Citation: Zhiyun Yin, Fuli Ren, Min Zhou, Shengyao Chen, Yali Deng, Sijing Hu, Fei Deng, Shu Shen, Junming Shi. Roles of the functional domains and conserved residues of the severe fever with thrombocytopenia syndrome virus L protein provide insights into the viral RNA transcription/replication mechanism .VIROLOGICA SINICA, 2022, 37(6) : 946-949.  http://dx.doi.org/10.1016/j.virs.2022.08.009

Roles of the functional domains and conserved residues of the severe fever with thrombocytopenia syndrome virus L protein provide insights into the viral RNA transcription/replication mechanism

  • Corresponding author: Shu Shen, shenshu@wh.iov.cn
    Junming Shi, sjm@wh.iov.cn
  • Received Date: 17 June 2022
    Accepted Date: 26 August 2022
    Available online: 03 September 2022
  • Highlights
    1. All the domains of SFTSV-L protein were required for its function in viral RNA replication/transcription.
    2. The influence of twelve conserved residues speculated basing on the atomic model of SFTSV-L were evaluated using mini-genome system, and nine of which showed significant roles in the function of L protein.
    3. Nine key residues of SFTSV-L were strictly conserved among emerging related phleboviruses, suggesting L protein may be a promising broad spectrum drug target of phleboviruses.

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    3. Cusack, S., Rosenthal, M., 2021. Errors in the deposited SFTSV L protein structure. Nat Microbiol 6, 549–550.

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    6. Kim, K.H., Yi, J., Kim, G., Choi, S.J., Jun, K.I., Kim, N.H., Choe, P.G., Kim, N.J., Lee, J.K., Oh, M.D., 2013. Severe fever with thrombocytopenia syndrome, South Korea, 2012. Emerg. Infect. Dis. 19, 1892–1894.

    7. Mourya, D.T., Yadav, Pd, Fau - Basu, A., Basu A Fau - Shete, A., Shete, A., Fau - Patil, D.Y., Patil, Dy, Fau - Zawar, D., Zawar D Fau - Majumdar, T.D., Majumdar, Td, Fau -Kokate, P., Kokate Fau - Sarkale, P., Sarkale, P., Fau - Raut, C.G., Raut, Cg, Fau -Jadhav, S.M., Jadhav, S.M., 2014. Malsoor virus, a novel bat phlebovirus, is closely related to severe fever with thrombocytopenia syndrome virus and heartland virus.J. Virol. 88, 3605–3609.

    8. Noda, K., Tsuda, Y., Kozawa, F., Igarashi, M., Shimizu, K., Arikawa, J., Yoshimatsu, K., 2020. The polarity of an amino acid at position 1891 of severe fever with thrombocytopenia syndrome virus L protein is critical for the polymerase activity. Viruses 13, 33.

    9. Pflug, A., Guilligay, D., Reich, S., Cusack, S., 2014. Structure of influenza A polymerase bound to the viral RNA promoter. Nature 516, 355–360.

    10. Sanchez, A.B., de la Torre, J.C., 2005. Genetic and biochemical evidence for an oligomeric structure of the functional L polymerase of the prototypic arenavirus lymphocytic choriomeningitis virus. J. Virol. 79, 7262–7268.

    11. Shen, S., Duan, X., Wang, B., Zhu, L., Zhang, Y., Zhang, J., Wang, J., Luo, T., Kou, C., Liu, D., Lv, C., Zhang, L., Chang, C., Su, Z., Tang, S., Qiao, J., Moming, A., Wang, C., Abudurexiti, A., Wang, H., Hu, Z., Zhang, Y., Sun, S., Deng, F., 2018. A novel tickborne phlebovirus, closely related to severe fever with thrombocytopenia syndrome virus and Heartland virus, is a potential pathogen. Emerg. Microb. Infect. 7, 95.

    12. Vogel, D., Thorkelsson, S.R., Quemin, E.R.J., Meier, K., Kouba, T., Gogrefe, N., Busch, C., Reindl, S., Günther, S., Cusack, S., Grünewald, K., Rosenthal, M., 2020. Structural and functional characterization of the severe fever with thrombocytopenia syndrome virus L protein. Nucleic Acids Res. 48, 5749–5765.

    13. Wang, P., Liu, L., Liu, A., Yan, L., He, Y., Shen, S., Hu, M., Guo, Y., Liu, H., Liu, C., Lu, Y., Wang, P., Deng, F., Rao, Z., Lou, Z., 2020. Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation. Nat Microbiol 5, 864–871.

    14. Wang, P., Liu, L., Liu, A., Yan, L., He, Y., Shen, S., Hu, M., Guo, Y., Liu, H., Liu, C., Lu, Y., Wang, P., Deng, F., Rao, Z., Lou, Z., 2021. Author Correction: structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation. Nat Microbiol 6, 697–698.

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    Roles of the functional domains and conserved residues of the severe fever with thrombocytopenia syndrome virus L protein provide insights into the viral RNA transcription/replication mechanism

      Corresponding author: Shu Shen, shenshu@wh.iov.cn
      Corresponding author: Junming Shi, sjm@wh.iov.cn
    • a National Virus Resource Center, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, 430071, China;
    • b Academic Affairs Office of Cangzhou Jiaotong University, Cangzhou, 061199, China;
    • c Center for Translational Medicine, Jinyintan Hospital, Wuhan, 430023, China

    Abstract: Highlights
    1. All the domains of SFTSV-L protein were required for its function in viral RNA replication/transcription.
    2. The influence of twelve conserved residues speculated basing on the atomic model of SFTSV-L were evaluated using mini-genome system, and nine of which showed significant roles in the function of L protein.
    3. Nine key residues of SFTSV-L were strictly conserved among emerging related phleboviruses, suggesting L protein may be a promising broad spectrum drug target of phleboviruses.

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