Ministry of Education, Youth and Sports of the Czech Republic
LM2018127
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ジャーナル: Commun Biol / 年: 2022 タイトル: Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion. 著者: Carina R Büttner / Radovan Spurný / Tibor Füzik / Pavel Plevka / 要旨: Coxsackievirus A6 (CV-A6) has recently overtaken enterovirus A71 and CV-A16 as the primary causative agent of hand, foot, and mouth disease worldwide. Virions of CV-A6 were not identified in previous ...Coxsackievirus A6 (CV-A6) has recently overtaken enterovirus A71 and CV-A16 as the primary causative agent of hand, foot, and mouth disease worldwide. Virions of CV-A6 were not identified in previous structural studies, and it was speculated that the virus is unique among enteroviruses in using altered particles with expanded capsids to infect cells. In contrast, the virions of other enteroviruses are required for infection. Here we used cryo-electron microscopy (cryo-EM) to determine the structures of the CV-A6 virion, altered particle, and empty capsid. We show that the CV-A6 virion has features characteristic of virions of other enteroviruses, including a compact capsid, VP4 attached to the inner capsid surface, and fatty acid-like molecules occupying the hydrophobic pockets in VP1 subunits. Furthermore, we found that in a purified sample of CV-A6, the ratio of infectious units to virions is 1 to 500. Therefore, it is likely that virions of CV-A6 initiate infection, like those of other enteroviruses. Our results provide evidence that future vaccines against CV-A6 should target its virions instead of the antigenically distinct altered particles. Furthermore, the structure of the virion provides the basis for the rational development of capsid-binding inhibitors that block the genome release of CV-A6.
名称: Capsid protein VP1 / タイプ: protein_or_peptide / ID: 1 詳細: The first amino-acid of VP1 in the corresponding section of the GenBank polyprotein entry (AAR38844) (Asn) is not the actual first residue as the proteolytic cleavage of the viral polyprotein ...詳細: The first amino-acid of VP1 in the corresponding section of the GenBank polyprotein entry (AAR38844) (Asn) is not the actual first residue as the proteolytic cleavage of the viral polyprotein occurs at an alternative location, leaving the following residue Asp-2 as the first residue (D-1), and the Asn as the additional C-term residue described for VP3 (N-241), as observed in the virion. コピー数: 1 / 光学異性体: LEVO
名称: Capsid protein VP3 / タイプ: protein_or_peptide / ID: 3 詳細: VP3 has an additional C-terminal residue (N-241) compared to GenBank entry AAR38844 due to alternative cleavage of the polyprotein as observed in the CV-A6 virion (see compound details for molecule 1 VP1). コピー数: 1 / 光学異性体: LEVO