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

ABSTRACT: 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.

SUBMITTER: Liu QT

PROVIDER: S-EPMC9279348 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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

Liu Qian T QT Wang Qian Q Zhang Youchang Y Kliemke Vicky V Liu Qian Q Chou Keng C KC

Biophysical journal 20220525 12

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 partic ...[more]

PMID: 35614854

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