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Morphology of Nipah virus-like particles studied by super-resolution microscopy Liu, Qian


Morphological studies are pivotal for understanding arrangements and properties of viral proteins. Virus-like particles (VLPs) are particles that contain partial or complete viral proteins without the existence of viral genomes. For highly contagious and fatal viruses, such as the Nipah virus (NiV), VLPs are widely-used research surrogates to study functions of viral proteins and structural details of virions. In this study, direct stochastic optical reconstruction microscopy (dSTORM) with a precision of 10 nm was used to characterize NiV VLPs. Examining NiV matrix proteins (NiV-M) clusters in host cells showed that NiV-M form larger clusters at the plasma membrane compared to those in the cytosol, indicating NiV-M assemble at the plasma membrane of host cells. NiV VLPs are pleomorphic under dSTORM. Statistical studies of over 3,000 VLPs showed that NiV-M tend to affect the shape of VLPs, producing a more non-spherical shape. On the other hand, the attachment proteins (NiV-G) and the fusion proteins (NiV-F) have no significant impacts on the shape of VLPs. The protein copy number of NiV-M in each NiV VLP was estimated by comparing the fluorescence intensity of GFP molecules in a VLP to that of single GFP molecules. Quantitative analysis of over 500 VLPs showed that a majority of NiV VLPs have less than 400 copies of NiV-M.

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