Advertisement

Comparative thermostability analysis of zoonotic and human influenza virus A and B neuraminidase

  • Vasily A. EvseenkoEmail author
  • Svetlana V. Svyatchenko
  • Natalia P. Kolosova
  • Valentina L. Kovrizhkina
  • Vasiliy Y. Marchenko
  • Aleksander G. Durymanov
  • Natalia I. Goncharova
  • Alexander B. Ryzhikov
Brief Report
  • 104 Downloads

Abstract

Neuraminidase (NA) thermostability of influenza A and B viruses isolated from birds, swine and humans was measured to evaluate its variability associated with host body temperature. The highest 50% inactivation temperature (IT50) was observed with H3N8 avian influenza virus (74 °C), and the lowest IT50 was observed with the seasonal human H3N2 virus (45.5 °C). The IT50 values of A(H1N1)pdm09 viruses 56.4-58.5 °C were statistically higher than that of the prepandemic strain A/Solomon Islands/03/06 (52.5 °C). An analysis of Ca2+ binding sites revealed the correspondence of amino acid changes to NA thermostability. This study demonstrates that changes in NA thermostability correspond to differences in host body temperature.

Notes

Acknowledgements

The authors thank the CDC (GA, USA), WHO CC for Reference and Research on Influenza, Australia, and Crick Worldwide Influenza Centre, UK, for providing virus strains through IRR and for sharing sequences through GISAID. The authors are especially grateful to the SRC VB “Vector” core sequence facilities.

Funding

This research was funded by the Russian Federal Service for Surveillance on Consumer Rights Protection and Human Wellbeing (Rospotrebnadzor).

Compliance with ethical standards

Conflict of interest

Evseenko V.A. declares that he has no conflict of interest. Kolosova N.P. declares that she has no conflict of interest. Svyatchenko S.V. declares that she has no conflict of interest. Kovrizhkina V.L. declares that she has no conflict of interest. Durymanov A.G. declares that he has no conflict of interest. Goncharova N.A. declares that she has no conflict of interest. Marchenko V.Y. declares that he has no conflict of interest. Ryzhikov A.B. declares that he has no conflict of interest.

Ethical approval

All applicable international, national and institutional guidelines for the care and use of animals were followed. This article does not contain any studies with human participants performed by any of the authors.

