181
Views
2
CrossRef citations to date
0
Altmetric
Research Article

Structural insights of Labeo catla (catla) myxovirus resistance protein,GTP binding recognition and constitutive expression induced with Poly I:C

ORCID Icon, ORCID Icon, ORCID Icon, ORCID Icon, ORCID Icon, ORCID Icon, ORCID Icon & ORCID Icon show all
Pages 3520-3534 | Received 03 Feb 2023, Accepted 08 May 2023, Published online: 25 May 2023

References

  • Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindah, E. (2015). Gromacs: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX, 1–2, 19–25. https://doi.org/10.1016/j.softx.2015.06.001
  • Altschul, S. F., Madden, T. L., Schaffer, A., Zhang, J., Zhang, Z., Miller, W., Lipman, D. J., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., & Lipman, D. J. (1997). Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Research, 25(17), 3389–3402. https://doi.org/10.1093/nar/25.17.3389
  • Avunje, S., & Jung, S.-J. (2017). Poly (I: C) and imiquimod induced immune responses and their effects on the survival of olive flounder (Paralichthys olivaceus) from viral haemorrhagic septicaemia. Fish & Shellfish Immunology, 71, 338–345.
  • Bergan, V., & Robertsen, B. (2004). Characterization of Atlantic halibut (Hippoglossus hippoglossus) Mx protein expression. Developmental and Comparative Immunology, 28(10), 1037–1047. https://doi.org/10.1016/j.dci.2004.03.003
  • Bravo, J., Acosta, F., Padilla, D., Grasso, V., & Real, F. (2011). Mx expression in gilthead sea bream (Sparus aurata L.) in response to poly I: C, bacterial LPS and chromosomal DNA: Preliminary study. Fish & Shellfish Immunology, 31(1), 170–172. https://doi.org/10.1016/j.fsi.2011.04.016
  • Buchan, D. W. A., & Jones, D. T. (2019). The PSIPRED protein analysis workbench: 20 years on. Nucleic Acids Research, 47(W1), W402–W407. https://doi.org/10.1093/nar/gkz297
  • Chomczynski, P., & Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry, 162(1), 156–159. https://doi.org/10.1016/0003-2697(87)90021-2
  • Colovos, C., & Yeates, T. O. (1993). Verification of protein structures: Patterns of nonbonded atomic interactions. Protein Science: A Publication of the Protein Society, 2(9), 1511–1519. https://doi.org/10.1002/pro.5560020916
  • Das, B. K., Roy, P., Rout, A. K., Sahoo, D. R., Panda, S. P., Pattanaik, S., Dehury, B., Behera, B. K., & Mishra, S. S. (2019). Molecular cloning, GTP recognition mechanism and tissue-specific expression profiling of myxovirus resistance (Mx) protein in Labeo rohita (Hamilton) after Poly I: C induction. Scientific Reports, 9(1), 1–19. https://doi.org/10.1038/s41598-019-40323-0
  • Daumke, O., Gao, S., von der Malsburg, A., Haller, O., & Kochs, G. (2010). Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module. Small GTPases, 1(1), 62–64. https://doi.org/10.4161/sgtp.1.1.12989
  • Dehury, B., Behera, S. K., & Mahapatra, N. (2017). Structural dynamics of Casein Kinase I (CKI) from malarial parasite Plasmodium falciparum (Isolate 3D7): Insights from theoretical modelling and molecular simulations. Journal of Molecular Graphics and Modelling, 71, 154–166. https://doi.org/10.1016/j.jmgm.2016.11.012
  • Dehury, B., Tang, N., Blundell, T. L., & Kepp, K. P. (2019). Structure and dynamics of γ-secretase with presenilin 2 compared to presenilin 1. RSC Advances, 9(36), 20901–20916. https://doi.org/10.1039/c9ra02623a
  • Eaton, W. D. (1990). Anti-viral activity in four species of salmonids following exposure to poly inosinic: Cytidylic acid. Diseases of Aquatic Organisms, 9(3), 193–198. https://doi.org/10.3354/dao009193
  • El-Gebali, S., Mistry, J., Bateman, A., Eddy, S. R., Luciani, A., Potter, S. C., Qureshi, M., Richardson, L. J., Salazar, G. A., Smart, A., Sonnhammer, E. L. L., Hirsh, L., Paladin, L., Piovesan, D., Tosatto, S. C. E., & Finn, R. D. (2019). The Pfam protein families database in 2019. Nucleic Acids Research, 47(D1), D427–D432. https://doi.org/10.1093/nar/gky995
  • Fao, R. (2014). FAO yearbook: Fishery and aquaculture statistics 2012. Food and Agriculture Organization of the United Nations.
