Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilus.
Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilus.
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DOI：
10.1016/j.jmb.2012.02.017
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发表时间：
2012-04-20
影响因子：
5.6
通讯作者：
Craig, Lisa
中科院分区：
文献类型：
--
作者：
Li, Juliana;Egelman, Edward H.;Craig, Lisa
IV型皮利是许多细菌病原体上显示的多功能丝状体。IVa型菌毛亚类的成员存在于多种人类病原体上，而IVb型皮利几乎只存在于肠道细菌上。IVa型和IVb型亚类的区别在于菌毛蛋白亚基的差异，包括球状结构域的折叠。为了了解不同的菌毛蛋白折叠的影响，我们比较了菌毛蛋白亚基和菌毛丝的稳定性IVa型GC菌毛淋病奈瑟菌和IVb型毒素共调节菌毛（TCP）霍乱弧菌。我们发现，虽然重组TCP菌毛蛋白比GC菌毛蛋白更稳定，GC皮利比TCP更耐蛋白水解，热和化学变性，在8 M尿素中保持完整。为了理解这些差异，我们通过电子显微镜和3D图像重建确定了TCP结构。TCP具有与GC皮利相似的结构，其亚基以右旋单头螺旋排列，并通过8.4 °的轴向上升和96.8°的方位角旋转相关。然而，TCP亚基不像GC菌毛蛋白那样紧密堆积，并且独特的IVb型菌毛蛋白折叠暴露TCP的α-螺旋核心的一段。疏水相互作用占主导地位的两个菌毛亚型，但由IVa型菌毛保守的芳香残基的碱基堆积可能有助于GC菌毛的稳定性。GC皮利的非凡稳定性可能代表IVa型皮利对恶劣环境的适应以及抵抗外力缩回的需要。
Type IV pili are multifunctional filaments displayed on many bacterial pathogens. Members of the Type IVa pilus subclass are found on a diverse group of human pathogens whereas Type IVb pili are almost exclusively on enteric bacteria. The Type IVa and IVb subclasses are distinguished by differences in the pilin subunits, including the fold of the globular domain. To understand the implications of the distinct pilin folds we compared the stabilities of pilin subunits and pilus filaments for the Type IVa GC pilus from Neisseria gonorrhoeae and the Type IVb toxin-coregulated pilus (TCP) from Vibrio cholerae. We show that while recombinant TCP pilin is more stable than GC pilin, the GC pili are more resistant than TCP to proteolysis, heat and chemical denaturation, remaining intact in 8 M urea. To understand these differences we determined the TCP structure by electron microscopy and 3D image reconstruction. TCP have a similar architecture to GC pili, with subunits arranged in a right-handed one-start helix and related by an 8.4 Å axial rise and a 96.8° azimuthal rotation. However, the TCP subunits are not as tightly packed as GC pilins and the distinct Type IVb pilin fold exposes a segment of the α-helical core of TCP. Hydrophobic interactions dominate for both pilus subtypes, but base-stacking by aromatic residues conserved among the Type IVa pilins may contribute to GC pilus stability. The extraordinary stability of GC pili may represent an adaptation of the Type IVa pili to harsh environments and the need to retract against external forces.
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影响因子：
10.5
作者：
KAUFMAN, MR;SEYER, JM;TAYLOR, RK
通讯作者：
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DOI：
10.1073/pnas.93.15.7991
发表时间：
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影响因子：
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3.1
作者：
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DOI：
10.1073/pnas.0707581104
发表时间：
2007-10-02
影响因子：
11.1
作者：
Helaine, Sophie;Dyer, David H.;Forest, Katrina T.
通讯作者：
Forest, Katrina T.