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

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...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports 2016-11, Vol.6 (1), p.37339-37339, Article 37339
Main Authors: Malik, Shweta, Petrova, Mariya I., Imholz, Nicole C. E., Verhoeven, Tine L. A., Noppen, Sam, Van Damme, Els J. M., Liekens, Sandra, Balzarini, Jan, Schols, Dominique, Vanderleyden, Jos, Lebeer, Sarah
Format: Article
Language:English
Subjects:
13/106
45/44
45/70
631/326/325/1506
631/326/46
631/326/596/1296
631/337/475
692/699/2768/1865
82/103
82/83
Biofilms
E coli
Epithelial cells
Genomes
Glycoprotein gp120
Humanities and Social Sciences
Lectins
Mannose
Mannose-binding lectin
multidisciplinary
Polysaccharides
Science
Sugar
Vagina
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep37339