The conserved N-terminus of human rhinovirus capsid protein VP4 contains membrane pore-forming activity and is a target for neutralizing antibodies.
The conserved N-terminus of human rhinovirus capsid protein VP4 contains membrane pore-forming activity and is a target for neutralizing antibodies.
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DOI：
10.1099/jgv.0.000629
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发表时间：
2016-12
期刊：
影响因子：
--
通讯作者：
Tuthill TJ
中科院分区：
文献类型：
--
作者：
Panjwani A;Asfor AS;Tuthill TJ
人鼻病毒是普通感冒的病原体，属于无包膜小核糖核酸病毒家族。诸如受体结合或低pH的触发物引发衣壳中的构象变化，其允许病毒附着于膜并形成用于将病毒RNA易位到细胞质中的孔。我们先前表明，重组衣壳蛋白VP 4能够形成膜孔。在这项研究中，我们发现VP 4的N-末端而不是C-末端形成的孔具有与全长VP 4相似的性质，并且与RNA转移所需的大小一致。针对VP 4的N-末端而非C-末端的血清显示中和病毒感染性。总之，这表明VP 4的N-末端负责膜活性。这项研究有助于更好地了解VP 4参与进入的机制及其作为抗病毒靶点的潜力。
Human rhinovirus is the causative agent of the common cold and belongs to the non-enveloped picornavirus family. A trigger such as receptor binding or low pH initiates conformational changes in the capsid that allow the virus to attach to membranes and form a pore for the translocation of viral RNA into the cytoplasm. We previously showed that recombinant capsid protein VP4 was able to form membrane pores. In this study, we show the N-terminus but not C-terminus of VP4 formed pores with properties similar to full-length VP4 and consistent with the size required for transfer of RNA. Sera against the N-terminus but not C-terminus of VP4 were shown to neutralize virus infectivity. Together, this suggests that the N-terminus of VP4 is responsible for membrane activity. This study contributes to an improved understanding of the mechanisms for involvement of VP4 in entry and its potential as an antiviral target.
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