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© Nadia Naffakh, Institut Pasteur
Immunofluorescence detection of influenza virus nucleoprotein in infected cells
Publication : Nature communications

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nature communications - 16 Nov 2010

Rudrawar S, Dyason JC, Rameix-Welti MA, Rose FJ, Kerry PS, Russell RJ, van der Werf S, Thomson RJ, Naffakh N, von Itzstein M

Link to Pubmed [PMID] – 21081911

Nat Commun 2010 Nov;1:113

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.

https://www.ncbi.nlm.nih.gov/pubmed/21081911