The entry of enveloped viruses requires the fusion of viral and host cell membranes. An effective fusion inhibitor aiming at impeding such membrane fusion may emerge as a broad-spectrum antiviral agent against a wide range of viral infections. Mycobacterium survives inside the phagosome by inhibiting phagosome-lysosome fusion with the help of a coat protein, coronin 1. Structural analysis of coronin 1 and other WD40-repeat proteins suggest that the trp-asp (WD) sequence is placed at distorted β-meander motif (more exposed) in coronin 1. The unique structural feature of coronin 1 was explored to identify a simple lipo-peptide (myr-WD),[1] which effectively inhibits membrane fusion by modulating the interfacial order, water penetration and surface potential. The mycobacterium inspired lipo-dipeptide was successfully tested to combat type 1 influenza virus (H1N1) and murine coronavirus infections as a ‘potential broad-spectrum’ antiviral agent.

Translation of Mycobacterium Survival Strategy to Develop a Lipo-peptide based Fusion Inhibitor

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27th CRSI National Symposium in Chemistry

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