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Viral structural proteins as targets for antivirals
Christopher John Schlicksup 1 , Adam Zlotnick 2
Affiliations
Affiliations
1
Molecular and Cellular Biology Department, Indiana University-Bloomington, Bloomington, IN 47401, United States.
2
Molecular and Cellular Biology Department, Indiana University-Bloomington, Bloomington, IN 47401, United States. Electronic address: [email protected].
PMID: 32777753 DOI: 10.1016/j.coviro.2020.07.001
Abstract
Viral structural proteins are emerging as effective targets for new antivirals. In a viral lifecycle, the capsid must assemble, disassemble, and respond to host proteins, all at the right time and place. These reactions work within a narrow range of conditions, making them susceptible to small molecule interference. In at least three specific viruses, this approach has had met with preliminary success. In rhinovirus and poliovirus, compounds like pleconaril bind capsid and block RNA release. Bevirimat binds to Gag protein in HIV, inhibiting maturation. In Hepatitis B virus, core protein allosteric modulators (CpAMs) promote spontaneous assembly of capsid protein leading to empty and aberrant particles. Despite the biological diversity between viruses and the chemical diversity between antiviral molecules, we observe common features in these antivirals' mechanisms of action. These approaches work by stabilizing protein-protein interactions.
Copyright © 2020 Elsevier B.V. All rights reserved.
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发表于 2020-8-12 16:23