alexa Novel sialic acid derivatives lock open the 150-loop of an influenza A virus group-1 sialidase.
General Science

General Science

Journal of Bioterrorism & Biodefense

Author(s): Rudrawar S, Dyason JC, RameixWelti MA, Rose FJ, Kerry PS,

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Abstract Influenza virus sialidase has an essential role in the virus' life cycle. Two distinct groups of influenza A virus sialidases have been established, that differ in the flexibility of the '150-loop', providing a more open active site in the apo form of the group-1 compared to group-2 enzymes. In this study we show, through a multidisciplinary approach, that novel sialic acid-based derivatives can exploit this structural difference and selectively inhibit the activity of group-1 sialidases. We also demonstrate that group-1 sialidases from drug-resistant mutant influenza viruses are sensitive to these designed compounds. Moreover, we have determined, by protein X-ray crystallography, that these inhibitors lock open the group-1 sialidase flexible 150-loop, in agreement with our molecular modelling prediction. This is the first direct proof that compounds may be developed to selectively target the pandemic A/H1N1, avian A/H5N1 and other group-1 sialidase-containing viruses, based on an open 150-loop conformation of the enzyme.
This article was published in Nat Commun and referenced in Journal of Bioterrorism & Biodefense

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