 |
Journal articles
The sweet connection: Solving the riddle of multiple sugar-binding fimbrial adhesins in Escherichia coli: Multiple E. coli fimbriae form a versatile arsenal of sugar-binding lectins potentially involved in surface-colonisation and tissue tropism.
Abstract : Proteinaceous stalks produced by Gram-negative bacteria are often used to adhere to environmental surfaces. Among them, chaperone-usher (CU) fimbriae adhesins, related to prototypical type 1 fimbriae, interact in highly specific ways with different ligands at different stages of bacterial infection or surface colonisation. Recent analyses revealed a large number of potential and often "cryptic" CU fimbriae homologues in the genome of commensal and pathogenic Escherichia coli and closely related bacteria. We propose that CU fimbriae form a yet unexplored arsenal of lectins, carbohydrate-binding proteins involved in various aspects of bacterial surface adhesion and tissue tropism. Combined efforts of molecular and structural biologists will be required to unravel the biological contribution of the bacterial lectome, however, current progress has already opened up new perspectives in the design of novel anti-infective strategies.
Keywords :
Signal Transduction
Surface Properties
Tropism
Protein Binding
Lectins/*metabolism
Operon
lectins
Escherichia coli Proteins/*metabolism/secretion
Fimbriae
Bacterial/*metabolism
Humans
Adhesins
Escherichia coli/*metabolism/ultrastructure
adhesion
Animals
bacterial tropism
Cell Adhesion
Escherichia coli
Escherichia coli/growth & development/*metabolism
Escherichia coli Infections/drug therapy/prevention & control
https://hal-pasteur.archives-ouvertes.fr/pasteur-01393506
Contributor : Anne Lassailly-Bondaz Connect in order to contact the contributor
Submitted on : Wednesday, May 5, 2021 - 6:50:39 PM
Last modification on : Tuesday, October 19, 2021 - 10:26:37 PM
Contributor : Anne Lassailly-Bondaz Connect in order to contact the contributor
Submitted on : Wednesday, May 5, 2021 - 6:50:39 PM
Last modification on : Tuesday, October 19, 2021 - 10:26:37 PM
Links full text
