Ralstonia solanacearum

Analyses of diverse mammals’ milk and lactoferrin glycans using five pathogenic bacterial lectins

“…Oligosaccharide clusters and branches bearing Lewis antigens are PA-IIL best ligands (Imberty, Chabre, & Roy, 2008;Mitchell et al, 2002). RSL also strongly binds to Fuca1-3 and core Fuca1-6 residues (Kostlanova et al, 2005;Sudakevitz et al, 2002;Wu et al, 2009). The reason for no binding of PA-IL to the lactoferrins despite their terminal galactosyl residues might be interference by adjacent masking residues such as the fucosylated ones of the human lactoferrin (that react with the bacterial fucophilic lectins) or the polymannosylated branches of the cow lactoferrin (Fig.…”

“…The present study has examined the 12 different milk glycan interactions with an additional 2 lectins of the plant aggressive pathogen R. solanacearum: the fucophilic RSL [displaying core Fuca1-6 preference, in addition to Fuca1-2/3/4-binding (Kostlanova et al, 2005;Sudakevitz et al, 2002;Wu et al, 2009)] and the mannophilic RS-IIL (Sudakevitz et al, 2004). Its aims were the following: (i) comparison of the milk glycan interactions with lectins from animal-vs. phyto-pathogens and two reference plant lectins; and (ii) application of the same 7-lectin series for the study of isolated (commercial) human and bovine lactoferrins, which were not hitherto probed by bacterial lectins.…”

“…The five pathogenic bacterial lectins used in this study vary in their carbohydrate specificities: PA-IL (LecA) is galactophilic and PA-IIL (LecB) is fucophilic (Gilboa-Garber, 1982); CV-IIL, which is also fucophilic, is a structural homologue of PA-IIL, exhibiting more selective H blood group specificity (Zinger-Yosovich et al, 2006); RSL, which is also fucophilic, exhibits Fuca1-2/3/4/6(core)-binding affinities (Kostlanova et al, 2005;Sudakevitz et al, 2002;Wu et al, 2009), and RS-IIL, which is another structural homologue of PA-IIL and CV-IIL, is mannophilic (Sudakevitz et al, 2004). These lectins are considered as virulence factors (VIFs) contributing to the bacterial adhesion to the target cells, to biofilm formation and to augmentation of the notorious effects of other VIFs (toxins and hydrolytic enzymes) which are co-produced with them (GilboaGarber et al, 1997).…”

Relative intensities of recognition factors at two combining sites of Ralstonia solanacearum lectin (RSL) for accommodating lFucα1→, dManα1→ and Galβ1→3/4GlcNAc glycotopes

“…RSL was purified from the bacterial extracts ( R. solanacearum ATCC 11696) as previously described [7–9]. RSL used for studying was biotinylated by the method established by Duk et al [13].…”

“…This lectin showed stronger affinity for papain‐treated human erythrocytes regardless of their O, A, B and AB types and it also interacted with human saliva of H and Le a,b phenotypes [7]. Its sugar‐binding preference was studied by thermodynamical and crystallographic approaches with various monomeric ligands [7–8], and also by both enzyme‐linked lectinosorbent (ELLSA) and inhibition assays [9]. It has been characterized as l Fuc > d Man.…”