RAS PhysicsКристаллография Crystallography Reports

  • ISSN (Print) 0023-4761
  • ISSN (Online) 3034-5510

Development of a subunit vaccine against virus of african svine virus based on cd2v protein with immunoinformatics and molecular dynamics methods

PII
10.31857/S0023476124060089-1
DOI
10.31857/S0023476124060089
Publication type
Article
Status
Published
Authors
Volume/ Edition
Volume 69 / Issue number 6
Pages
987-997
Abstract
A subunit vaccine against the African swine fever virus (ASF) has been designed using immunoinformatics and molecular dynamics methods. The three-dimensional structure of the selected immunogenic protein of the ASF-CD2v virus was modelled, and its topology relative to the membrane was predicted. B- and T-cell epitopes for the supramembrane part of CD2v were predicted, and their immunogenicity, allergenicity, and toxicity were evaluated. In order to facilitate the development of a subunit vaccine, the least variable site was identified on the basis of an analysis of the conservatism of the predicted epitopes. The stability of the selected supramembrane site in an aqueous salt solution was evaluated using molecular dynamics methods, and it was demonstrated that the site is structurally stable. The immunomodulation method has demonstrated that the developed candidate vaccine is capable of eliciting a sustained immune response and does not result in the development of a cytokine storm.
Keywords
Date of publication
15.09.2025
Year of publication
2025
Number of purchasers
0
Views
6

