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首页> 外文期刊>Biochemistry >P-protein of chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage.
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P-protein of chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage.

机译：查德普拉病毒的P蛋白是一种N蛋白特异性伴侣蛋白，在成核阶段起作用。

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The nucleocapsid protein N of Chandipura virus is prone to aggregation in vitro. We have shown that this aggregation occurs in two phases in a nucleation-dependent manner. Electron microscopy suggests that the aggregated state may have a ring-like structure. Using a GFP fusion, we have shown that the N-protein also aggregates in vivo. The P-protein suppresses the N-protein aggregation efficiently, both in vitro and in vivo. Increased lag phase in the presence of the P-protein suggests that chaperone-like action of the P-protein occurs before the nucleation event. The P-protein, however, does not exert any chaperone-like action against other proteins, suggesting that it binds to the N-protein specifically. Surface plasmon resonance and fluorescence enhancement indeed suggest that the P-protein binds tightly to the native N-protein. The P-protein is thus an N-protein-specific chaperone which inhibits the nucleation phase of N-protein aggregation, thus keeping a pool of encapsidation-competent N-protein for viral maturation.
机译：Chandipura病毒的核衣壳蛋白N在体外易于聚集。我们已经表明，这种聚集以成核依赖性的方式在两个阶段中发生。电子显微镜表明，聚集态可以具有环状结构。使用GFP融合蛋白，我们已经显示N蛋白在体内也会聚集。 P蛋白在体外和体内均有效抑制N蛋白聚集。在存在P蛋白的情况下增加的滞后阶段表明P蛋白的伴侣样作用发生在成核事件之前。但是，P蛋白对其他蛋白没有任何伴侣状作用，表明它与N蛋白特异性结合。表面等离子体共振和荧光增强确实表明，P蛋白与天然N蛋白紧密结合。因此，P蛋白是一种N蛋白特异性伴侣蛋白，可抑制N蛋白聚集的成核相，从而保留了能进行衣壳化的N蛋白，可用于病毒成熟。

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