  • Fribourgh, J. L., Nguyen, H. C., Matreyek, K. A., Alvarez, F. J. D., Summers, B. J., Dewdney, T. G., Aiken, C., Zhang, P., Engelman, A., & Xiong, Y. (2014). Structural insight into HIV-1 restriction by MxB. Cell Host & Microbe, 16(5), 627–638. https://doi.org/10.1016/j.chom.2014.09.021
  • Fröhlich, C., Grabiger, S., Schwefel, D., Faelber, K., Rosenbaum, E., Mears, J., Rocks, O., & Daumke, O. (2013). Structural insights into oligomerization and mitochondrial remodelling of dynamin 1‐like protein. The EMBO Journal, 32(9), 1280–1292. https://doi.org/10.1038/emboj.2013.74
  • Gao, S., Von Der Malsburg, A., Dick, A., Faelber, K., Schröder, G. F., Haller, O., Kochs, G., & Daumke, O. (2011). Structure of myxovirus resistance protein a reveals intra-and intermolecular domain interactions required for the antiviral function. Immunity, 35(4), 514–525. https://doi.org/10.1016/j.immuni.2011.07.012
  • Gao, S., von der Malsburg, A., Paeschke, S., Behlke, J., Haller, O., Kochs, G., & Daumke, O. (2010). Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature, 465(7297), 502–506. https://doi.org/10.1038/nature08972
  • Gordien, E., Rosmorduc, O., Peltekian, C., Garreau, F., Bréhot, C., & Kremsdorf, D. (2001). Inhibition of hepatitis B virus replication by the interferon-inducible MxA protein. Journal of Virology, 75(6), 2684–2691.
  • Goujon, C., Moncorgé, O., Bauby, H., Doyle, T., Ward, C. C., Schaller, T., Hué, S., Barclay, W. S., Schulz, R., & Malim, M. H. (2013). Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection. Nature, 502(7472), 559–562. https://doi.org/10.1038/nature12542
  • Haller, O., Kochs, G., & Weber, F. (2007). Interferon, Mx, and viral countermeasures. Cytokine & Growth Factor Reviews, 18(5–6), 425–433. https://doi.org/10.1016/j.cytogfr.2007.06.001
  • Jensen, I., Albuquerque, A., Sommer, A.-I., & Robertsen, B. (2002). Effect of poly I: C on the expression of Mx proteins and resistance against infection by infectious salmon anaemia virus in Atlantic salmon. Fish & Shellfish Immunology, 13(4), 311–326. https://doi.org/10.1006/fsim.2001.0406
  • Jensen, I., & Robertsen, B. (2002). Effect of double-stranded RNA and interferon on the antiviral activity of Atlantic salmon cells against infectious salmon anemia virus and infectious pancreatic necrosis virus. Fish & Shellfish Immunology, 13(3), 221–241. https://doi.org/10.1006/fsim.2001.0397
  • Kane, M., Yadav, S. S., Bitzegeio, J., Kutluay, S. B., Zang, T., Wilson, S. J., Schoggins, J. W., Rice, C. M., Yamashita, M., Hatziioannou, T., & Bieniasz, P. D. (2013). MX2 is an interferon-induced inhibitor of HIV-1 infection. Nature, 502(7472), 563–566. https://doi.org/10.1038/nature12653
  • Ko, J., Park, H., Heo, L., & Seok, C. (2012). GalaxyWEB server for protein structure prediction and refinement. Nucleic Acids Research, 40(Web Server issue), W294–W297. https://doi.org/10.1093/nar/gks493
  • Kochs, G., Haener, M., Aebi, U., & Haller, O. (2002). Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers. The Journal of Biological Chemistry, 277(16), 14172–14176. https://doi.org/10.1074/jbc.M200244200
  • Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography, 26(2), 283–291. https://doi.org/10.1107/S0021889892009944
