Bacterial recognition of thermal glycation products derived from porcine serum albumin with lactose.

Abstract

Recently, glyco-therapy is proposed to prevent the interaction of bacterial lectins with host ligands (glycoconjugates). This interaction represents the first step in infection. Neoglycans referred to as PSA-Lac (PSA-Glu (β1-4) Gal) were obtained by conjugation of porcine serum albumin (PSA) with lactose at 80 °C, 100 °C and 120 ºC. Characterization studies of the products showed that PSA could contain 1, 38 or 41 added lactoses, depending on the reaction temperature. These neoglycans were approximately 10 times more glycated than PSA-Lac obtained in previous work. Lactose conjugation occurred only at lysines and PSA-Lac contained terminal galactoses as confirmed by Ricinus communis lectin recognition. Furthermore, Escherichia coli K88+, K88ab, K88ac and K88ad adhesins showed affinity toward all PSA-Lac neoglycans, and the most effective was the PSA-Lac obtained after 100 ºC treatment. In vitro, this neoglycan partially inhibited the adhesion of E. coli K88+ to piglet mucin (its natural ligand). These results provide support for the hypothesis that glycated proteins can be used as an alternative for bioactive compounds for disease prevention.

K88 Fimbrial Adhesin Targeting of Microspheres Containing Gentamicin Made with Albumin Glycated with Lactose

“…Albumin modified with lactose (BSA-Lac) was used as the polymer for the synthesis of lactosylated albumin microspheres [ 14 , 15 ]. Three formulations labeled as MS-Lac1, MS-Lac2 and MS-Lac3, obtained by water-in-oil emulsion at three concentrations of crosslinker were imaged by scanning electron microscopy.…”

“…K88 strains of ETEC that cause diarrhea in pigs possess an adhesin essential for disease to occur [ 19 ]. Recent reports show that K88 adhesin targets specific receptors containing galactose exposed when using lactosylated albumin [ 13 , 14 ]. In this study, the formulation of stabilized microspheres, antibiotic carriers, using lactosylated albumin as encapsulation polymer, was examined.…”

“…Our group has reported that BSA chemically modified with lactose (BSA-Lac) leads to recognition of piglet pathogens, such as enterotoxigenic Escherichia coli K88, and by carbohydrate-binding proteins from Ricinus communis agglutinin I (RCA I), a galactose specific lectin [ 13 , 14 ]. The aim of this work was to use BSA-Lac as a polymer to obtain lactosylated microspheres (MS-Lac) that carry gentamicin and to stabilize them by crosslinking.…”

Molecular recognition of glyconanoparticles by RCA and E. coli K88 - designing transports for targeted therapy

“…This coupling reaction of protein with sugar produces neoglycans. Previous reports indicate that glycation is favored by temperatures above 60°C, alkaline pH, and influenced by moisture and reaction time (Ledesma-Osuna et al, 2009;Sarabia-Sainz et al, 2011). Other factors, such as water activity, intrinsic properties of protein and sugar, and the amino group-reducing sugar ratio, influence the yields and types of the Maillard reaction products.…”

“…These bacteria are a perfect model to study the feasibility of glyco-nanomaterials in different processes in the field of medicine (Miura et al, 2016;Sattin & Bernardi, 2016). Previously, we reported that the modification of BSA with lactose (BSA-Lac) through thermal glycation promotes recognition of the bacterial adhesin (Sarabia-Sainz et al, 2011). In addition, the BSA-Lac microspheres were recognized by partially purified K88 adhesin of E. coli K88 (Sarabia-Sainz et al, 2015).…”