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. 2022 Aug 5;13:4399. doi: 10.1038/s41467-022-32019-3

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Differential interference contrast (DIC) and fluorescence images of liquid-liquid phase separation (LLPS) of N protein (TAMRA-labeled) with or without M protein (FITC-labeled). The experiment was repeated three times with similar results. b FLAG tag pull-down assay using recombinant M protein (FLAG-tagged) and N protein (no tag) in the absence or presence of poly(I:C). The experiment was repeated twice with similar results. Source data are provided as a Source Data file. c StrepII tag pull-down assay using recombinant N protein (StrepII-tagged) and M protein (FLAG-tagged) in the absence or presence of RNAs of different sizes. RNA-H and RNA-L indicate yeast RNA with molecular weights >30 kDa and 3–30 kDa, respectively. The experiment was repeated twice with similar results. d Electrostatic surface potentials of the intravirion side of the M protein dimer (long form). Positively charged residues to which the mutations were introduced in e are shown using stick representations and labeled. e Co-immunoprecipitation assay of wild-type (WT) or mutant M proteins with N protein in HEK293T cells. The experiment was repeated three times with similar results. Source data are provided as a Source Data file. f Model of M protein-triggered SARS-CoV-2 assembly M protein in the endoplasmic reticulum–Golgi intermediate compartment (ERGIC) forms dimers in two different conformations that assemble into higher-order oligomers to induce membrane curvature. M protein recruits N and genomic RNA in a cooperative manner. S and E proteins are also recruited to the budding site via an unknown mechanism. Source data are provided as a Source Data file.