Enterovirus particles expel capsid pentamers to enable genome release

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Publikace nespadá pod Ekonomicko-správní fakultu, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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BUCHTA David FÜZIK Tibor HREBÍK Dominik LEVDANSKY Yevgen SUKENÍK Lukáš MUKHAMEDOVA Liya MORAVCOVÁ Jana VÁCHA Robert PLEVKA Pavel

Rok publikování 2019
Druh Článek v odborném periodiku
Časopis / Zdroj Nature Communications
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.nature.com/articles/s41467-019-09132-x.pdf
Doi http://dx.doi.org/10.1038/s41467-019-09132-x
Klíčová slova MOLECULAR-DYNAMICS; CONFORMATIONAL-CHANGES; FORCE-FIELD; CELL ENTRY; POLIOVIRUS; VIRUS; RNA; MODEL; TRANSITIONS; RECOGNITION
Popis Viruses from the genus Enterovirus are important human pathogens. Receptor binding or exposure to acidic pH in endosomes converts enterovirus particles to an activated state that is required for genome release. However, the mechanism of enterovirus uncoating is not well understood. Here, we use cryo-electron microscopy to visualize virions of human echovirus 18 in the process of genome release. We discover that the exit of the RNA from the particle of echovirus 18 results in a loss of one, two, or three adjacent capsid-protein pentamers. The opening in the capsid, which is more than 120 A in diameter, enables the release of the genome without the need to unwind its putative double-stranded RNA segments. We also detect capsids lacking pentamers during genome release from echovirus 30. Thus, our findings uncover a mechanism of enterovirus genome release that could become target for antiviral drugs.
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