  • Lee, S. H., & Vidal, S. M. (2002). Functional diversity of Mx proteins: Variations on a theme of host resistance to infection. Genome Research, 12(4), 527–530. https://doi.org/10.1101/gr.20102
  • Letunic, I., & Bork, P. (2018). 20 years of the SMART protein domain annotation resource. Nucleic Acids Research, 46(D1), D493–D496. https://doi.org/10.1093/nar/gkx922
  • Lindorff‐Larsen, K., Piana, S., Palmo, K., Maragakis, P., Klepeis, J. L., Dror, R. O., & Shaw, D. E. (2010). Improved side‐chain torsion potentials for the Amber ff99SB protein force field. Proteins, 78(8), 1950–1958. https://doi.org/10.1002/prot.22711
  • Liu, Z., Pan, Q., Ding, S., Qian, J., Xu, F., Zhou, J., Cen, S., Guo, F., & Liang, C. (2013). The interferon-inducible MxB protein inhibits HIV-1 infection. Cell Host & Microbe, 14(4), 398–410. https://doi.org/10.1016/j.chom.2013.08.015
  • Lu, S., Wang, J., Chitsaz, F., Derbyshire, M. K., Geer, R. C., Gonzales, N. R., Gwadz, M., Hurwitz, D. I., Marchler, G. H., Song, J. S., Thanki, N., Yamashita, R. A., Yang, M., Zhang, D., Zheng, C., Lanczycki, C. J., & Marchler-Bauer, A. (2020). CDD/SPARCLE: The conserved domain database in 2020. Nucleic Acids Research, 48(D1), D265–D268. https://doi.org/10.1093/nar/gkz991
  • MacKerell, A. D., Bashford, D., Bellott, M., Dunbrack, R. L., Evanseck, J. D., Field, M. J., Fischer, S., Gao, J., Guo, H., Ha, S., Joseph-McCarthy, D., Kuchnir, L., Kuczera, K., Lau, F. T., Mattos, C., Michnick, S., Ngo, T., Nguyen, D. T., Prodhom, B., … Karplus, M. (1998). All-atom empirical potential for molecular modeling and dynamics studies of proteins. The Journal of Physical Chemistry. B, 102(18), 3586–3616. https://doi.org/10.1021/jp973084f
  • Nygaard, R., Husgard, S., Sommer, A.-I., Leong, J.-A C., & Robertsen, B. (2000). Induction of Mx protein by interferon and double-stranded RNA in salmonid cells. Fish & Shellfish Immunology, 10(5), 435–450. https://doi.org/10.1006/fsim.1999.0249
  • Panda, S. P., Soren, D., Nayak, K. K., Roy, P., & Das, B. K. (2021). Poly i: C stimulates, mx transcript and promotes an antiviral state in blood of Labeo catla (Hamilton 1822). Indian Journal of Fisheries, 68(3), 93–99. https://doi.org/10.21077/ijf.2021.68.3.112825-12
  • Ponten, A., Sick, C., Weeber, M., Haller, O., & Kochs, G. (1997). Dominant-negative mutants of human MxA protein: Domains in the carboxy-terminal moiety are important for oligomerization and antiviral activity. Journal of Virology, 71(4), 2591–2599. https://doi.org/10.1128/JVI.71.4.2591-2599.1997
  • Rennie, M. L., McKelvie, S. A., Bulloch, E. M. M., & Kingston, R. L. (2014). Transient dimerization of human MxA promotes GTP hydrolysis, resulting in a mechanical power stroke. Structure (London, England: 1993), 22(10), 1433–1445. https://doi.org/10.1016/j.str.2014.08.015
  • Rout, A. K., Dehury, B., Maharana, J., Nayak, C., Baisvar, V. S., Behera, B. K., & Das, B. K. (2018). Deep insights into the mode of ATP-binding mechanism in Zebrafish cyclin-dependent protein kinase-like 1 (zCDKL1): A molecular dynamics approach. Journal of Molecular Graphics and Modelling, 81, 175–183. https://doi.org/10.1016/j.jmgm.2018.02.002
  • Rout, A. K., Acharya, V., Maharana, D., Dehury, B., Udgata, S. R., Jena, R., Behera, B., Parida, P. K., & Behera, B. K. (2021). Insights into structure and dynamics of extracellular domain of Toll-like receptor 5 in Cirrhinus mrigala (mrigala): A molecular dynamics simulation approach. Plos One, 16(1), e0245358. https://doi.org/10.1371/journal.pone.0245358
