Interdomain interaction in the FimH adhesin of Escherichia coli regulates the affinity to mannose

被引:117
作者
Aprikian, Pavel
Tchesnokova, Veronika
Kidd, Brian
Yakovenko, Olga
Yarov-Yarovoy, Vladimir
Trinchina, Elena
Vogel, Viola
Thomas, Wendy [2 ]
Sokurenko, Evgeni
机构
[1] Univ Washington, Dept Microbiol, Seattle, WA 98105 USA
[2] Univ Washington, Dept Bioengn, Seattle, WA 98105 USA
[3] Univ Washington, Dept Pharmacol, Seattle, WA 98105 USA
[4] Univ Washington, Nanotechnol Ctr, Seattle, WA 98105 USA
[5] ETH, Swiss Fed Inst Technol, Dept Mat, Lab Biol Oriented Mat, CH-8093 Zurich, Switzerland
关键词
D O I
10.1074/jbc.M702037200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
FimH is a mannose-specific adhesin located on the tip of type 1 fimbriae of Escherichia coli that is capable of mediating shear-enhanced bacterial adhesion. FimH consists of a fimbria-associated pilin domain and a mannose-binding lectin domain, with the binding pocket positioned opposite the interdomain interface. By using the yeast two-hybrid system, purified lectin and pilin domains, and docking simulations, we show here that the FimH domains interact with one another. The affinity for mannose is greatly enhanced (up to 300-fold) in FimH variants in which the interdomain interaction is disrupted by structural mutations in either the pilin or lectin domains. Also, affinity to mannose is dramatically enhanced in isolated lectin domains or in FimH complexed with the chaperone molecule that is wedged between the domains. Furthermore, FimH with native structure mediates weak binding at low shear stress but shifts to strong binding at high shear, whereas FimH with disrupted interdomain contacts ( or the isolated lectin domain) mediates strong binding to mannose-coated surfaces even under low shear. We propose that interactions between lectin and pilin domains decrease the affinity of the mannose-binding pocket via an allosteric mechanism. We further suggest that mechanical force at high shear stress separates the two domains, allowing the lectin domain to switch from a low affinity to a high affinity state. This shift provides a mechanism for FimH-mediated shear-enhanced adhesion by enabling the adhesin to form catch bond-like interactions that are longer lived at high tensile force.
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页码:23437 / 23446
页数:10
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