• FluTrackers.com Inc. does not provide medical advice. Information on this web site is collected from various internet resources, and the FluTrackers board of directors makes no warranty to the safety, efficacy, correctness or completeness of the information posted on this site by any author or poster. The information collated here is for instructional and/or discussion purposes only and is NOT intended to diagnose or treat any disease, illness, or other medical condition. Every individual reader or poster should seek advice from their personal physician/healthcare practitioner before considering or using any interventions that are discussed on this website. By continuing to access this website you agree to consult your personal physican before using any interventions posted on this website, and you agree to hold harmless FluTrackers.com Inc., the board of directors, the members, and all authors and posters for any effects from use of any medication, supplement, vitamin or other substance, device, intervention, etc. mentioned in posts on this website, or other internet venues referenced in posts on this website.
  • We are not asking for any donations. Do not donate to any entity who says they are raising funds for us.

Unique structural features of influenza H15 HA

tetano

Editor, Senior Moderator
J Virol. 2017 Apr 12. pii: JVI.00046-17. doi: 10.1128/JVI.00046-17. [Epub ahead of print]
[h=1]Unique structural features of influenza H15 HA.[/h] Tzarum N[SUP]1[/SUP], McBride R[SUP]2[/SUP], Nycholat CM[SUP]2[/SUP], Paulson JC[SUP]3,[/SUP][SUP]4[/SUP], Wilson IA[SUP]5,[/SUP][SUP]6[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] Influenza A H15 viruses are members of a subgroup (H7-H10-H15) of group 2 hemagglutinin (HA) subtypes that include H7N9 and H10N8 viruses that were isolated from humans during 2013. The isolation of avian H15 viruses is, however, quite rare, and until recently, geographically restricted to wild shorebirds and waterfowl in Australia. The HAs of H15 viruses contain an insertion in the 150-loop of the receptor-binding site common to this subgroup and a unique insertion in the 260-loop compared to any other subtype. Here, we show that the H15 HA has a high preference for avian receptor analogs by glycan array analyses. The H15 HA crystal structure reveals that it is structurally closest to H7N9 HA, but the head domain of the H15 trimer is wider than all other HAs due to a tilt and opening of the HA1 subunits of head domain. The extended 150-loop of the H15 HA retains the conserved conformation as in H7 and H10 HAs. Furthermore, the elongated 260-loop increases the HA exposed surface and can contribute to antigenic variation in H15 HAs. Since avian-origin H15 HA viruses have been shown to cause enhanced disease in mammalian models, further characterization and immune surveillance of H15 viruses is warranted.IMPORTANCE In the last two decades, an apparent increase has been reported for cases of human infection by emerging avian influenza A subtypes, including H7N9 and H10N8 viruses isolated during 2013. H15 is the other member of the subgroup of influenza A group 2 hemagglutinins (HA) that also include H7 and H10. H15 viruses have been restricted to Australia, but recent isolation of H15 viruses in Western Siberia suggests that they could be spread more globally via the avian flyways that converge and emanate from this region. Here we report on characterization of the three-dimensional structure and receptor specificity of the H15 hemagglutinin that reveals distinct features and specificities that can aid in global surveillance of such viruses for potential spread and emerging threat to the human population.
Copyright ? 2017 American Society for Microbiology.


PMID: 28404848 DOI: 10.1128/JVI.00046-17
 
Back
Top Bottom