References

  1. 1.
    Webster RG, Bean WJ, Gorman OT, Chambers TM, Kawaoka Y (1992) Evolution and ecology of influenza A viruses. Microbiol Rev 56(1):152–179PubMedPubMedCentralGoogle Scholar
  2. 2.
    Tong S, Zhu X, Li Y, Shi M, Zhang J, Bourgeois M et al (2013) New World bats harbor diverse influenza A viruses. PLoS Pathog 9:e1003657.  https://doi.org/10.1371/journal.ppat.1003657 CrossRefPubMedPubMedCentralGoogle Scholar
  3. 3.
    Kawaoka Y, Krauss S, Webster RG (1989) Avian-to-human transmission of the PB1 gene of influenza A viruses in the 1957 and 1968 pandemics. J Virol 63(11):4603–4608PubMedPubMedCentralGoogle Scholar
  4. 4.
    Scholtissek C, Rohde W, Von Hoyningen V, Rott R (1978) On the origin of the human influenza virus subtypes H2N2 and H3N2. Virology 87(1):13–20CrossRefGoogle Scholar
  5. 5.
    Scholtissek C (1994) Source for influenza pandemics. Eur J Epidemiol 10(4):455–458CrossRefGoogle Scholar
  6. 6.
    Torre-Bueno JR (1976) Temperature regulation and heat dissipation during flight in birds. J Exp Biol 65:471–482PubMedGoogle Scholar
  7. 7.
    Murray Pullar E (1949) The rectal temperature in normal and infected pigs. Br Vet J 105(12):437–453CrossRefGoogle Scholar
  8. 8.
    Burmeister W, Cusack S, Ruigrok RJ (1994) Calcium is needed for the thermostability of influenza B virus neuraminidase. Gen Virol 75(2):381–388.  https://doi.org/10.1099/0022-1317-75-2-381 CrossRefGoogle Scholar
  9. 9.
    Baker NJ, Gandhi SS (1976) Effect of Ca ++ on the stability of influenza virus neuraminidase. Arch Virol 52(1–2):7–18CrossRefGoogle Scholar
  10. 10.
    Xu X, Zhu X, Dwek RA, Stevens J, Wilson IA (2008) Structural characterization of the 1918 influenza virus H1N1 neuraminidase. J Virol 82(21):10493–10501.  https://doi.org/10.1128/JVI.00959-08 CrossRefPubMedPubMedCentralGoogle Scholar
  11. 11.
    Air GM (2012) Influenza neuraminidase. Influenza Other Respir Viruses 6(4):245–256CrossRefGoogle Scholar
  12. 12.
    Manual for the laboratory diagnosis and virological surveillance of influenza. 2011 (ISBN: 9789241548090) Google Scholar
  13. 13.
    Marchenko V, Goncharova N, Susloparov I, Kolosova N, Gudymo A, Svyatchenko S et al (2018) Isolation and characterization of H5Nx highly pathogenic avian influenza viruses of clade 2.3.4.4 in Russia. Virology 525:216–223CrossRefGoogle Scholar
  14. 14.
    Tewawong N, Marathe BM, Poovorawan Y, Vongpunsawad S, Webby RJ, Govorkova EA (2018) Neuraminidase inhibitor susceptibility and neuraminidase enzyme kinetics of human influenza A and B viruses circulating in Thailand in 2010–2015. PLoS One 13(1):e0190877CrossRefGoogle Scholar
  15. 15.
    Labadie T, Batéjat C, Manuguerra JC, Leclercq I (2018) Influenza virus segment composition influences viral stability in the environment. Front Microbiol 9:1496.  https://doi.org/10.3389/fmicb.2018.01496(Published 2018 Jul 9) CrossRefPubMedPubMedCentralGoogle Scholar
  16. 16.
    Jhung MA, Epperson S, Biggerstaff M et al (2013) Outbreak of variant influenza A(H3N2) virus in the United States. Clin Infect Dis 57(12):1703–1712.  https://doi.org/10.1093/cid/cit649 CrossRefPubMedPubMedCentralGoogle Scholar
  17. 17.
    Yen HL, Herlocher LM, Hoffmann E et al (2005) Neuraminidase inhibitor-resistant influenza viruses may differ substantially in fitness and transmissibility. Antimicrob Agents Chemother 49(10):4075–4084.  https://doi.org/10.1128/AAC.49.10.4075-4084.2005 CrossRefPubMedPubMedCentralGoogle Scholar
  18. 18.
    Negovetich NJ, Webster RG (2010) Thermostability of subpopulations of H2N3 influenza virus isolates from mallard ducks. J Virol 84(18):9369–9376.  https://doi.org/10.1128/JVI.01170-10 CrossRefPubMedPubMedCentralGoogle Scholar
  19. 19.
    Belser JA, Tumpey TM (2013) H5N1 pathogenesis studies in mammalian models. Virus Res 178(1):168–185.  https://doi.org/10.1016/j.virusres.2013.02.003 CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2019

Authors and Affiliations

  • Vasily A. Evseenko
    • 1
    Email author
  • Svetlana V. Svyatchenko
    • 1
  • Natalia P. Kolosova
    • 1
  • Valentina L. Kovrizhkina
    • 1
  • Vasiliy Y. Marchenko
    • 1
  • Aleksander G. Durymanov
    • 1
  • Natalia I. Goncharova
    • 1
  • Alexander B. Ryzhikov
    • 1
  1. 1.State Research Center of Virology and Biotechnology “Vector”, RospotrebnadzorNovosibirsk RegionRussian Federation

Personalised recommendations