Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.
Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.
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DOI：
10.1126/sciadv.abq0619
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发表时间：
2023-02-22
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影响因子：
13.6
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中科院分区：
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捕食性δ-变形杆菌黄色粘球菌在细菌粘着斑（bFA）部位使用螺旋状的马达来驱动滑行运动。使用全内反射荧光和力显微镜，我们确定了冯维勒布兰德A域包含外膜（OM）脂蛋白CglB作为一个必不可少的基底耦合粘附的滑行换能器（GLT）机械在bFAs。生物化学和遗传学分析表明，CglB定位于细胞表面，独立于Glt装置;一旦到达那里，它就被滑动机制的OM模块招募，OM模块是一种含有完整OM β桶GltA、GltB和GltH以及OM蛋白GltC和OM脂蛋白GltK的异源低聚复合物。该Glt OM平台介导细胞表面可及性和Glt装置对CglB的保留。总之，这些数据表明，滑动复合物促进调节的表面暴露的CglB在bFA，从而解释了由内膜马达施加的收缩力跨细胞被膜转导到底层的方式。一个外膜复合物暴露的细胞表面CglB粘附素在细菌的焦点粘附网站介导的滑行运动。
The predatory deltaproteobacterium Myxococcus xanthus uses a helically-trafficked motor at bacterial focal-adhesion (bFA) sites to power gliding motility. Using total internal reflection fluorescence and force microscopies, we identify the von Willebrand A domain-containing outer-membrane (OM) lipoprotein CglB as an essential substratum-coupling adhesin of the gliding transducer (Glt) machinery at bFAs. Biochemical and genetic analyses reveal that CglB localizes to the cell surface independently of the Glt apparatus; once there, it is recruited by the OM module of the gliding machinery, a heteroligomeric complex containing the integral OM β barrels GltA, GltB, and GltH, as well as the OM protein GltC and OM lipoprotein GltK. This Glt OM platform mediates the cell-surface accessibility and retention of CglB by the Glt apparatus. Together, these data suggest that the gliding complex promotes regulated surface exposure of CglB at bFAs, thus explaining the manner by which contractile forces exerted by inner-membrane motors are transduced across the cell envelope to the substratum. An outer-membrane complex exposes the cell-surface CglB adhesin at bacterial focal-adhesion sites to mediate gliding motility.
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