Search for Potential Epitopes in the Envelope Protein of the African Swine Fever Virus

I. A. Kolesnikov; Колесников И. А.; V. I. Timofeev; Тимофеев В. И.; A. V. Ermakov; Ермаков А. В.; A. S. Ivanovsky; Ивановский А. С.; Yu. A. Dyakova; Дьякова Ю. А.; Yu. V. Pisarevsky; Писаревский Ю. В.; M. V. Kovalchuk; Ковальчук М. В.

doi:10.31857/S0023476123600179

Search for Potential Epitopes in the Envelope Protein of the African Swine Fever Virus

作者: Kolesnikov I.A.¹, Timofeev V.I.¹^,2, Ermakov A.V.¹, Ivanovsky A.S.², Dyakova Y.A.¹, Pisarevsky Y.V.²^,1, Kovalchuk M.V.¹^,2
隶属关系:
1. National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia
2. Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia
期: 卷 68, 编号 6 (2023)
页面: 971-978
栏目: КРИСТАЛЛОГРАФИЯ В БИОЛОГИИ И МЕДИЦИНЕ
URL: https://journal-vniispk.ru/0023-4761/article/view/231848
DOI: https://doi.org/10.31857/S0023476123600179
EDN: https://elibrary.ru/HJNXSQ
ID: 231848

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详细

The spatial structure of the envelope protein of African swine fever (ASF) virus is modeled; its topology relative to the cell membrane is calculated; the B- and T-cell epitopes are predicted for this protein; and their immunogenecity, allergenicity, and toxicity are estimated. The variability of protein amino acids and the conservativity of the found epitopes are studied. It is shown that a new peptide vaccine against ASF can be developed based on the found epitopes.

作者简介

I. Kolesnikov

National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва

V. Timofeev

National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia; Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва; Россия, Москва

A. Ermakov

National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва

A. Ivanovsky

Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва

Yu. Dyakova

National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва

Yu. Pisarevsky

Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia; National Research Centre “Kurchatov Institute”, 123182, Moscow, Russia

Email: a.1wanowskiy@gmail.com
Россия, Москва; Россия, Москва

M. Kovalchuk

编辑信件的主要联系方式.
Email: a.1wanowskiy@gmail.com
Россия, Москва; Россия, Москва

参考

Mettenleiter T.C., Sobrino F. // Animal Viruses: Molecular Biology. 2008. V. 14. P. 5. https://doi.org/10.3201/eid1405.080077
Anderson E.C., Hutchings G.H., Mukarati N., Wilkinson P.J. // Veterinary Microbiology. 1998. V. 62 (1). P. 1. https://doi.org/10.1016/S0378-1135(98)00187-4
Khomenko S., Beltrán-Alcrudo D., Rozstalnyy A. et al. // Empress Watch. 2013. V. 28. P. 1
Mazur-Panasiuk N., Woźniakowski G., Niemczuk K. // Sci Rep. 2019. V. 9. № 4556. https://doi.org/10.1038/s41598-018-36823-0
Colson P., De Lamballerie X., Yutin N. et al. // Arch Virol. 2013. V. 158. P. 2517. https://doi.org/10.1007/s00705-013-1768-6
Dixon L.K., Chapman D.A., Netherton C.L., Upton C. // Virus Res. 2013. V. 173 (1). P. 3.
Netherton C.L., Wileman T.E. // Virus Res. 2013. V. 173 (1). P. 76. https://doi.org/10.1016/j.virusres.2012.12.014
Gaudreault N.N., Madden D.W., Wilson W.C. et al. // Front. Vet. Sci. 2020. V. 7. 215. https://doi.org/10.3389/fvets.2020.00215
Rodríguez J.M., Yáñez R.J., Almazán F. et al. // J. Virol. 1993. V. 67. № 9. P. 5312. https://doi.org/10.1128/jvi.67.9.5312-5320.1993
Ruiz-Gonzalvo F., Rodríguez F., Escribano J.M. // Virology. 1996. V. 218 (1). P. 285. https://doi.org/10.1006/viro.1996.0193
Abass O.A., Timofeev V.I., Sarkar B. et al. // J. Biomol. Struct. Dynamics. 2021. V. 40 (16). P. 7283. https://doi.org/10.1080/07391102.2021.1896387
Araf Y., Moin A.T., Timofeev V.I. et al. // Front. Immunol. 2022. V. 13. 863234. https://doi.org/10.3389/fimmu.2022.863234
Q89501. https://nbgi.ru/
Altschul S.F., Gish W., Miller W. et al. // J. Mol. Biol. 1990. V. 215 (3). P. 403.
Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596. P. 583. https://doi.org/10.1038/s41586-021-03819-2
Jeppe H., Trigos K.D., Pedersen M.D. et al. // bioRxiv. 2022. https://doi.org/10.1101/2022.04.08.487609
Larsen M.V., Lundegaard C., Lamberth K. et al. // BMC Bioinformatics. 2007. V. 8. 424. https://doi.org/10.1186/1471-2105-8-424
http://tools.iedb.org/ellipro/
Ponomarenko J., Bui HH., Li W. et al. // BMC Bioinformatics. 2008. V. 9. 514. https://doi.org/10.1186/1471-2105-9-514
Dimitrov I., Bangov I., Flower D.R. et al. // J. Mol. Model. 2014. V. 20 (5). 2278. https://doi.org/10.1007/s00894-014-2278-5
Gupta S., Kapoor P., Chaudhary K. et al. // PLoS ONE. 2020. V. 8 (9). e73957. https://doi.org/10.1371/journal.pone.0073957
Doytchinova I.A., Flower D.R. // BMC Bioinformatics. 2007. V. 8. 4. https://doi.org/10.1186/1471-2105-8-4
Bui H., Sidney J.H., Li W. et al. // BMC Bioinformatics. 2007. V. 8 (1). 361. https://doi.org/10.1186/1471-2105-8-361
Larsen M.V., Lundegaard C., Lamberth K. et al. // BMC Bioinformatics. 2007. V. 8. 424. https://doi.org/10.1186/1471-2105-8-424
Choo S.Y. // Yonsei Med J. 2007. V. 48 (1). P. 11. https://doi.org/10.3349/ymj.2007.48.1.11
Potocnakova L., Bhide M., Pulzova L.B. // J. Immunol. Res. 2016. https://doi.org/10.1155/2016/6760830