tetano
Editor, Senior Moderator
J Virol. 2014 Dec 24. pii: JVI.02723-14. [Epub ahead of print]
[h=1]Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.[/h] Yang H[SUP]1[/SUP], Nguyen HT[SUP]1[/SUP], Carney PJ[SUP]1[/SUP], Guo Z[SUP]1[/SUP], Chang JC[SUP]1[/SUP], Jones J[SUP]1[/SUP], Davis CT[SUP]1[/SUP], Villanueva JM[SUP]1[/SUP], Gubareva LV[SUP]1[/SUP], Stevens J[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] In late 2011, an A(H3N8) influenza virus infection resulted in the deaths of 162 New England harbor seals. Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference (Anthony et al. ; MBio 3: e00166-00112). Here we present a detailed structural and biochemical analysis of the surface antigens of this virus. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase, indicate a true avian receptor binding preference. Although the detection of this virus in new species highlights an increased potential for cross-species transmission with these viruses, our results indicate that the A(H3N8) virus currently poses a low risk to humans.
[h=4]IMPORTANCE:[/h] Cross-species transmission of zoonotic influenza viruses increases public health concerns. Here we report a molecular and structural study of the major surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals. Results improve our understanding of these viruses as they evolve and provide important information to aid ongoing risk assessment analyses, as these zoonotic influenza viruses continue to circulate and adapt to new hosts.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID: 25540377 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25540377
[h=1]Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.[/h] Yang H[SUP]1[/SUP], Nguyen HT[SUP]1[/SUP], Carney PJ[SUP]1[/SUP], Guo Z[SUP]1[/SUP], Chang JC[SUP]1[/SUP], Jones J[SUP]1[/SUP], Davis CT[SUP]1[/SUP], Villanueva JM[SUP]1[/SUP], Gubareva LV[SUP]1[/SUP], Stevens J[SUP]2[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] In late 2011, an A(H3N8) influenza virus infection resulted in the deaths of 162 New England harbor seals. Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference (Anthony et al. ; MBio 3: e00166-00112). Here we present a detailed structural and biochemical analysis of the surface antigens of this virus. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase, indicate a true avian receptor binding preference. Although the detection of this virus in new species highlights an increased potential for cross-species transmission with these viruses, our results indicate that the A(H3N8) virus currently poses a low risk to humans.
[h=4]IMPORTANCE:[/h] Cross-species transmission of zoonotic influenza viruses increases public health concerns. Here we report a molecular and structural study of the major surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals. Results improve our understanding of these viruses as they evolve and provide important information to aid ongoing risk assessment analyses, as these zoonotic influenza viruses continue to circulate and adapt to new hosts.
Copyright ? 2014, American Society for Microbiology. All Rights Reserved.
PMID: 25540377 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25540377