Unveiling molecular interactions that stabilize bacterial adhesion pili.
Unveiling molecular interactions that stabilize bacterial adhesion pili.
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DOI:
10.1016/j.bpj.2022.04.036
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发表时间:
2022-06-07
影响因子:
3.4
通讯作者:
Andersson, Magnus
中科院分区:
文献类型:
--
作者:
Dahlberg, Tobias;Baker, Joseph L.;Bullitt, Esther;Andersson, Magnus
Adhesion pili assembled by the chaperone-usher pathway are superelastic helical filaments on the surface of bacteria, optimized for attachment to target cells. Here, we investigate the biophysical function and structural interactions that stabilize P pili from uropathogenic bacteria. Using optical tweezers, we measure P pilus subunit-subunit interaction dynamics and show that pilus compliance is contour-length dependent. Atomic details of subunit-subunit interactions of pili under tension are shown using steered molecular dynamics (sMD) simulations. sMD results also indicate that the N-terminal “staple” region of P pili, which provides interactions with pilins that are four and five subunits away, significantly stabilizes the helical filament structure. These data are consistent with previous structural data, and suggest that more layer-to-layer interactions could compensate for the lack of a staple in type 1 pili. This study informs our understanding of essential structural and dynamic features of adhesion pili, supporting the hypothesis that the function of pili is critically dependent on their structure and biophysical properties.
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影响因子:
64.5
作者:
Hospenthal MK;Redzej A;Dodson K;Ukleja M;Frenz B;Rodrigues C;Hultgren SJ;DiMaio F;Egelman EH;Waksman G
通讯作者:
Waksman G
DOI:
10.1016/j.str.2017.10.004
发表时间:
2017-12-05
期刊:
Structure (London, England : 1993)
影响因子:
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作者:
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DOI:
10.1007/s00249-007-0223-6
发表时间:
2008-04-01
影响因子:
2
作者:
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通讯作者:
Andersson, Magnus
DOI:
10.1007/s00249-009-0552-8
发表时间:
2010-07-01
影响因子:
2
作者:
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通讯作者:
Andersson, Magnus
影响因子:
3.4
作者:
Jass, J;Schedin, S;Axner, O
通讯作者:
Axner, O