GENETIC AND ANTIGENIC CHARACTERISTICS OF RESPIRATORY SYNCYTIAL VIRUS STRAINS ISOLATED IN ST. PETERSBURG IN 2013-2016

Cover Page


Cite item

Full Text

Abstract

Antigenic and genetic characteristics of Russian RSV isolates are presented for the first time. Of the 69 strains isolated in St. Petersburg, 93% belonged to the RSV-A antigenic group. The antigenic variations in the F-protein RSV were analyzed using a panel from 6 monoclonal antibodies by the method of micro-cultural ELISA. Depending on the decrease in the effectiveness of interaction with monoclonal antibodies (relative to the reference strain Long), RSV-A isolates were divided into 4 antigenic subgroups. The results of 24 isolates sequencing showed that more than 60% of them had substitutions in significant F-protein sites compared to the ON67-1210A reference strain of the current RSV genotype ON1/GA2. The most variable were the signal peptide and antigenic site II. When comparing the results of ELISA and sequencing, it was not possible to identify any specific key substitutions in the amino acid sequence of the F-protein that affect the interaction of the virus with antibodies. The nucleotide sequence of the F-gene from 19 of the 24 characterized isolates was close to that of ON67-1210A reference virus and was significantly different from RSV-A Long and A2 viruses. A separate group consisted of 5 strains, in which the F-protein structure was approximated to RSV Long.

