Abstract:
:Oseltamivir (Tamiflu) is the preferred anti-viral drug employed to fight the flu virus in infected individuals. The principal target for this drug is a virus surface glycoprotein, neuraminidase (NA), which facilitates the release of nascent virus and thus spreads infections. Until recently, only a low prevalence of neuraminidase inhibitors (NAIs) resistance (<1%) had been detected in circulating viruses. However, there have been reports of significant numbers of A (H1N1) influenza strains with a H274Y neuraminidase mutation that was highly resistant to the NAI, oseltamivir. In this study, we highlight the effect of point mutation-induced oseltamivir resistance in H1N1 subtype neuraminidases by molecular docking and molecular dynamics simulation approach. Our results suggested that wild-type NA could be more indispensable for the oseltamivir binding, as characterized by minimum number of H-bonds, high flexibility and largest binding affinity than mutant-type NA. This study throws light on the possible effects of drug-resistant mutations on the large functionally important collective motions in biological systems.
journal_name
Appl Biochem Biotechnoljournal_title
Applied biochemistry and biotechnologyauthors
Karthick V,Shanthi V,Rajasekaran R,Ramanathan Kdoi
10.1007/s12010-012-9687-7subject
Has Abstractpub_date
2012-05-01 00:00:00pages
237-49issue
2eissn
0273-2289issn
1559-0291journal_volume
167pub_type
杂志文章abstract::Sugarcane bagasse samples were pretreated with ozone via atmospheric O2 pressure plasma. A delignification efficiency of approximately 80 % was observed within 6 h of treatment. Some hemicelluloses were removed, and the cellulose was not affected by ozonolysis. The quantity of moisture in the bagasse had a large influ...
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更新日期:2012-11-01 00:00:00
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