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. 2022 Oct 18;12:16952. doi: 10.1038/s41598-022-20970-6

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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 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/.

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Generation of CRFK cells expressing chimeric TRIM5 proteins. (a) Alignment of bovine TRIM5 and human TRIM5α. The protein sequences of bovine TRIM5 and human TRIM5α were aligned using MEGA X. The domains of TRIM5 were indicated in yellow (RING domain), green (B-box domain), blue (Coiled-coil domain), and pink (SPRY domain). (b) Schematic representation of chimeric TRIM5 molecules generated in this study. The chimera TRIM5 molecule “HuBo” consists of the RING, B-box, and Coiled-coil (RBCC) domains of human TRIM5α and the SPRY domain of bovine TRIM5. The chimeric TRIM5 molecule “BoHu” consists of the RBCC domain of bovine TRIM5 and SPRY domain of human TRIM5α. A truncated version of bovine TRIM5 lacking the SPRY domain was termed “delSPRY.” (c) Expression of each HA-tagged TRIM5 protein in CRFK cells was determined using Western blotting. The cellular lysate of unmodified CRFK cells was used as a negative control (empty).