The MSHA pilus of Vibrio parahaemolyticus has lectin functionality and enables TTSS-mediated pathogenicity
| Autor: | Michelle Kilcoyne, Benoit Houeix, Lokesh Joshi, Aoife Boyd, Nicky O’Boyle |
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| Rok vydání: | 2013 |
| Předmět: |
Microbiology (medical)
Virulence Factors Cell DNA Mutational Analysis Microbiology Mannose-Binding Lectin Pilus Bacterial Adhesion Type three secretion system 03 medical and health sciences Polysaccharides medicine Humans Secretion Bacterial Secretion Systems 030304 developmental biology 0303 health sciences biology 030306 microbiology Effector Vibrio parahaemolyticus Epithelial Cells General Medicine biology.organism_classification Intestinal epithelium Bacterial adhesin Infectious Diseases medicine.anatomical_structure Hemagglutinins Blood Group Antigens bacteria Fimbriae Proteins Caco-2 Cells Protein Binding |
| Zdroj: | International Journal of Medical Microbiology International Journal of Medical Microbiology; Vol 303 |
| ISSN: | 1618-0607 |
| Popis: | Vibrio parahaemolyticus is a seafood-borne pathogen which causes acute inflammatory gastroenteritis--a process which is mediated by the translocation of type three secretion system effector proteins. The molecular interactions governing colonization of the intestinal epithelium by this pathogen remain poorly understood. The mannose-sensitive haemagglutinin (MSHA) pilus was identified in this study as a significant factor in bacterial-host cell adherence and subsequent pathogenesis towards Caco-2 human intestinal epithelial cells. Deletion of essential components of the MSHA pilus resulted in a 60% decrease in adherence and a similar reduction in bacterial uptake by human intestinal cells. The diminished adherence of MSHA mutants correlated with significant decreases in V. parahaemolyticus-induced Caco-2 cell lysis, cell rounding and IL-8 secretion. Glycan array comparison between the V. parahaemolyticus wild type and MSHA deficient mutants identified lectin functionality for the MSHA pilus with specificity towards the fucosylated blood group oligosaccharide antigens Lewis A and X and blood groups A and B. The MSHA pilus also exhibited high affinity for the structurally related asialo-GM1 ganglioside, lacto-N-fucopentaose I and lacto-N-difucohexaose I. We hypothesize that these glycans act as receptors for the MSHA pilus in the gastrointestinal tract, thereby facilitating efficient colonization of the intestinal epithelium by V. parahaemolyticus. |
| Databáze: | OpenAIRE |
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