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Influenza A(H7N9) virus gains neuraminidase inhibitor resistance without loss of in vivo virulence or transmissibility

Author

Listed:
  • Rong Hai

    (Icahn School of Medicine at Mount Sinai)

  • Mirco Schmolke

    (Icahn School of Medicine at Mount Sinai
    Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai)

  • Victor H. Leyva-Grado

    (Icahn School of Medicine at Mount Sinai)

  • Rajagowthamee R. Thangavel

    (Icahn School of Medicine at Mount Sinai)

  • Irina Margine

    (Icahn School of Medicine at Mount Sinai)

  • Eric L. Jaffe

    (Icahn School of Medicine at Mount Sinai)

  • Florian Krammer

    (Icahn School of Medicine at Mount Sinai)

  • Alicia Solórzano

    (Public Health Research Institute and Regional Biocontainment Laboratory, New Jersey Medical School, RUTGERS, The State University of New Jersey)

  • Adolfo García-Sastre

    (Icahn School of Medicine at Mount Sinai
    Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai
    Icahn School of Medicine at Mount Sinai)

  • Peter Palese

    (Icahn School of Medicine at Mount Sinai
    Icahn School of Medicine at Mount Sinai)

  • Nicole M. Bouvier

    (Icahn School of Medicine at Mount Sinai
    Icahn School of Medicine at Mount Sinai)

Abstract

Without baseline human immunity to the emergent avian influenza A(H7N9) virus, neuraminidase inhibitors are vital for controlling viral replication in severe infections. An amino acid change in the viral neuraminidase associated with drug resistance, NA-R292K (N2 numbering), has been found in some H7N9 clinical isolates. Here we assess the impact of the NA-R292K substitution on antiviral sensitivity and viral replication, pathogenicity and transmissibility of H7N9 viruses. Our data indicate that an H7N9 isolate encoding the NA-R292K substitution is highly resistant to oseltamivir and peramivir and partially resistant to zanamivir. Furthermore, H7N9 reassortants with and without the resistance mutation demonstrate comparable viral replication in primary human respiratory cells, virulence in mice and transmissibility in guinea pigs. Thus, in stark contrast to oseltamivir-resistant seasonal influenza A(H3N2) viruses, H7N9 virus replication and pathogenicity in these models are not substantially altered by the acquisition of high-level oseltamivir resistance due to the NA-R292K mutation.

Suggested Citation

  • Rong Hai & Mirco Schmolke & Victor H. Leyva-Grado & Rajagowthamee R. Thangavel & Irina Margine & Eric L. Jaffe & Florian Krammer & Alicia Solórzano & Adolfo García-Sastre & Peter Palese & Nicole M. Bo, 2013. "Influenza A(H7N9) virus gains neuraminidase inhibitor resistance without loss of in vivo virulence or transmissibility," Nature Communications, Nature, vol. 4(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3854
    DOI: 10.1038/ncomms3854
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    Cited by:

    1. Manxue Jia & Hanjun Zhao & Nicholas C. Morano & Hong Lu & Yin-Ming Lui & Haijuan Du & Jordan E. Becker & Kwok-Yung Yuen & David D. Ho & Peter D. Kwong & Lawrence Shapiro & Kelvin Kai-Wang To & Xueling, 2024. "Human neutralizing antibodies target a conserved lateral patch on H7N9 hemagglutinin head," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Guha Asthagiri Arunkumar & Disha Bhavsar & Tiehai Li & Shirin Strohmeier & Veronika Chromikova & Fatima Amanat & Mehman Bunyatov & Patrick C. Wilson & Ali H. Ellebedy & Geert-Jan Boons & Viviana Simon, 2021. "Functionality of the putative surface glycoproteins of the Wuhan spiny eel influenza virus," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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