  • Rout, A. K., Paramanik, S., Dehury, B., Acharya, V., Swain, H. S., Pradhan, S. K., Behera, B., Pati, S. K., Behera, B. K., & Das, B. K. (2020). Elucidating the molecular interaction of Zebrafish (Danio rerio) peptidoglycan recognition protein 2 with diaminopimelic acid and lysine type peptidoglycans using in silico approaches. Journal of Biomolecular Structure & Dynamics, 38(12), 3687–3699. https://doi.org/10.1080/07391102.2019.1666742
  • Roy, P., Rout, A. K., Maharana, J., Sahoo, D. R., Panda, S. P., Pal, A., Nayak, K. K., Behera, B. K., & Das, B. K. (2019). Molecular characterization, constitutive expression and GTP binding mechanism of Cirrhinus mrigala (Hamilton, 1822) Myxovirus resistance (Mx) protein. International Journal of Biological Macromolecules, 136, 1258–1272. https://doi.org/10.1016/j.ijbiomac.2019.06.161
  • Sadler, A. J., & Williams, B. R. G. (2008). Interferon-inducible antiviral effectors. Nature Reviews. Immunology, 8(7), 559–568. https://doi.org/10.1038/nri2314
  • Staeheli, P., Pitossi, F., & Pavlovic, J. (1993). Mx proteins: GTPases with antiviral activity. Trends in Cell Biology, 3(8), 268–272. https://doi.org/10.1016/0962-8924(93)90055-6
  • Su, J., Yang, C., Zhu, Z., Wang, Y., Jang, S., & Liao, L. (2009). Enhanced grass carp reovirus resistance of Mx-transgenic rare minnow (Gobiocypris rarus). Fish & Shellfish Immunology, 26(6), 828–835. https://doi.org/10.1016/j.fsi.2008.12.007
  • Theofilopoulos, A. N., Baccala, R., Beutler, B., & Kono, D. H. (2005). Type I interferons (α/β) in immunity and autoimmunity. Annual Review of Immunology, 23, 307–336. https://doi.org/10.1146/annurev.immunol.23.021704.115843
  • Wallner, B., & Elofsson, A. (2003). Can correct protein models be identified? Protein Science: A Publication of the Protein Society, 12(5), 1073–1086. https://doi.org/10.1110/ps.0236803
  • Wang, Z., Chai, K., Liu, Q., Yi, D.-R., Pan, Q., Huang, Y., Tan, J., Qiao, W., Guo, F., & Cen, S. (2020). HIV-1 resists MxB inhibition of viral Rev protein. Emerging Microbes & Infections, 9(1), 2030–2045.
  • Wang, Z., Xu, J., Feng, J., Wu, K., Chen, K., Jia, Z., Zhu, X., Huang, W., Zhao, X., Liu, Q., Wang, B., Chen, X., Wang, J., & Zou, J. (2022). Structural and functional analyses of type I IFNa Shed light into its interaction with multiple receptors in fish. Frontiers in Immunology, 13, 862764. https://doi.org/10.3389/fimmu.2022.862764
  • Webb, B., & Sali, A. (2017). Protein Structure Modeling with MODELLER (pp. 39–54). Humana Press. https://doi.org/10.1007/978-1-4939-7231-9_4
  • Wiederstein, M., & Sippl, M. J. (2007). ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Research, 35, W407–W410. https://doi.org/10.1093/nar/gkm290
  • Workenhe, S. T., Rise, M. L., Kibenge, M. J. T., & Kibenge, F. S. B. (2010). The fight between the teleost fish immune response and aquatic viruses. Molecular Immunology, 47(16), 2525–2536. https://doi.org/10.1016/j.molimm.2010.06.009
  • Zou, J., Bird, S., & Secombes, C. (2010). Antiviral sensing in teleost fish. Current Pharmaceutical Design, 16(38), 4185–4193. https://doi.org/10.2174/138161210794519093

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.