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High-resolution melting analysis for detection of nucleotide mutation markers in the polymerase-acidic (PA) gene of influenza virus that are associated with baloxavir marboxil resistance.
Arch Virol
January 2025
Department Experimental and Clinical Medicine, University of Florence, Florence, Italy.
The I38T substitution in the influenza virus polymerase-acidic (PA) subunit is a resistance marker of concern for treatment with the antiviral baloxavir marboxil (BXM). Thus, monitoring PA/I38T mutations is of clinical importance. Here, we developed three rapid and sensitive assays for the detection and monitoring of the PA/I38T mutation.
View Article and Find Full Text PDFIn vitro neuraminidase inhibitory concentrations (IC) of four neuraminidase inhibitors in the Japanese 2023-24 season: Comparison with the 2010-11 to 2022-23 seasons.
J Infect Chemother
December 2024
Japan Physicians Association, Tokyo, Japan; Ricerca Clinica Co., Fukuoka, Japan.
Introduction: To assess the susceptibility of epidemic influenza viruses to the four most used neuraminidase inhibitors (NAIs) during the 2023-24 influenza season in Japan, we measured the 50% inhibitory concentration (IC) of oseltamivir, peramivir, zanamivir, and laninamivir in virus isolates from the sample of 100 patients.
Methods: Viral isolation was done using specimens obtained before and after treatment, with the type/subtype determined by RT-PCR using type- and subtype-specific primers. IC values were determined by a neuraminidase inhibition assay using a fluorescent substrate.
An outbreak of influenza A(H1N1)pdm09 antigenic variants exhibiting cross-resistance to oseltamivir and peramivir in an elementary school in Japan, September 2024.
Euro Surveill
December 2024
Research Center for Influenza and Respiratory Viruses, National Institute of Infectious Diseases, Tokyo, Japan.
An outbreak of influenza A(H1N1)pdm09 viruses exhibiting cross-resistance to oseltamivir and peramivir occurred in Yokohama, Japan, in September 2024. Among 24 students in a class, 11 were diagnosed with influenza or influenza-like illness, and viruses harbouring the NA H275Y and HA Q210H substitutions were isolated from four. Deep sequencing analysis confirmed the clonal spread of these mutants.
View Article and Find Full Text PDFMolecular dynamics study on the effect of the N1 neuraminidase double mutant G147R/H274Y on oseltamivir sensitivity.
RSC Adv
December 2024
Bioinformatics Research Group, University-CoE-Research Center for Bio-Molecule Engineering (BIOME), Universitas Airlangga Surabaya 60115 Indonesia.
Inhibition of neuraminidase is the most prominent target in influenza medication using oseltamivir as an inhibitor. However, the emerging resistance of neuraminidase toward oseltamivir due to mutation reduces the efficacy of oseltamivir. The generally reported mutation is a single mutation at H274Y, which declines the sensitivity of oseltamivir by almost 900 folds compared to the wild-type variant.
View Article and Find Full Text PDFElaborate Structural Modifications Yielding Novel Boron-Containing N-Substituted Oseltamivir Derivatives as Potent Neuraminidase Inhibitors with Significantly Improved Broad-Spectrum Antiresistance Profiles.
J Med Chem
December 2024
Department of Medicinal Chemistry, Key Laboratory of Chemical Biology (Ministry of Education), School of Pharmaceutical Sciences, Shandong University, 44 West Culture Road, Jinan, Shandong 250012, P. R. China.
Inspired by our previous finding that targeting the 150-cavity with a multisite-binding strategy emerged as an effective approach to obtain more potent and selective neuraminidase (NA) inhibitors against influenza virus, we present here the design, synthesis, and optimization of novel boron-containing N-substituted oseltamivir (OSC) derivatives. Exploratory structure-activity relationship (SAR) studies led to the identification of compounds and as the most potent NA inhibitors, surpassing OSC in potency against both wild-type group-1 NAs and oseltamivir-resistant NAs. These compounds demonstrated significant antiviral activity against several wild-type strains and H1N1pdm09 strains (EC = 0.
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