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Structure of avian influenza hemagglutinin in complex with a small molecule entry inhibitor
Journal article   Open access   Peer reviewed

Structure of avian influenza hemagglutinin in complex with a small molecule entry inhibitor

Aleksandar Antanasijevic, Matthew A. Durst, Han Cheng, Irina N. Gaisina, Jasmine T. Perez, Balaji Manicassamy, Lijun Rong, Arnon Lavie and Michael Caffrey
Life science alliance, Vol.3(8), p.e202000724
08/01/2020
DOI: 10.26508/lsa.202000724
PMCID: PMC7335401
PMID: 32611549
url
https://doi.org/10.26508/lsa.202000724View
Published (Version of record) Open Access

Abstract

HA plays a critical role in influenza infection and, thus HA is a potential target for antivirals. Recently, our laboratories have described a novel fusion inhibitor, termed CBS1117, with EC50 similar to 3 mu M against group 1 HA. In this work, we characterize the binding properties of CBS1117 to avian H5 HA by x-ray crystallography, NMR, and mutagenesis. The x-ray structure of the complex shows that the compound binds near the HA fusion peptide, a region that plays a critical role in HA-mediated fusion. NMR studies demonstrate binding of CBS1117 to H5 HA in solution and show extensive hydrophobic contacts between the compound and HA surface. Mutagenesis studies further support the location of the compound binding site proximal to the HA fusion peptide and identify additional amino acids that are important to compound binding. Together, this work gives new insights into the CBS1117 mechanism of action and can be exploited to further optimize this compound and better understand the group specific activity of small-molecule inhibitors of HA-mediated entry.
Biology Life Sciences & Biomedicine Life Sciences & Biomedicine - Other Topics Science & Technology

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