| Literature DB >> 32222293 |
Amira F A Hussein1, Han Cheng2, Smanla Tundup3, Aleksandar Antanasijevic4, Elizabeth Varhegyi5, Jasmine Perez6, Eiman M AbdulRahman7, Mervat G Elenany7, Soheir Helal7, Michael Caffrey4, Norton Peet8, Balaji Manicassamy3, Lijun Rong9.
Abstract
Influenza A viruses (IAVs) cause seasonal flu and occasionally pandemics. The current therapeutics against IAVs target two viral proteins - neuraminidase (NA) and M2 ion-channel protein. However, M2 ion channel inhibitors (amantadine and rimantadine) are no longer recommended by CDC for use due to the emergence of high level of antiviral resistance among the circulating influenza viruses, and resistant strains to NA inhibitors (oseltamivir and zanamivir) have also been reported. Therefore, development of novel anti-influenza therapies is urgently needed. As one of the viral surface glycoproteins, hemagglutinin (HA) mediates critical virus entry steps including virus binding to host cells and virus-host membrane fusion, which makes it a potential target for anti-influenza drug development. In this study, we report the identification of compound CBS1116 with a 4-aminopiperidine scaffold from a chemical library screen as an entry inhibitor specifically targeting two group 1 influenza A viruses, A/Puerto Rico/8/34 (H1N1) and recombinant low pathogenic avian H5N1 virus (A/Vietnam/1203/04, VN04Low). Mechanism of action studies show that CBS1116 interferes with the HA-mediated fusion process. Further structure activity relationship study generated a more potent compound CBS1117 which has a 50% inhibitory concentration of 70 nM and a selectivity index of ~4000 against A/Puerto Rico/8/34 (H1N1) infection in human lung epithelial cell line (A549).Entities:
Keywords: Fusion inhibitor; Hemagglutinin; Influenza a viruses; Structure activity relationship; Virus entry
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Year: 2020 PMID: 32222293 PMCID: PMC7243365 DOI: 10.1016/j.antiviral.2020.104782
Source DB: PubMed Journal: Antiviral Res ISSN: 0166-3542 Impact factor: 5.970