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. 2021 Oct 27;12:6197. doi: 10.1038/s41467-021-26499-y

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© The Author(s) 2021

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. 1 — a Structure and design of the NDV-HXP-S genome. The ectodomain of the spike was connected to the transmembrane domain and cytoplasmic tail (TM/CT) of the F protein (blue: the ectodomain of the spike; black: NDV components; gray: NDV F gene with L289A mutation). The original polybasic cleavage site was removed by mutating RRAR to A. The HexaPro (F817P, A892P, A899P, A942P, K986P, and V987P) stabilizing mutations were introduced. The sequence was codon-optimized for mammalian host expression. b Protein staining of NDV-HXP-S. WT NDV as well as NDV-HXP-S were partially purified from the allantoic fluid through a sucrose cushion and resuspended in PBS. In all, 5 µg (1) and 10 µg (2) of the WT NDV, as well as 10 µg of NDV-HXP-S were resolved on 4–20% SDS–PAGE. The viral proteins were visualized by Coomassie Blue staining (L, S[Blue], HN, N, P, and M). A representative image out of more than three independent experiments is shown.