Consecutive influenza surveillance of neuraminidase mutations and neuraminidase inhibitor resistance in Japan.
PMID: 30548432
2019
Influenza and other respiratory viruses
Abstract: Even in Japan, no spread of NAI-resistant viruses has been observed, and A/H1N1pdm09 viruses carrying H275Y remain limited.
Abstract: Four of the five mutations in the catalytic sites of A/H1N1pdm09 consisted of H275Y, which was related to high resistance to oseltamivir and peramivir.
Introduction: These NAIs exert their antiviral function by binding to the enzymatic catalytic sites of influenza surface protein NA.1 In the 2007-2008, oseltamivir-resistant seasonal A/H1N1 viruses carrying NA amino acid (AA) mutation Result: With regard to the substantial RI/HRI-related AA mutations detected in this study, four A/H1N1pdm09 viruses displaying HRI by oseltamivir and RI by peramivir contained H275Y mutations.
Molecular characterization of influenza A(H1N1)pdm09 in Cameroon during the 2014-2016 influenza seasons.
Result: None of the strains possessed the H275Y mutation that has been reported clinically to cause highly reduced inhibition to NAIs.
Discussion: These results are however different from that noted on H1N1 strains collected between 2007 and 2008 from Cameroon in which the H275Y mutation peculiar of resistance to NAIs was observed despite the non-exposition to this antiviral.
Effect of influenza H1N1 neuraminidase V116A and I117V mutations on NA activity and sensitivity to NA inhibitors.
Abstract: The efficiencies of NAs with E119A, H275Y, and N295S mutations to catalyze all substrates were ~19.4% of the CA/04 NA.
Abstract: We compared the impact of V116A and I117V on the functional properties of NA and compared these mutations with that of previously reported NAI-resistant mutations, E119A, H275Y, and N295S.
Superb Specific, Ultrasensitive, and Rapid Identification of the Oseltamivir-Resistant H1N1 Virus: Naked-Eye and SERS Dual-Mode Assay Using Functional Gold Nanoparticles.
Abstract: By measuring the SERS signals, we could detect the pH1N1/H275Y mutant virus with a detection limit of 10 PFU.
Abstract: Herein, we report specific and ultrasensitive detection of oseltamivir-resistant (pH1N1/H275Y mutant) virus using functional Au nanoparticles (NPs).
Abstract: Importantly, the pH1N1/H275Y mutant virus could be detected by using the functional Au NPs even in a mixture of mutant and wild-type viruses with a ratio of 1/100.
Abstract: OHT is an excellent receptor for the pH1N1/H275Y mutant virus because it has a 250-fold higher binding affinity for the pH1N1/H275Y mutant virus than for the wild-type virus.
Abstract: Only in the presence of the pH1N1/H275Y mutant
Diagnosis of Tamiflu-Resistant Influenza Virus in Human Nasal Fluid and Saliva Using Surface-Enhanced Raman Scattering.
Abstract: By combining SERS-active urchin Au nanoparticles and oseltamivir hexylthiol, an excellent receptor for the pH1N1/H275Y mutant virus, we detected the pH1N1/H275Y virus specifically and sensitively in human saliva and nasal fluid samples.
Antiviral Activity of Benzoic Acid Derivative NC-5 Against Influenza A Virus and Its Neuraminidase Inhibition.
PMID: 31842256
2019
International journal of molecular sciences
Result: As in the case of H1N1-H275Y, the inhibition rate of NC-5 at 80 muM was 72.9%, while that of OC was only 4.0% (Figure 3F).
Result: As shown in Figure 5E and Figure 6E, severe hyperemia appeared in the alveolar walls, and the spaces between the alveolar walls were filled with moderate inflammatory infiltrates of neutrophils, macrophages and lymphocytes in the H1N1 and H1N1-H275Y virus-infected models as well as in mice given OS following infection with H1N1-H275Y.
Result: Effective Protection by NC-5 in Mice Infected with Influenza Virus A/FM/1/47 (H1N1) and Oseltamivir-Resistant Mutant A/FM/1/47 (H1N1-H275Y)
Result: Effective Protection by NC-5 in Mice Infected with Influenza Virus A/FM/1/47 (H1N1) and Oseltamivir-Resistant Mutant A/FM/1/47 (H1N1-H275Y).
Result: Examples include NA H275Y in the pre-2009-pandemic H1N1 lineage and M2 S31 N in the majority of currently circulating seasonal influenza viruses as well as other viruses.
Kinetic, Thermodynamic, and Structural Analysis of Drug Resistance Mutations in Neuraminidase from the 2009 Pandemic Influenza Virus.
Abstract: Combination of H275Y with an I223V or S247N mutation results in extreme impairment of oseltamivir's inhibition potency.
Abstract: In contrast, the major oseltamivir resistance mutation H275Y causes a significant decrease in the enzyme's ability to bind this drug.
Abstract: Our crystal structures also helped explain the augmenting effect on resistance of combining H275Y with both substitutions.
Abstract: Our structural analyses revealed that the H275Y substitution has a major effect on the oseltamivir binding pose within the active site while the influence of other studied mutations is much less prominent.
Abstract: The resistance substitutions I223V and S247N, alone or in comb
Neuraminidase inhibitor susceptibility profile of human influenza viruses during the 2016-2017 influenza season in Mainland China.
PMID: 29866491
2018
Journal of infection and chemotherapy
Abstract: The most common neuraminidase (NA) amino acid substitution was H275Y in A (H1N1)pdm09 virus, which confers HRI by oseltamivir.
Influenza A/H3N2 virus infection in immunocompromised ferrets and emergence of antiviral resistance.