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Virulent forms of flu have previously caused high levels of mortality globally. To prevent future pandemics, an arsenal of drugs has been stockpiled, but drug-resistance threatens our preparedness. Neuraminidase is a key drug target because it enables influenza virus’ infection. We designed physical models based on overlaid crystal structures of the wild type and His274Tyr neuraminidase mutant to visualize the shift in Glu276 (that inhibits binding to the drug, Tamiflu, but not Relenza) and displayed catalytic residues to demonstrate continued inhibition by Relenza. To best design drugs that are impervious to resistance, innovative approaches based on structural analyses are promising.
