Preparations of probiotic bifidobacterial and lactobacillus lectins possessed system affinity to mannan and mucin-type polymers. It was shown that these lectins possess fungistatic and fungicidal activities against nystatin-resistant Candida albicans clinical strains. Lectins revealed destructive properties with respect to C. albicans and Staphylococcus aureus biofilms, depending on clinical strain origin and lectin preparation type. Synergistic antipathogen activities between lectins and between lectins and nystatin were observed. In the presence of lectins, pathogen biofilm degradation occurred in sequential steps, including biofilm refinement, appearance of edge cavities, segmentation, detachment of fragments and their lysis. Fungal response to lectins was more complex compared to that of staphylococci. Cold stress improved pictures of lectin antipathogen action. The data indicate that probiotic bacterial lectins are members of a new class of antimicrobials-destructors of pathogen biofilms.
In this review our last results and proposals with respect to general aspects of lectin studies are summarised and compared. System presence, organisation and functioning of lectins are proposed, and accents on beneficial symbiotic microbial lectins studies are presented. The proposed general principles of lectin functioning allows for a comparison of lectins with other carbohydrate-recognition systems. A new structure-functional superfamily of symbiotic microbial lectins is proposed and its main properties are described. The proposed superfamily allows for extended searches of the biological activities of any microbial member. Prospects of lectins of beneficial symbiotic microorganisms are discussed.
Lectins (natural or artificial nonimmunoglobulin origin proteins/glycoproteins) are able to bind noncovalently with carbohydrate targets. Lectins and lectin-like substances of lactobacilli (L. acidophilus K 3 III 24 ; 100ash; NK1; L. plantarum 8RA3) and bifidobacteria (B. adolescentis MC42; B gallinarum, B. bifidum 1) have been investigated. Bacteria were grown in semi-anaerobic conditions in a casein-yeast broth. Medium was microfiltrated and ultrafiltrated for isolation of 30 kDa compounds which were then separated by isoelectric focusing in polyacrylamide gel in the presence of urea and sucrose. Components isolated were electrotransferred to immobillon P. Blots obtained were then treated with a set of biotinylated artificial linear homopolysaccharides revealed by streptavidin-peroxidase conjugate. Chemiluminescence registration of peroxidase bound to blots was performed using the 'BioChemi System' camera. A spectrum of different polysaccharidebinding individual components reacting with such homopolymers as mannan-alpha (phosphorylated or not), GalNAcalpha-polysaccharide of mucin-like-type or galactan-beta (sulfated or not)-binding was found in lactobacilli and bifidobacteria. Lactobacilli produced a more limited spectrum of lectins or lectin-like compounds with higher affinities to polysaccharides tested than bifidobacteria having more extended pI polysaccharide-binding activity spectrum. Interaction of isolated lectins with T and B lymphocytes, macrophages, and thrombocytes was demonstrated. The importance of lactobacilli and bifidobacteria lectins/lectin-like components and their effector complexes in cell mitoses, blood coagulation, aerobic metabolic reactions, and other biological activities is discussed.
A system of new lectins (acidic and basic) isolated from probiotic lactobacilli and bifidobacteria cultural fluids are described for the first time. The lectins investigated have many physicochemical, biochemical and biological features in common. The basic properties of investigated probiotic lectins are discussed. The new working determination of lectins and their current classification are proposed. The perspectives of investigated lactobacilli and bifidobacteria lectins are given.
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