Dynamic residue interaction network analysis of the oseltamivir binding site of N1 neuraminidase and its H274Y mutation site conferring drug resistance in influenza A virus.
Introduction: These strains include an oseltamivir carboxylate-resistant strain, where a tyrosine replaces histidine at position 274 in NA, and a zanamivir-resistant strain, where an arginine replaces isoleucine at position 222.
Generation and Characterization of Recombinant Influenza A(H1N1) Viruses Resistant to Neuraminidase Inhibitors.
PMID: 24524021
2013
Osong public health and research perspectives
Result: Compared with the double Chungbuk-Y274H-N295S mutant, triple Chungbuk-Y275H-N295S-I117V, Y275H-N295S-I117M, and Y275H-N295S-I223V mutants also had slightly increased IC50 values for oseltamivir (1.5-fold, 1.3-fold, and 2.4-fold), whereas these mutants were susceptible to zanamivir.
Result: Compared with the single Chungbuk-Y274H mutant, triple Chungbuk-Y275H-E119V-I117V and Y275H-E119V-<
The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo.
Abstract: A substitution of the conserved histidine at position 274 for tyrosine in the NA active site has been selected via site directed mutagenesis, serial passage in culture under drug pressure in H1N1 and during the treatment of experimental H1N1 infection in man.
IV mutation literature information.
PMID: 
2021
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