Herpesvirus UL11/UL32 / Herpesvirus large structural phosphoprotein UL32 / Small capsid protein, Herpesviridae / Small capsid protein of Herpesviridae / Herpesvirus capsid shell protein 1 / Herpesvirus capsid shell protein VP19C / Herpesvirus capsid protein 2 / Herpesvirus VP23 like capsid protein / Herpesvirus major capsid protein / Herpesvirus major capsid protein, upper domain superfamily / Herpes virus major capsid protein 類似検索 - ドメイン・相同性
Large structural phosphoprotein / Triplex capsid protein 2 / Major capsid protein / Triplex capsid protein 1 / Small capsomere-interacting protein 類似検索 - 構成要素
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE028583/DE025567
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI094386
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1U24GM116792
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1S10OD018111
米国
National Science Foundation (NSF, United States)
DBI-1338135, DMR-1548924
米国
引用
ジャーナル: Nat Commun / 年: 2021 タイトル: Structure of human cytomegalovirus virion reveals host tRNA binding to capsid-associated tegument protein pp150. 著者: Yun-Tao Liu / David Strugatsky / Wei Liu / Z Hong Zhou / 要旨: Under the Baltimore nucleic acid-based virus classification scheme, the herpesvirus human cytomegalovirus (HCMV) is a Class I virus, meaning that it contains a double-stranded DNA genome-and no RNA. ...Under the Baltimore nucleic acid-based virus classification scheme, the herpesvirus human cytomegalovirus (HCMV) is a Class I virus, meaning that it contains a double-stranded DNA genome-and no RNA. Here, we report sub-particle cryoEM reconstructions of HCMV virions at 2.9 Å resolution revealing structures resembling non-coding transfer RNAs (tRNAs) associated with the virion's capsid-bound tegument protein, pp150. Through deep sequencing, we show that these RNA sequences match human tRNAs, and we built atomic models using the most abundant tRNA species. Based on our models, tRNA recruitment is mediated by the electrostatic interactions between tRNA phosphate groups and the helix-loop-helix motif of HCMV pp150. The specificity of these interactions may explain the absence of such tRNA densities in murine cytomegalovirus and other human herpesviruses.