tetano
Editor, Senior Moderator
Vet Microbiol. 2016 Nov 30;196:9-13. doi: 10.1016/j.vetmic.2016.10.006. Epub 2016 Oct 11.
[h=1]Impact of a potential glycosylation site at neuraminidase amino acid 264 of influenza A/H9N2 virus.[/h] Shao H[SUP]1[/SUP], Zhou X[SUP]1[/SUP], Fan Z[SUP]1[/SUP], Wan Z[SUP]2[/SUP], Qian K[SUP]1[/SUP], Perez D[SUP]3[/SUP], Qin A[SUP]4[/SUP], Ye J[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] To determine the role of the potential glycosylation site NA264N, which has been shown to be prevalent in recent Chinese H9N2 isolates, four reverse genetic viruses, rgWS1-NA264N, rgWS1-NA264H, rgBJ-NA264H and rgBJ-NA264N, were rescued. Growth kinetics showed that viruses with NA264H grew faster than viruses with NA264N. Mouse studies revealed that rgBJ-NA264H replicated to a significantly higher titer than rgBJ-NA264N at 3dpi. Notably, in contact chickens, rgBJ-NA264H and rgWS1-NA264H shed significantly more virus than rgBJ-NA264N at 6dpi from the larynx and rgWS1-NA264N at 4dpi from the cloaca, respectively. The present study demonstrates that NA264N affects viral replication of H9N2.
Copyright ? 2016 Elsevier B.V. All rights reserved.
[h=4]KEYWORDS:[/h] H9N2; NA264N; Pathogenesis; Viral replication; Virus rescuing
PMID: 27939162 DOI: 10.1016/j.vetmic.2016.10.006
[PubMed - in process]
[h=1]Impact of a potential glycosylation site at neuraminidase amino acid 264 of influenza A/H9N2 virus.[/h] Shao H[SUP]1[/SUP], Zhou X[SUP]1[/SUP], Fan Z[SUP]1[/SUP], Wan Z[SUP]2[/SUP], Qian K[SUP]1[/SUP], Perez D[SUP]3[/SUP], Qin A[SUP]4[/SUP], Ye J[SUP]5[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] To determine the role of the potential glycosylation site NA264N, which has been shown to be prevalent in recent Chinese H9N2 isolates, four reverse genetic viruses, rgWS1-NA264N, rgWS1-NA264H, rgBJ-NA264H and rgBJ-NA264N, were rescued. Growth kinetics showed that viruses with NA264H grew faster than viruses with NA264N. Mouse studies revealed that rgBJ-NA264H replicated to a significantly higher titer than rgBJ-NA264N at 3dpi. Notably, in contact chickens, rgBJ-NA264H and rgWS1-NA264H shed significantly more virus than rgBJ-NA264N at 6dpi from the larynx and rgWS1-NA264N at 4dpi from the cloaca, respectively. The present study demonstrates that NA264N affects viral replication of H9N2.
Copyright ? 2016 Elsevier B.V. All rights reserved.
[h=4]KEYWORDS:[/h] H9N2; NA264N; Pathogenesis; Viral replication; Virus rescuing
PMID: 27939162 DOI: 10.1016/j.vetmic.2016.10.006
[PubMed - in process]