Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence
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 adh...
Salvato in:
| Autore principale: | |
|---|---|
| Natura: | Journal Article |
| Lingua: | inglese |
| Pubblicazione: |
2018
|
| Accesso online: | https://demo7.dspace.org/handle/123456789/202 |
| Tags: |
Nessun Tag, puoi essere il primo ad aggiungerne!!
|
| _version_ | 1860822453917319169 |
|---|---|
| author | Simmons, Cameron |
| author_browse | Simmons, Cameron |
| author_facet | Simmons, Cameron |
| author_sort | Simmons, Cameron |
| collection | DSpace |
| description | 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. |
| format | Journal Article |
| id | oai:localhost:123456789-202 |
| institution | DSPACE.FCHPT |
| language | English |
| publishDate | 2018 |
| publishDateRange | 2018 |
| publishDateSort | 2018 |
| record_format | dspace |
| spelling | oai:localhost:123456789-2022021-04-07T16:30:08Z Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence Simmons, Cameron 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. 2018-09-14T11:15:06Z 2017-07-05T04:56:35Z 2018-09-14T11:15:06Z 2002-03-01 Journal Article https://demo7.dspace.org/handle/123456789/202 English |
| spellingShingle | Simmons, Cameron Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title_full | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title_fullStr | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title_full_unstemmed | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title_short | Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence |
| title_sort | mutagenesis of conserved tryptophan residues within the receptor binding domain of intimin influence on binding activity and virulence |
| url | https://demo7.dspace.org/handle/123456789/202 |
| work_keys_str_mv | AT simmonscameron mutagenesisofconservedtryptophanresidueswithinthereceptorbindingdomainofintimininfluenceonbindingactivityandvirulence |