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To characterize the interaction potential of the human vaginal isolate  Lactobacillus plantarum  CMPG5300, its genome was mined for genes encoding lectin-like proteins.  cmpg5300.05_29  was identified as the gene encoding a putative mannose-binding lectin. Phenotypic analysis of a gene knock-out mutant of  cmpg5300.05_29  showed that expression of this gene is important for auto-aggregation, adhesion to the vaginal epithelial cells, biofilm formation and binding to mannosylated glycans. Purification of the predicted lectin domain of Cmpg5300.05_29 and characterization of its sugar binding capacity confirmed the specificity of the lectin for high- mannose glycans. Therefore, we renamed Cmpg5300.05_29 as a mannose-specific lectin (Msl). The purified lectin domain of Msl could efficiently bind to HIV-1 glycoprotein gp120 and  Candida albicans,  and showed an inhibitory activity against biofilm formation of uropathogenic  Escherichia coli ,  Staphylococcus aureus  and  Salmonella  Typhimurium. Thus, using a combination of molecular lectin characterization and functional assays, we could show that lectin-sugar interactions play a key role in host and pathogen interactions of a prototype isolate of the vaginal  Lactobacillus  microbiota.

High mannose-specific lectin Msl mediates key interactions of the vaginal Lactobacillus plantarum isolate CMPG5300