| Autor: |
Valiente E; Department of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK., Davies C; Department of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK., Mills DC; Department of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK.; Robert Frederick Smith School of Chemical and Biomolecular Engineering, Cornell University, Olin Hall, Ithaca, NY, USA., Getino M; Department of Microbial Sciences, Faculty of Health and Medical Sciences, University of Surrey, Guildford, GU2 7XH, UK., Ritchie JM; Department of Microbial Sciences, Faculty of Health and Medical Sciences, University of Surrey, Guildford, GU2 7XH, UK., Wren BW; Department of Pathogen Molecular Biology, London School of Hygiene and Tropical Medicine, Keppel Street, WC1E 7HT, London, UK. Brendan.wren@lshtm.ac.uk. |
| Abstrakt: |
Vibrio cholerae O1 El Tor is an aquatic Gram-negative bacterium responsible for the current seventh pandemic of the diarrheal disease, cholera. A previous whole-genome analysis on V. cholerae O1 El Tor strains from the 2010 epidemic in Pakistan showed that all strains contained the V. cholerae pathogenicity island-1 and the accessory colonisation gene acfC (VC_0841). Here we show that acfC possess an open reading frame of 770 bp encoding a protein with a predicted size of 28 kDa, which shares high amino acid similarity with two adhesion proteins found in other enteropathogens, including Paa in serotype O45 porcine enteropathogenic Escherichia coli and PEB3 in Campylobacter jejuni. Using a defined acfC deletion mutant, we studied the specific role of AcfC in V. cholerae O1 El Tor environmental survival, colonisation and virulence in two infection model systems (Galleria mellonella and infant rabbits). Our results indicate that AcfC might be a periplasmic sulfate-binding protein that affects chemotaxis towards mucin and bacterial infectivity in the infant rabbit model of cholera. Overall, our findings suggest that AcfC contributes to the chemotactic response of WT V. cholerae and plays an important role in defining the overall distribution of the organism within the intestine. |
