Mutations I117V and I117M and Oseltamivir Sensitivity of Pandemic (H1N1) 2009 Viruses
Aeron C. Hurt , Sook Kwan Leang, David J. Speers, Ian G. Barr, and Sebastian Maurer-Stroh
Author affiliations: World Health Organization Collaborating Centre for Reference and Research on Influenza, North Melbourne, Victoria, Australia (A.C. Hurt, S.K. Leang, I.G. Barr); PathWest Laboratory Medicine, Nedlands, Western Australia, Australia (D.J. Speers); Agency for Science, Technology and Research, Singapore (S. Maurer-Stroh); Ministry of Health, Singapore (S. Maurer-Stroh); Nanyang Technological University, Singapore (S. Maurer-Stroh)
Figure 1. Structural details of neuraminidase mutations from pandemic (H1N1) 2009 viruses. A) Wildtype mutation I117 (green). B) mutation I117V (red). C) I117M (blue). All were modeled with FoldX (11) in YASARA (12) in the context of the pandemic (H1N1) 2009 virus neuraminidase crystal structure (Protein Data Bank: 3nss). Side chains of residues <3 Å of residue 117 are shown as sticks. Cavities within the structure (1.4 Å radius water probe) are shown in magenta.
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