About the authors

V. Z. Krivitskaya

Research Institute of Influenza

Author for correspondence.
Email: vera.kriv@influenza.spb.ru
Россия

K. S. Sintsova

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

E. R. Petrova

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

M. V. Sverlova

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

E. V. Sorokin

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

T. R. Tsareva

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

A. B. Komissarov

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

A. V. Fadeev

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

M. M. Pisareva

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

Zh. V. Buzitskaya

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

V. S. Afanaseva

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

V. F. Sukhovetskaya

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

A. A. Sominina

Research Institute of Influenza

Email: noemail@neicon.ru
Россия

References

  1. Соминина А.А., Писарева М.М., Бузицкая Ж.В., Осидак Л.В., Суховецкая В.Ф., Афанасьева О.И. и др. Особенности этиологии респираторных вирусных инфекций у госпитализированных больных в зависимости от демографических, социально-экономических факторов и предшествующей вакцинации. Эпидемиология и вакцинопрофилактика. 2015; (3): 74-83
  2. Adams O., Werzmirzowsky J., Hengel H. Genetic analysis and antigenic characterization of human respiratory syncytial virus group A viruses isolated in Germany 1996-2008. Virus Genes. 2013; 47(2): 210-8.
  3. Trento A., Ábrego L., Rodriguez-Fernandez R., González-Sánchez M.I., González-Martínez F., Delfraro A., et al. Conservation of G-Protein Epitopes in Respiratory Syncytial Virus (Group A) Despite Broad Genetic Diversity: Is Antibody Selection Involved in Virus Evolution? J. Virol. 2015; 89(15): 7776-85.
  4. Melero J., Moore M. Influence of respiratory syncytial virus strain differences on pathogenesis and immunity. Curr. Top. Microbiol. Immunol. 2013; 72: 59-82.
  5. Kimura H., Nagasawa K., Tsukagoshi H., Matsushima Y., Fujita K., Yoshida L.M., et al. Molecular evolution of the fusion protein gene in human respiratory syncytial virus subgroup A. Infect. Genet. Evol. 2016; 43: 398-406.
  6. Kimura H., Nagasawa K., Kimura R., Tsukagoshi H., Matsushima Y., Fujita K., et al. Molecular evolution of the fusion protein (F) gene in human respiratory syncytial virus subgroup B. Infect. Genet. Evol. 2017; 52: 1-9.
  7. Melero J.A., Mas V. The Pneumovirinae fusion (F) protein: A common target for vaccines and antivirals. Virus. Res. 2015; 209: 128-35.
  8. Кривицкая В.З., Петрова Е.Р., Сорокин Е.В., Царева Т.Р., Сверлова М.В., Фадеев А.В. и др. Получение и характеристика моноклональных антител, специфичных к респираторно-синцитиальному вирусу. Биотехнология. 2016; (1): 65-75
  9. Agenbach E., Tiemessen C.T., Venter M. Amino acid variation within the fusion protein of respiratory syncytial virus subtype A and B strains during annual epidemics in South Africa. Virus Genes. 2005; 30(2): 267-78.
  10. Eshaghi A., Duvvuri V.R., Lai R., Nadarajah J.T., Li A., Patel S.N., et al. Genetic variability of human respiratory syncytial virus A strains circulating in Ontario: a novel genotype with a 72 nucleotide G gene duplication. PLoS One. 2012; 7(3): e32807.
  11. Tapia L.I., Shaw C.A., Aideyan L.O., Jewell A.M., Dawson B.C., Haq T.R., et al. Gene sequence variability of the three surface proteins of human respiratory syncytial virus (HRSV) in Texas. PLoS One. 2014; 9(3): e90786.
  12. Day N.D., Branigan P.J., Liu C., Gutshall L.L., Luo J., Melero J.A., et al. Contribution of cysteine residues in the extracellular domain of the F protein of human respiratory syncytial virus to its function. Virol. J. 2006; (3): 34.
  13. Castilow E.M., Varga S.M. Overcoming T cell-mediated immunopathology to achieve safe RSV vaccination. Future Virol. 2008; 3(5): 445-54.
  14. McLellan J.S. Neutralizing epitopes on the respiratory syncytial virus fusion glycoprotein. Curr. Opin. Virol. 2015; (11): 70-5.
  15. Lambert D.M., Barney S., Lambert A.L., Guthrie K., Medinas R., Davis D.E., et al. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion. Proc. Natl. Acad. USA. 1996; 93: 2186-91.
  16. Johnstone C., Guil S., Rico M.A., García-Barreno B., López D., Melero J.A., et al. Relevance of viral context and diversity of antigen-processing routes for respiratory syncytial virus cytotoxic T-lymphocyte epitopes. J. Gen. Virol. 2008; 89(Pt. 9): 2194-203.
  17. Zimmer G., Budz L., Herrler G. Proteolytic activation of respiratory syncytial virus fusion protein. Cleavage at two furin consensus sequences. J. Biol. Chem. 2001; 276(34): 31642-50.
  18. Crim R.L., Audet S.A., Feldman S.A., Mostowski H.S., Beeler J.A. Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity. J. Virol. 2007; 81(1): 261-71.
  19. Martín D., Calder L.J., García-Barreno B., Skehel J.J., Melero J.A. Sequence elements of the fusion peptide of human respiratory syncytial virus fusion protein required for activity. J. Gen. Virol. 2006; 87(Pt. 6): 1649-58.
  20. Tripp R.A., Hou S., Etchart N., Prinz A., Moore D., Winter J., et al. CD4(+) T cell frequencies and Th1/Th2 cytokine patterns expressed in the acute and memory response to respiratory syncytial virus I-E(d)-restricted peptides. Cell Immunol. 2001; 207(1): 59-71.
  21. Morton C.J., Cameron R., Lawrence L.J., Lin B., Lowe M., Luttick A., et al. Structural characterization of respiratory syncytial virus fusion inhibitor escape mutants: homology model of the F protein and a syncytium formation assay. Virology. 2003; 311(2): 275-88.
  22. Adams O., Bonzel L., Kovacevic A., Mayatepek E., Hoehn T., Vogel M. Palivizumab-resistant human respiratory syncytial virus infection in infancy. Clin. Infect. Dis. 2010; 51(2): 185-8.
  23. Zhu Q., McAuliffe J.M., Patel N.K., Palmer-Hill F.J., Yang C.F., Liang B., et al. Analysis of respiratory syncytial virus preclinical and clinical variants resistant to neutralization by monoclonal antibodies palivizumab and/or motavizumab. J. Infect. Dis. 2011; 203: 674-82.
  24. Singh S.R., Dennis V.A., Carter C.L., Pillai S.R., Jefferson A., Sahi S.V., et al. Immunogenicity and efficacy of recombinant RSV-F vaccine in a mouse model. Vaccine. 2007; 25(33): 6211-23.
  25. López J.A., Bustos R., Orvell C., Berois M., Arbiza J., García-Barreno B., et al. Antigenic structure of human respiratory syncytial virus fusion glycoprotein. J. Virol. 1998; 72(8): 6922-8.
  26. Scopes G.E., Watt P.J., Lambden P.R. Identification of linear epitope on the fusion glycoprotein of respiratory syncytial virus. J. Gen. Virology. 1990; 71: 53-9.
  27. Oliveira D.B., Iwane M.K., Prill M.M., Weinberg G.A., Williams J.V., Griffin M.R., et al. Molecular characterization of respiratory syncytial viruses infecting children reported to have received palivizumab immunoprophylaxis. J. Clin. Virol. 2015; 65: 26-31.
  28. Zhu Q., Patel N.K., McAuliffe J.M., Zhu W., Wachter L., McCarthy M.P., et al. Natural polymorphisms and resistance-associated mutations in the fusion protein of respiratory syncytial virus (RSV): effects on RSV susceptibility to palivizumab. J. Infect. Dis. 2012; 205(4): 635-8.
  29. Low K.W., Tan T., Ng K., Tan B.H., Sugrue R.J. The RSV F and G glycoproteins interact to form a complex on the surface of infected cells. Biochem. Biophys. Res. Commun. 2008; 366(2): 308-13.

Supplementary files

Supplementary Files
Action
1. JATS XML

Copyright (c) 2017 Krivitskaya V.Z., Sintsova K.S., Petrova E.R., Sverlova M.V., Sorokin E.V., Tsareva T.R., Komissarov A.B., Fadeev A.V., Pisareva M.M., Buzitskaya Z.V., Afanaseva V.S., Sukhovetskaya V.F., Sominina A.A.

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

СМИ зарегистрировано Федеральной службой по надзору в сфере связи, информационных технологий и массовых коммуникаций (Роскомнадзор).
Регистрационный номер и дата принятия решения о регистрации СМИ: серия ПИ № ФС77-77676 от 29.01.2020.


This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies