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

Biophys J. 2022 Jun 21;121(12):2290-2296. doi: 10.1016/j.bpj.2022.05.026. Epub 2022 May 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Microscopy
  • Nipah Virus* / genetics
  • Viral Envelope Proteins / metabolism
  • Viral Matrix Proteins / metabolism
  • Virion / metabolism
  • Virus Assembly

Substances

  • Viral Envelope Proteins
  • Viral Matrix Proteins