Publication: Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence
| dc.contributor.author | Simmons, Cameron | |
| dc.date.accessioned | 2018-09-14T11:15:06Z | |
| dc.date.available | 2017-07-05T04:56:35Z | |
| dc.date.available | 2018-09-14T11:15:06Z | |
| dc.date.issued | 2002-03-01 | en_US |
| dc.description.abstract | Intimate bacterial adhesion to intestinal epithelium is a pathogenic mechanism shared by several human and animal enteric pathogens, including enteropathogenic and enterohaemorrhagic Escherichia coli and Citrobacter rodentium. The proteins directly involved in this process are the outer-membrane adhesion molecule intimin and the translocated intimin receptor, Tir. The receptor-binding activity of intimin resides within the carboxy terminus 280 aa (Int280) of the polypeptide. Four tryptophan residues, W117/776, W136/795, W222/881 and W240/899, are conserved within different Int280 molecules that otherwise show considerable sequence variation. In this study the influence of site-directed mutagenesis of each of the four tryptophan residues on intimin-Tir interactions and on intimin-mediated intimate attachment was determined. The mutant intimins were also studied using a variety of in vitro and in vivo infection models. The results show that all the substitutions modulated intimin activity, although some mutations had more profound effects than others. | |
| dc.identifier.uri | https://demo7.dspace.org/handle/123456789/202 | |
| dc.language | English | en_US |
| dc.title | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence | en_US |
| dc.type | Journal Article | |
| dspace.entity.type | Publication | |
| dspace.relatedentity.type | Person | |
| relation.isAuthorOfPublication | b1b2c768-bda1-448a-a073-fc541e8b24d9 | |
| relation.isAuthorOfPublication.latestForDiscovery | b1b2c768-bda1-448a-a073-fc541e8b24d9 |