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. 2017 Oct 25;7:14053. doi: 10.1038/s41598-017-13784-4

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© The Author(s) 2017

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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A proposed model. In the absence of UAP56, monomeric NP first binds to RNA, and the additional monomers randomly bind to the monomeric NP on NP-RNA complex, slowly. The dimerized UAP56 proteins bind to trimeric NP, respectively. UAP56 stimulates the transfer of NP to viral RNA by facilitating trimeric NP formation for the structural integrity of NP-RNA complex competent for viral RNA synthesis.