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Neuraminidase mutations conferring resistance to laninamivir lead to faster drug binding and dissociation

tetano

Editor, Senior Moderator
Antiviral Res. 2014 Dec 9. pii: S0166-3542(14)00335-0. doi: 10.1016/j.antiviral.2014.12.004. [Epub ahead of print]
[h=1]Neuraminidase mutations conferring resistance to laninamivir lead to faster drug binding and dissociation.[/h] L McKimm-Breschkin J[SUP]1[/SUP], Barrett S[SUP]2[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] The neuraminidase (NA) inhibitors oseltamivir and zanamivir are administered twice daily for five days for treatment of influenza. Laninamivir is a 7-methoxy derivative of zanamivir, but a single dose is effective when taken as the laninamivir octanoate prodrug. We show here in IC[SUB]50[/SUB] kinetics assays and a solid phase reactivation assay that compared to zanamivir laninamivir also demonstrates slow binding to but slower dissociation from multiple wild type NAs. A D197E mutation in an influenza B and an E119G in an N9 neuraminidase which confer 15- and 150-fold resistance to laninamivir result in faster binding and dissociation. Despite similar IC[SUB]50[/SUB]s our assays demonstrate more rapid dissociation of laninamivir from clade 1 compared to 2 H5N1 NAs.
Copyright ? 2014. Published by Elsevier B.V.


[h=4]KEYWORDS:[/h] Enzyme kinetics; Influenza; Laninamivir; Resistance

PMID: 25499124 [PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/25499124
 
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