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X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus

Author

Listed:
  • Zachary A. Bornholdt

    (Department of Molecular Virology and Microbiology,)

  • B. V. Venkataram Prasad

    (Department of Molecular Virology and Microbiology,
    Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA)

Abstract

Avian flu virulence The NS1 protein of influenza virus is a critical virulence factor that antagonizes the host antiviral response by multiple mechanisms, including the binding and sequestration of double-stranded RNA. The structure of full-length NS1 protein has now been determined using samples from a virulent H5N1 avian influenza virus strain isolated during a 2004 Vietnamese 'bird flu' outbreak. The molecule's RNA binding domain shows subtle differences when compared to that in non-H5N1 strains whereas the effector domain is significantly altered. The two domains interact in such a way as to form tubules that may act to sequester dsRNA, allowing the virus to evade the host's innate immune response.

Suggested Citation

  • Zachary A. Bornholdt & B. V. Venkataram Prasad, 2008. "X-ray structure of NS1 from a highly pathogenic H5N1 influenza virus," Nature, Nature, vol. 456(7224), pages 985-988, December.
  • Handle: RePEc:nat:nature:v:456:y:2008:i:7224:d:10.1038_nature07444
    DOI: 10.1038/nature07444
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