Potent peptidic fusion inhibitors of influenza virus

We report here on the design and structural characterization of potent peptidic inhibitors of influenza hemagglutinin. The peptide design was based on complementarity-determining region loops of human broadly neutralizing antibodies against the hemagglutinin (FI6v3 and CR9114). The optimized peptides exhibit nanomolar affinity and neutralization against influenza A group 1 viruses, including the 2009 H1N1 pandemic and avian H5N1 strains. The peptide inhibitors bind to the highly conserved stem epitope and block the low pH–induced conformational rearrangements associated with membrane fusion. These peptidic compounds and their advantageous biological properties should accelerate the development of new small molecule– and peptide-based therapeutics against influenza virus.

Source: ScienceNOW - October 26, 2017 Category: Science Authors: Kadam, R. U., Juraszek, J., Brandenburg, B., Buyck, C., Schepens, W. B. G., Kesteleyn, B., Stoops, B., Vreeken, R. J., Vermond, J., Goutier, W., Tang, C., Vogels, R., Friesen, R. H. E., Goudsmit, J., van Dongen, M. J. P., Wilson, I. A. Tags: Biochemistry, Epidemiology r-articles Source Type: news