Preparation and Crystallization of Picornain 3C of Rhinovirus A28

A. E. Tishin; Тишин А. Е.; A. V. Gladysheva; Гладышева А. В.; L. A. Pyatavina; Пятавина Л. А.; S. E. Olkin; Олькин С. Е.; A. A. Gladysheva; Гладышева А. А.; I. R. Imatdionov; Иматдинов И. Р.; A. V. Vlaskina; Власкина А. В.; A. Yu. Nikolaeva; Николаева А. Ю.; V. R. Samygina; Самыгина В. Р.; A. P. Agafonov; Агафонов А. П.

doi:10.31857/S0023476123600313

Preparation and Crystallization of Picornain 3C of Rhinovirus A28

Authors: Tishin A.E.¹, Gladysheva A.V.², Pyatavina L.A.¹^,3, Olkin S.E.¹, Gladysheva A.A.²^,4, Imatdionov I.R.¹, Vlaskina A.V.⁵, Nikolaeva A.Y.⁵, Samygina V.R.⁶^,7, Agafonov A.P.¹
Affiliations:
1. State Research Center of Virology and Biotechnology “Vector,” Rospotrebnadzor, 630559, Koltsovo, Novosibirsk oblast, Russia
2. State Scientific Center of Virology and Biotechnology «Vector»
3. Novosibirsk National Research State University, 630090, Novosibirsk, Russia
4. Novosibirsk National Research State University
5. National Research Centre “Kurchatov Institute”, 123098, Moscow, Russia
6. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
7. Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia
Issue: Vol 68, No 6 (2023)
Pages: 926-933
Section: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://rjmseer.com/0023-4761/article/view/673291
DOI: https://doi.org/10.31857/S0023476123600313
EDN: https://elibrary.ru/HZHBKY
ID: 673291

Cite item

Full Text

Open Access
Restricted Access

Access granted
Restricted Access

Subscription Access

Abstract
About the authors
References
Supplementary files
Statistics

Abstract

Human rhinovirus picornain 3C is a high-value commercial cysteine protease, which is widely used to remove affinity tags and fusion proteins during the purification of the target proteins. A variant of rhinovirus A28 picornain 3C produced in this study is not annotated in the NCBI databases, shares 79% sequence identity in the PDB, and was not previously used in the protein engineering. A protocol was developed for the isolation and purification of the protein to use it in structural studies. The initial crystallization conditions were found. The determination and analysis of the structure of rhinovirus A28 picornain 3C will provide new possibilities for performing basic research on the evolution of proteolytic enzymes and for the design of the optimal variant of this protease.

About the authors

A. E. Tishin

State Research Center of Virology and Biotechnology “Vector,” Rospotrebnadzor, 630559, Koltsovo, Novosibirsk oblast, Russia

Email: gladysheva_av@vector.nsc.ru
Россия, Кольцово

A. V. Gladysheva

State Scientific Center of Virology and Biotechnology «Vector»

Email: gladysheva_av@vector.nsc.ru
ORCID iD: 0000-0002-7396-3954
SPIN-code: 5214-3421
Scopus Author ID: 57194590629

Postgraduate student, Juniour Researcher, Department of Molecular Virology for Flaviviruses and Viral Hepatitis

Russian Federation, 630559, Novosibirsk region, Koltsovo

L. A. Pyatavina

State Research Center of Virology and Biotechnology “Vector,” Rospotrebnadzor, 630559, Koltsovo, Novosibirsk oblast, Russia; Novosibirsk National Research State University, 630090, Novosibirsk, Russia

Email: gladysheva_av@vector.nsc.ru
Россия, Кольцово; Россия, Новосибирск

S. E. Olkin

State Research Center of Virology and Biotechnology “Vector,” Rospotrebnadzor, 630559, Koltsovo, Novosibirsk oblast, Russia

Email: gladysheva_av@vector.nsc.ru
Россия, Кольцово

A. A. Gladysheva

State Scientific Center of Virology and Biotechnology «Vector»; Novosibirsk National Research State University

Email: gladysheva_aa@vector.nsc.ru
ORCID iD: 0000-0002-9490-1939

Graduate student, Assistant, Department of Molecular Virology for Flaviviruses and Viral Hepatitis

Russian Federation, 630559, Novosibirsk region, Koltsovo; 630090, Novosibirsk

References

Bizot E., Bousquet A., Charpié M. et al. // Front. Pediatr. 2021. V. 22. P. 643219. https://doi.org/10.3389/fped.2021.643219
Ljubin-Sternak S., Meštrović T. // Viruses. 2023. V. 15 (4). P. 825. https://doi.org/10.3390/v15040825
Flather D., Nguyen J.H.C., Semler B.L., Gershon P.D. // PLoS Pathog. 2018. V. 14 (8). P. e1007277. https://doi.org/10.1371/journal.ppat.1007277
Jensen L.M., Walker E.J., Jans D.A., Ghildyal R. // Methods Mol. Biol. 2015. V. 1221. P. 129. https://doi.org/10.1007/978-1-4939-1571-2_10
Matthews D.A., Dragovich P.S., Webber S.E. et al. // Proc. Natl. Acad. Sci. USA. 1999. V. 96 (20). P. 11000. https://doi.org/10.1073/pnas.96.20.11000
Bjorndahl T.C., Andrew L.C., Semenchenko V., Wishart D.S. // Biochemistry. 2007. V. 46 (45). P. 12945–58. https://doi.org/10.1021/bi7010866
Cui S., Wang J., Fan T. et al. // J. Mol. Biol. 2011. V. 408 (3). P. 449. https://doi.org/10.1016/j.jmb.2011.03.007
Yuan S., Fan K., Chen Z. et al. // Virol. Sin. 2020. V. 35 (4). P. 445. https://doi.org/10.1007/s12250-020-00196-4
Sun D., Chen S., Cheng A., Wang M. // Viruses. 2016. V. 8 (3) P. 82. https://doi.org/10.3390/v8030082
Ullah R., Shah M.A., Tufail S. et al. // PLoS One. 2016. V. 11 (4) P. e0153436. https://doi.org/10.1371/journal.pone.0153436
Wanga Q.M., Chen S.H. // Curr. Protein Pept. Sci. 2007. V. 8 (1). P. 19. https://doi.org/10.2174/138920307779941523
Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596 (7873). P. 583. https://doi.org/10.1038/s41586-021-03819-2
de Marco A. // Nat Protoc. 2006. V. 1 (3). P. 1538. https://doi.org/10.1038/nprot.2006.289
Brunelle J.L., Green R. // Methods Enzymol. 2014. V. 541. P. 151. https://doi.org/10.1016/B978-0-12-420119-4.00012-4
Akaberi D., Båhlström A., Chinthakindi P.K. // Antiviral Res. 2021. V. 190. P. 105074. https://doi.org/10.1016/j.antiviral.2021.105074
Fan X., Li X., Zhou Y. et al. // ACS Chem Biol. 2020. V. 15 (1). P. 63. https://doi.org/10.1021/acschembio.9b00539
Timofeev V., Samygina V. // Crystals. 2023. V. 13 P. 71. https://doi.org/10.3390/cryst13010071