Mutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus budding
Mutations in the FPIV motif of Newcastle disease virus matrix protein attenuate virus replication and reduce virus budding
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DOI：
10.1007/s00705-014-1998-2
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发表时间：
2014-07-01
影响因子：
2.7
通讯作者：
Liu, Xiufan
中科院分区：
文献类型：
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作者：
Duan, Zhiqiang;Hu, Zenglei;Liu, Xiufan
在副流感病毒5型和腮腺炎病毒的基质（M）蛋白中鉴定的FPIV样晚期结构域已被证明对病毒出芽至关重要。在本研究中，我们发现相同的FPIV序列基序存在于纽卡斯尔病毒（NDV）M蛋白的N-末端。突变实验表明，苯丙氨酸（F）或脯氨酸（P）突变为丙氨酸均使病毒毒力和复制能力明显下降，并导致突变病毒的出芽能力下降。此外，获得了涉及细胞多泡体（MVB）蛋白的证据，因为在VPS 4A-E228 Q蛋白的显性阴性形式表达后，NDV产生被抑制。总之，这些结果表明，FPIV基序，特别是残基F和P，在NDV M蛋白中，在NDV复制和出芽中起关键作用，并且该出芽过程可能涉及细胞MVB途径。
The FPIV-like late domains identified in the matrix (M) proteins of parainfluenza virus 5 and mumps virus have been demonstrated to be critical for virus budding. In this study, we found that the same FPIV sequence motif is present in the N-terminus of the Newcastle disease virus (NDV) M protein. Mutagenesis experiments demonstrated that mutation of either phenylalanine (F) or proline (P) to alanine led to a more obvious decrease in viral virulence and replication and resulted in poor budding of the mutant viruses. Additionally, evidence for the involvement of cellular multivesicular body (MVB) proteins was obtained, since NDV production was inhibited upon expression of dominant-negative versions of the VPS4A-E228Q protein. Together, these results demonstrate that the FPIV motif, especially the residues F and P, within the NDV M protein, plays a critical role in NDV replication and budding, and this budding process likely involves the cellular MVB pathway.