FimH family of type 1 fimbrial adhesins: functional heterogeneity due to minor sequence variations among fimH genes
نویسندگان
چکیده
منابع مشابه
Heterobinary adhesins based on the Escherichia coli FimH fimbrial protein.
The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to D-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions b...
متن کاملPopulation variability of the FimH type 1 fimbrial adhesin in Klebsiella pneumoniae.
FimH is an adhesive subunit of type 1 fimbriae expressed by different enterobacterial species. The enteric bacterium Klebsiella pneumoniae is an environmental organism that is also a frequent cause of sepsis, urinary tract infection (UTI), and liver abscess. Type 1 fimbriae have been shown to be critical for the ability of K. pneumoniae to cause UTI in a murine model. We show here that the K. p...
متن کاملType 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of Escherichia coli.
Escherichia coli causes about 90% of urinary tract infections (UTI), and more than 95% of all UTI-causing E. coli express type 1 fimbriae. The fimbrial tip-positioned adhesive protein FimH utilizes a shear force-enhanced, so-called catch-bond mechanism of interaction with its receptor, mannose, where the lectin domain of FimH shifts from a low- to a high-affinity conformation upon separation fr...
متن کاملTranscriptional Response Of E. coli Upon FimH-mediated Fimbrial Adhesion
Functionalities which may be genetically programmed into a bacterium are limited by its range of possible activities and its sensory capabilities. Therefore, enhancing the bacterial sensory repertoire is a crucial step for expanded utility in potential biomedical, industrial or environmental applications. Using microarray and qRT-PCR analyses, we have investigated transcription in E. coli (stra...
متن کاملAllosteric Coupling in FimH
Background: The bacterial adhesin FimH is allosterically regulated. Results: Mutations designed to control the allosteric state of the protein created low or high affinity variants as predicted. Conclusion: Three regulatory regions are strongly coupled together, while the active site is more weakly coupled to those regions. Significance: Allosteric regulation can be used to develop antiadhesive...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1994
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.176.3.748-755.1994