- PII
- 10.31857/S0023476123600179-1
- DOI
- 10.31857/S0023476123600179
- Publication type
- Status
- Published
- Authors
- Volume/ Edition
- Volume 68 / Issue number 6
- Pages
- 971-978
- Abstract
- 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.
- Keywords
- Date of publication
- 14.09.2025
- Year of publication
- 2025
- Number of purchasers
- 0
- Views
- 4
References
- 1. Mettenleiter T.C., Sobrino F. // Animal Viruses: Molecular Biology. 2008. V. 14. P. 5. https://doi.org/10.3201/eid1405.080077
- 2. 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
- 3. Khomenko S., Beltrán-Alcrudo D., Rozstalnyy A. et al. // Empress Watch. 2013. V. 28. P. 1
- 4. Mazur-Panasiuk N., Woźniakowski G., Niemczuk K. // Sci Rep. 2019. V. 9. № 4556. https://doi.org/10.1038/s41598-018-36823-0
- 5. 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
- 6. Dixon L.K., Chapman D.A., Netherton C.L., Upton C. // Virus Res. 2013. V. 173 (1). P. 3.
- 7. Netherton C.L., Wileman T.E. // Virus Res. 2013. V. 173 (1). P. 76. https://doi.org/10.1016/j.virusres.2012.12.014
- 8. 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
- 9. 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
- 10. Ruiz-Gonzalvo F., Rodríguez F., Escribano J.M. // Virology. 1996. V. 218 (1). P. 285. https://doi.org/10.1006/viro.1996.0193
- 11. 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
- 12. Araf Y., Moin A.T., Timofeev V.I. et al. // Front. Immunol. 2022. V. 13. 863234. https://doi.org/10.3389/fimmu.2022.863234
- 13. Q89501. https://nbgi.ru/
- 14. Altschul S.F., Gish W., Miller W. et al. // J. Mol. Biol. 1990. V. 215 (3). P. 403.
- 15. Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596. P. 583. https://doi.org/10.1038/s41586-021-03819-2
- 16. Jeppe H., Trigos K.D., Pedersen M.D. et al. // bioRxiv. 2022. https://doi.org/10.1101/2022.04.08.487609
- 17. Larsen M.V., Lundegaard C., Lamberth K. et al. // BMC Bioinformatics. 2007. V. 8. 424. https://doi.org/10.1186/1471-2105-8-424
- 18. http://tools.iedb.org/ellipro/
- 19. Ponomarenko J., Bui HH., Li W. et al. // BMC Bioinformatics. 2008. V. 9. 514. https://doi.org/10.1186/1471-2105-9-514
- 20. 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
- 21. Gupta S., Kapoor P., Chaudhary K. et al. // PLoS ONE. 2020. V. 8 (9). e73957. https://doi.org/10.1371/journal.pone.0073957
- 22. Doytchinova I.A., Flower D.R. // BMC Bioinformatics. 2007. V. 8. 4. https://doi.org/10.1186/1471-2105-8-4
- 23. 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
- 24. Larsen M.V., Lundegaard C., Lamberth K. et al. // BMC Bioinformatics. 2007. V. 8. 424. https://doi.org/10.1186/1471-2105-8-424
- 25. Choo S.Y. // Yonsei Med J. 2007. V. 48 (1). P. 11. https://doi.org/10.3349/ymj.2007.48.1.11
- 26. Potocnakova L., Bhide M., Pulzova L.B. // J. Immunol. Res. 2016. https://doi.org/10.1155/2016/6760830
