The nanoscale organization of Nipah virus matrix protein revealed by super-resolution microscopy

被引:2
作者
Liu, Qian T. [1 ,2 ]
Wang, Qian [3 ]
Zhang, Youchang [1 ,2 ]
Kliemke, Vicky [3 ]
Liu, Qian [3 ]
Chou, Keng C. [1 ,2 ]
机构
[1] Univ British Columbia, Dept Chem, Vancouver, BC, Canada
[2] Univ British Columbia, Life Sci Inst, Vancouver, BC, Canada
[3] McGill Univ, Inst Parasitol, Ste Anne De Bellevue, PQ, Canada
基金
加拿大自然科学与工程研究理事会;
关键词
LOCALIZATION;
D O I
10.1016/j.bpj.2022.05.026
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The matrix proteins (M) of many enveloped RNA viruses mediate virus assembly and budding. However, it remains poorly understood how M are involved in virus budding and how they interact with envelope proteins. Here, we show that the expression level of Nipah (NiV) M in particles produced by the host cells deviates from a gamma distribution and does not reflect that of the host cells, indicating assembly of the NiV-M in the process. Our data reveal that NiV-M affects the circularity of the particles while the NiV envelope proteins do not. The organization of NiV envelope proteins on the membrane of the particles is similar to those that do not express NiV-M, suggesting that NiV-M does not directly interact with the envelope proteins during assembly and budding.
引用
收藏
页码:2290 / 2296
页数:7
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