References

  1. 1. Revilla Y., Pérez-Núñez D., Juergen A. // Adv. Virus Res. 2018. V. 100. P. 41. https://doi.org/10.1016/bs.aivir.2017.10.002
  2. 2. Россельхознадзор. Африканская чума свиней. https://fsvps.gov.ru/jepizooticheskaja – situacija/rossija/jepidsituacija-po-achs-v-rossijskoj-federacii/hronologija-achs/
  3. 3. Liu Q., Ma B., Qian N. et al. // Cell Res. 2019. V. 29. P. 953. https://doi.org/10.1038/s41422-019-0232-x
  4. 4. Ros-Lucas A., Correa-Fiz F., Bosch-Camós L., Rodriguez F. // Pathogens. 2020. V. 9. P. 1078. https://doi.org/10.3390/pathogens9121078
  5. 5. Blome S., Franzke K., Beer M. // Virus Res. 2020. V. 287. № 198099. https://doi.org/10.1016/j.virusres.2020.198099
  6. 6. Borca M.V., Ramirez-Medina E., Silva E. et al. // Viruses. 2020. V. 13 (5). P. 765. https://doi.org/10.3390/v13050765
  7. 7. Lewis T., Zsak L., Burrage T.G. et al. // J. Virol. 2000. V. 74 (3). P. 1275.
  8. 8. Monteagudo P.L., Lacasta A., Lopez E. et al. // J. Virol. 2017. V. 91 (21). https://doi.org/10.1128/JVI.01058-17
  9. 9. Moore D.M., Zsak L., Neilan J.G. et al. // J. Virology. 1998. V. 72 (12). P. 10310.
  10. 10. O'Donnell V., Holinka L.G., Gladue D.P. et al. // J. Virol. 2015. V. 89 (11). P.6048. https://doi.org/10.1128/JVI.00554-15
  11. 11. O'Donnell V., Risatti G.R., Holinka L.G. et al. // J. Virol. 2017. V. 91 (1). https://doi.org/10.1128/JVI.01760-16
  12. 12. Reis A.L., Goatley L.C., Jabbar T. et al. // J. Virol. 2017. V. 91. P. 24. https://doi.org/10.1128/JVI.01428-17
  13. 13. Sanchez-Cordon P.J., Jabbar T., Berrezaie M. et al. // Vaccine. 2018. V. 36 (5). P. 707. https://doi.org/10.1016/j.vaccine.2017.12.030
  14. 14. Tran X.H., Le T.T.P., Nguyen Q.H. et al. // Transbound. Emerg. Dis. 2022. V. 69. P. 497. https://doi.org/10.1111/tbed.14329
  15. 15. Алексеев К.П., Раев С.А., Южаков А.Г. и др. // Сельхозбиология. 2019. Т. 54 (6). С. 1236. https://doi.org/10.15389/agrobiology.2019.6.1236rus
  16. 16. Purcell A., McCluskey J., Rossjohn J. // Nat. Rev. Drug Discov. 2007. V. 6. P. 404. https://doi.org/10.1038/nrd2224
  17. 17. Шамсутдинова О.А. // Инфекция и иммунитет. 2017. Т. 7. № 2. C. 107. https://doi.org/10.15789/2220-7619-2017-2-107-116
  18. 18. Moyle P.M., Toth I. // ChemMedChem. 2013. V. 8. P. 360. https://doi.org/10.1002/cmdc.201200487
  19. 19. Abass O.A., Timofeev V.I., Sarkar B. et al. // J. Biomol. Struct. Dyn. 2022. V. 40 (16). P. 7283. https://doi.org/10.1080/07391102.2021.1896387
  20. 20. Adekunle B.R., Angus Nnamdi Oli, Mercy Titilayo Asala et al. // Veterinary Vaccine. 2023. V. 2 (1). P. 2772. https://doi.org/10.1016/j.vetvac.2023.100013
  21. 21. Rakitina T.V., Smirnova E.V., Podshivalov D.D. et al. // Crystals. 2023. V. 13. P. 1416. https://doi.org/10.3390/cryst13101416
  22. 22. Zhang M., Lv L., Luo H. et al. // Vet. Res. 2023. V. 54. P. 106. https://doi.org/10.1186/s13567-023-01239-w
  23. 23. Чернышев Р.С., Спрыгин А.В., Иголкин А.С. и др. // Сельскохозяйственная биология. 2022. T. 57. № 4. С. 609. https://doi.org/10.15389/agrobiology.2022.4.609rus
  24. 24. Колесников И.А., Тимиофеев В.И., Ермаков А.В. и др. // Кристаллография. 2023. Т. 68. № 6. C. 971. https://doi.org/10.31857/S0023476123600179
  25. 25. Ивановский А.С., Колесников И.А., Кордонская Ю.В. и др. // Кристаллография. 2023. Т. 68. № 6. C. 979. https://doi.org/10.31857/S0023476123600805
  26. 26. A0A7T0LXP0 // UniProtKB. https://www.uniprot.org/uniprotkb
  27. 27. Jumper J., Evans R., Pritzel A. et al. // Nature. 2021. V. 596.P. 583. https://doi.org/10.1038/s41586-021-03819-2
  28. 28. Jeppe H., Trigos K.D., Pedersen M.D. et al. // ВioRxiv. 2022.№ 487609. https://doi.org/10.1101/2022.04.08.487609
  29. 29. The PyMOL Molecular Graphics System, Version 3.0 Schrödinger, LLC. https://pymol.org/
  30. 30. Larsen M.V., Lundegaard C., Lamberth K. et al. // BMC Bioinformatics. 2007. V. 8. P. 424.
  31. 31. https://doi.org/10.1186/1471-2105-8-424
  32. 32. Ponomarenko J., Bui HH., Li W. et al. // BMC Bioinformatics. 2008.V. 9. P. 514. https://doi.org/10.1186/1471-2105-9-514
  33. 33. Sudipto Saha, Raghava G.P.S. // Nucleic Acids Res. 2006. V. 34. P. 202.
  34. 34. https://doi.org/10.1093/nar/gkl343
  35. 35. Sharma N., Naorem L.D., Jain S., Raghava G.P.S. // Brief Bioinform. 2022. V. 23 (5). P. 174. https://doi.org/10.1093/bib/bbac174.
  36. 36. Doytchinova I.A., Flower D.R. // BMC Bioinformatics. 2007. V. 8. P. 4. https://doi.org/10.1186/1471-2105-8-4
  37. 37. Altschul S.F., Gish W., Miller W. et al. // J. Mol. Biol. 1990. V. 215 (3). P. 403
  38. 38. Bui H., Sidney J.H., Li W. et al. // BMC Bioinformatics. 2007. V. 8 (1). P. 361. https://doi.org/10.1186/1471-2105-8-361
  39. 39. Rapin N., Lund O., Bernaschi M., Castiglione F. // PLoS One. 2010. V. 5 (4). P. 9862. https://doi.org/10.1371/journal.pone.0009862
  40. 40. Carvalho L., Sano Gi., Hafalla J. et al. // Nat. Med. 2002. V. 8. P. 166. https://doi.org/10.1038/nm0202-166
  41. 41. Berendsen H.J.C., Postma J.P.M., van Gunsteren W.F. et al. // J. Chem. Phys. 1984. V. 81. P. 3684. https://doi.org/10.1063/1.448118
  42. 42. Parrinello M., Rahman A. // J. Chem. Phys. 1982. V. 76. P. 2662. https://doi.org/ 10.1063/1.443248
  43. 43. Hess B., Bekker H., Herman J.C. et al. // J. Comput. Chem. 1997. V. 18. P. 1463. https://doi.org/10.1002/ (SICI)1096-987X(199709)18:12%3C1463::AID-JCC4%3E3.0.CO;2-H
  44. 44. Darden T., York D., Pedersen L. // J. Chem. Phys. 1993. V. 98 (12). P. 10089. https://doi.org/10.1063/1.464397
  45. 45. Potocnakova L., Bhide M., Pulzova L.B. // J. Immunol. Res. 2016. № 6760830. https://doi.org/10.1155/2016/6760830
QR
Translate

Индексирование

Scopus

Scopus

Scopus

Crossref

Scopus

Higher Attestation Commission

At the Ministry of Education and Science of the Russian Federation

Scopus

Scientific Electronic Library