Department of Microbiology and Infectious Diseases, Division of Zoonosis, Graduate School of Medicine, Kobe University, Japan.
J Infect Dis. 2011 Nov;204 Suppl 3(Suppl 3):S871-7. doi: 10.1093/infdis/jir309.
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.
马尔堡病毒的基质蛋白 VP40 促进病毒样颗粒 (VLPs) 的形成和释放。马尔堡病毒 VP40 通过其 L 结构域基序与细胞 Tsg101 相互作用；然而，该基序的突变并不影响 VLP 的出芽或 VP40 在多泡体 (MVBs) 中的积累，MVBs 是病毒颗粒形成的平台。为了确定马尔堡病毒 VP40 中对 VLP 出芽重要的区域，我们研究了 VP40 的 N 和 C 末端缺失突变体和丙氨酸扫描突变体，以确定它们是否参与 VLP 出芽。在存在 Ile39 和 Thr40 丙氨酸取代突变体的情况下，未检测到 VLPs，并且 Asn297 丙氨酸突变体的 VLP 出芽水平降低。此外，这些突变体不会在 MVBs 中积累。我们的结果表明，在 VLP 出芽和 VP40 向 MVBs 的运输中涉及一种新的宿主因子。
