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. 2022 Aug 24;19:19. doi: 10.1186/s12977-022-00598-0

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Analysis of the binding of a recombinant chimeric ALV-A/K gp85 protein for the Tva receptor. a Homology comparison between ALV-A RSA and ALV-K GDFX0602 gp85 protein sequences; b technology roadmap of co-IP and competitive blocking tests; c, d binding of recombinant chimeric fragments s1–s5 of the Agp85 protein to the Tva receptor and relative grey values; e, f binding of recombinant chimeric fragments s1–s5 of the Agp85 protein to the Tva receptor and relative grey values; g Competitive blocking of a recombinant chimeric ALV-A/K gp85 protein. Three independent experiments were performed, and the data are shown as the mean ± SD of triplicate samples from a representative experiment. Statistical analysis (two-way analysis of variance) was performed using GraphPad Prism 7; *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001