Regulation of Marburg virus (MARV) budding by Nedd4.1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40.
Regulation of Marburg virus (MARV) budding by Nedd4.1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40.
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Nedd4.1 对马尔堡病毒 (MARV) 出芽的调节：Nedd4.1 的不同 WW 结构域对于与 MARV 和埃博拉病毒 VP40 的结合至关重要。
DOI：
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发表时间：
2010
影响因子：
3.8
通讯作者：
Jiro Yasuda
中科院分区：
文献类型：
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作者：
Shuzo Urata;Jiro Yasuda
马尔堡病毒（MARV）的VP 40基质蛋白已被证明是MARV出芽的驱动力，在此过程中，VP 40的PPPY L结构域基序起着关键作用。在这里，我们报告Vps 4 B和Nedd4.1在MARV VP 40介导的出芽中起关键作用。我们发现Nedd4.1 HECT结构域的未鉴定的活性，沿着其E3泛素连接酶活性，可能是MARV出芽所必需的。此外，我们发现Nedd4.1的第一个WW结构域WW 1对于与MARV VP 40结合至关重要，表明MARV VP 40和埃博拉病毒VP 40被Nedd4.1的不同WW结构域识别。这是第一次报告表明，含有PPxY的病毒L-结构域具有特异性结合WW结构域。我们的发现为MARV出芽提供了新的见解，这可能有助于开发新的抗MARV治疗策略。
The VP40 matrix protein of Marburg virus (MARV) has been shown to be the driving force behind MARV budding, a process in which the PPPY L-domain motif of VP40 plays a critical role. Here, we report that Vps4B and Nedd4.1 play critical roles in MARV VP40-mediated budding. We showed that unidentified activities of the Nedd4.1 HECT domain, along with its E3 ubiquitin ligase activity, may be required for MARV budding. Moreover, we showed that the first WW domain of Nedd4.1, WW1, is critical for binding to MARV VP40, indicating that MARV VP40 and Ebola virus VP40 are recognized by a different WW domain of Nedd4.1. This is the first report showing that the viral L-domains containing PPxY have specificities for binding to WW domains. Our findings provide new insights into MARV budding, which may contribute to the development of novel anti-MARV therapeutic strategies.
DOI：
10.1073/pnas.88.8.3195
发表时间：
1991-04-01
影响因子：
11.1
作者：
GOTTLINGER, HG;DORFMAN, T;HASELTINE, WA
通讯作者：
HASELTINE, WA