Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits.
Characterization of a glycan-binding complex of minor pilins completes the analysis of Streptococcus sanguinis type 4 pili subunits.
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DOI:
10.1073/pnas.2216237120
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发表时间:
2023-01-17
影响因子:
11.1
通讯作者:
Pelicic, Vladimir
中科院分区:
文献类型:
--
作者:
Shahin, Meriam;Sheppard, Devon;Raynaud, Claire;Berry, Jamie-Lee;Gurung, Ishwori;Silva, Lisete M.;Feizi, Ten;Liu, Yan;Pelicic, Vladimir
Type 4 pili (T4P)—important in bacterial pathogens—are filaments composed of one well-characterized major pilin, and several minor pilins whose roles are often poorly understood. Streptococcus sanguinis T4P are composed of five pilins, which makes it a good model to determine the role of each pilin subunit in detail. Here, we characterize PilA and PilC, showing how they interact and how they function. Together with our previous findings, this provides an integrated view of the role of the five pilin subunits in S. sanguinis T4P. PilE1/PilE2 are the major pilins forming the backbone of the filament, while the three minor pilins (PilA, PilB, and PilC) form a tip-located complex promoting adhesion to various host receptors. Type 4 filaments (T4F)—of which type 4 pili (T4P) are the archetype—are a superfamily of nanomachines nearly ubiquitous in prokaryotes. T4F are polymers of one major pilin, which also contain minor pilins whose roles are often poorly understood. Here, we complete the structure/function analysis of the full set of T4P pilins in the opportunistic bacterial pathogen Streptococcus sanguinis. We determined the structure of the minor pilin PilA, which is unexpectedly similar to one of the subunits of a tip-located complex of four minor pilins, widely conserved in T4F. We found that PilA interacts and dramatically stabilizes the minor pilin PilC. We determined the structure of PilC, showing that it is a modular pilin with a lectin module binding a subset of glycans prevalent in the human glycome, the host of S. sanguinis. Altogether, our findings support a model whereby the minor pilins in S. sanguinis T4P form a tip-located complex promoting adhesion to various host receptors. This has general implications for T4F.
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DOI:
10.1126/science.aad2001
发表时间:
2016-03-11
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
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通讯作者:
Jensen GJ
影响因子:
64.8
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通讯作者:
Hassabis D
DOI:
10.1073/pnas.1218832110
发表时间:
2013-02-19
影响因子:
11.1
作者:
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通讯作者:
Pelicic, Vladimir
影响因子:
6.8
作者:
Egelman, Edward H.
通讯作者:
Egelman, Edward H.
DOI:
10.1107/s0907444909042073
发表时间:
2010-01
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
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作者:
Chen VB;Arendall WB 3rd;Headd JJ;Keedy DA;Immormino RM;Kapral GJ;Murray LW;Richardson JS;Richardson DC
通讯作者:
Richardson DC