期刊
CELL
卷 109, 期 7, 页码 913-923出版社
CELL PRESS
DOI: 10.1016/S0092-8674(02)00796-1
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资金
- NHGRI NIH HHS [1 P50 HG02360-01] Funding Source: Medline
- NIAID NIH HHS [R01 AI45820] Funding Source: Medline
- NIDDK NIH HHS [P01 DK53369] Funding Source: Medline
- NIGMS NIH HHS [5R01 GM49063] Funding Source: Medline
Surface adhesion of bacteria generally occurs in the presence of shear stress, and the lifetime of receptor bonds is expected to be shortened in the presence of external force. However, by using Escherichia coli expressing the lectin-like adhesin FimH and guinea pig erythrocytes in flow chamber experiments, we show that bacterial attachment to target cells switches from loose to firm upon a 10-fold increase in shear stress applied. Steered molecular dynamics simulations of tertiary structure of the FimH receptor binding domain and subsequent site-directed mutagenesis studies indicate that shear-enhancement of the FimH-receptor interactions involves extention of the interdomain linker chain under mechanical force. The ability of FimH to function as a force sensor provides a molecular mechanism for discrimination between surface-exposed and soluble receptor molecules.
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