Identification of Amino Acids in Marburg Virus VP40 That Are Important for Virus-Like Particle Budding
Identification of Amino Acids in Marburg Virus VP40 That Are Important for Virus-Like Particle Budding
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DOI：
10.1093/infdis/jir309
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发表时间：
2011-11-01
影响因子：
6.4
通讯作者：
Kawaoka, Yoshihiro
中科院分区：
文献类型：
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作者：
Makino, Akiko;Yamayoshi, Seiya;Kawaoka, Yoshihiro
马尔堡病毒的基质蛋白VP 40促进病毒样颗粒（VLP）的形成和释放。马尔堡病毒VP 40通过其L结构域基序与细胞Tsg 101相互作用;然而，该基序的突变不影响VLP出芽或VP 40在多泡体（MVB）中的积累，多泡体是病毒颗粒形成的平台。为了鉴定马尔堡病毒VP 40中对VLP出芽重要的区域，我们检测了VP 40 N-和C-末端的缺失突变体和丙氨酸扫描突变体，以了解它们参与VLP出芽的情况。在Ile 39和Thr 40处的丙氨酸置换突变体的存在下未检测到VLP，并且Asn 297处的丙氨酸突变体的VLP出芽水平降低。此外，这些突变体在MVB中不积累。我们的研究结果表明，一种新的宿主因子参与了VLP出芽和VP 40向MVB的转运。
The matrix protein VP40 of Marburg virus promotes the formation and release of virus-like particles (VLPs). Marburg virus VP40 interacts with cellular Tsg101 via its L domain motif; however, mutation of this motif does not affect VLP budding or the accumulation of VP40 in multivesicular bodies (MVBs), which are platforms for virus particle formation. To identify regions of Marburg virus VP40 that are important for VLP budding, we examined deletion mutants and alanine-scanning mutants at the N- and C-terminus of VP40 for their involvement in VLP budding. VLPs were not detected in the presence of alanine-replacement mutants at Ile39 and Thr40, and the level of VLP budding for the alanine mutant at Asn297 was decreased. Moreover, these mutants did not accumulate in MVBs. Our results suggest the involvement of a novel host factor(s) in VLP budding and VP40 transport to MVBs.