• 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.

Reduction of Influenza Virus Envelope's Fusogenicity by Viral Fusion Inhibitors

tetano

Editor, Senior Moderator
ACS Infect Dis. 2016 Jan 8;2(1):47-53. Epub 2015 Oct 22.
[h=1]Reduction of Influenza Virus Envelope's Fusogenicity by Viral Fusion Inhibitors.[/h] Rowse M[SUP]1[/SUP], Qiu S[SUP]1[/SUP], Tsao J[SUP]1[/SUP], Yamauchi Y[SUP]2[/SUP], Wang G[SUP]3[/SUP], Luo M[SUP]3,[/SUP][SUP]4[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] During cell entry of an enveloped virus, the viral membrane must be fused with the cellular membrane. The virus envelope has a unique structure consisting of viral proteins and a virus-specific lipid composition, whereas the host membrane has its own structure with host membrane proteins. Compound 136 was previously found to bind in close proximity to the viral envelope and inhibit influenza virus entry. We showed here that the 136-treated influenza virus still caused hemolysis. When liposomes were used as the target membrane for 136-treated viruses, aberrant fusion occurred; few liposomes fused per virion, and glycoproteins were not distributed evenly across fusion complexes. Additionally, large fusion aggregates did not form, and in some instances, neck-like structures were found. Based on previous results and hemolysis, fusion inhibition by 136 occurs post-scission but prior to lipid mixing.


[h=4]KEYWORDS:[/h] fusion inhibitor; fusogenicity; influenza virus; lipid composition; liposome

PMID: 27622947 DOI: 10.1021/acsinfecdis.5b00109
[PubMed - as supplied by publisher]
 
Back
Top Bottom