Tyrosine residues at the immunoglobulin-C-type lectin inter-domain boundary of intimin are not involved in Tir-binding but implicated in colonisation of the host
Intimin is an outer membrane adhesion molecule involved in bacterial adhesion to intestinal epithelium by several human and animal enteric pathogens, including enteropathogenic and enterohaemorrhagic Escherichia coli and Citrobacter rodentium. Intimin binds to the translocated intimin receptor, Tir,...
Salvato in:
| Autore principale: | |
|---|---|
| Natura: | Journal Article |
| Lingua: | inglese |
| Pubblicazione: |
2018
|
| Accesso online: | https://demo7.dspace.org/handle/123456789/210 |
| Tags: |
Nessun Tag, puoi essere il primo ad aggiungerne!!
|
Documenti analoghi: Tyrosine residues at the immunoglobulin-C-type lectin inter-domain boundary of intimin are not involved in Tir-binding but implicated in colonisation of the host
- Mutagenesis of conserved tryptophan residues within the receptor-binding domain of intimin: influence on binding activity and virulence
- Equilibrium and kinetics of binding of immunoglobulin G and impurity proteins on chromatographic adsorbents dissertation thesis
- Site-directed mutagenesis of intimin alpha modulates intimin-mediated tissue tropism and host specificity
- Lectins and Glycoconjugates in Oncology /
- Microbial Lectins and Agglutinins : Properties and Biological Activity /
- Podmienky v systéme TIR čoraz prísnejšie