tetano
Editor, Senior Moderator
J Virol. 2013 Nov 27. [Epub ahead of print]
The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity.
Tefsen B, Lu G, Zhu Y, Haywood J, Zhao L, Deng T, Qi J, Gao GF.
Source
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Abstract
Influenza imposes a great burden on society, not only in its seasonal appearance that affects both humans and domesticated animals, but also through the constant threat of potential pandemics. Migratory birds are considered to be the reservoir hosts for influenza viruses, but other animals must also be considered. The recently identified influenza-like virus genome, H17N10, in bats, was shown to be markedly different from other known influenza viruses, as both its surface glycoproteins hemagglutinin (HA) and neuraminidase (NA) do not have canonical functions. However no studies on other individual proteins from this particular virus have been reported until now. Here, we describe the structure of the N-terminal domain of PA from H17N10 influenza-like virus at 2.7 ? resolution and show that it has a similar fold as homologous PA domains present in more familiar influenza A strains. Moreover, we demonstrate that it possesses endonuclease activity and that the histidine residue in the active site is essential for this activity. Although this particular influenza subtype is probably not infectious for humans (even its virus state has not been confirmed in bat as only the genome has been sequenced), reassortment of canonical influenza viruses with certain segments from H17N10 cannot be ruled out at this stage. Therefore further studies are urgently called for the sake of influenza prevention and control.
PMID:
24284327
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24284327
The N-terminal domain of PA from bat-derived influenza-like virus H17N10 has endonuclease activity.
Tefsen B, Lu G, Zhu Y, Haywood J, Zhao L, Deng T, Qi J, Gao GF.
Source
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Abstract
Influenza imposes a great burden on society, not only in its seasonal appearance that affects both humans and domesticated animals, but also through the constant threat of potential pandemics. Migratory birds are considered to be the reservoir hosts for influenza viruses, but other animals must also be considered. The recently identified influenza-like virus genome, H17N10, in bats, was shown to be markedly different from other known influenza viruses, as both its surface glycoproteins hemagglutinin (HA) and neuraminidase (NA) do not have canonical functions. However no studies on other individual proteins from this particular virus have been reported until now. Here, we describe the structure of the N-terminal domain of PA from H17N10 influenza-like virus at 2.7 ? resolution and show that it has a similar fold as homologous PA domains present in more familiar influenza A strains. Moreover, we demonstrate that it possesses endonuclease activity and that the histidine residue in the active site is essential for this activity. Although this particular influenza subtype is probably not infectious for humans (even its virus state has not been confirmed in bat as only the genome has been sequenced), reassortment of canonical influenza viruses with certain segments from H17N10 cannot be ruled out at this stage. Therefore further studies are urgently called for the sake of influenza prevention and control.
PMID:
24284327
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24284327