About: Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding

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About: Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding
Creator	Jin, Dong-Yan Fang, Shouguo Wang, Jibin Chen, Bo Xiao, Han Liu, Ding Tam, James
Source	Medline; PMC
abstract	Coronavirus M protein is an essential component of virion and plays pivotal roles in virion assembly, budding and maturation. The M protein is integrated into the viral envelope with three transmembrane domains flanked by a short amino-terminal ectodomain and a large carboxy-terminal endodomain. In this study, we showed co-purification of the M protein from coronavirus infectious bronchitis virus (IBV) with actin. To understand the cellular factors that may be involved in virion assembly, budding and maturation processes, IBV M was used as the bait in a yeast two-hybrid screen, resulting in the identification of β-actin as a potentially interacting partner. This interaction was subsequently confirmed by coimmunoprecipitation and immunofluorescence microscopy in mammalian cells, and mutation of amino acids A159 and K160 on the M protein abolished the interaction. Introduction of the A159-K160 mutation into an infectious IBV clone system blocks the infectivity of the clone, although viral RNA replication and subgenomic mRNA transcription were actively detected. Disruption of actin filaments with cell-permeable agent cytochalasin D at early stages of the infection cycle led to the detection of viral protein synthesis in infected cells but not release of virus particles to the cultured media. However, the same treatment at late stages of the infection cycle did not affect the release of virus particles to the media, suggesting that disruption of the actin filaments might block virion assembly and budding, but not release of the virus particles. This study reveals an essential function of actin in the replication cycle of coronavirus.
has issue date	2009-03-16(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0004908
bibo:pmid	19287488
has license	cc-by
sha1sum (hex)	7379b8c28321b7f9c78d2b4d35109a87b35cf883
schema:url	https://doi.org/10.1371/journal.pone.0004908
resource representing a document's title	Interaction of the Coronavirus Infectious Bronchitis Virus Membrane Protein with β-Actin and Its Implication in Virion Assembly and Budding
has PubMed Central identifier	PMC2653722
has PubMed identifier	19287488
schema:publication	PLoS One
resource representing a document's body	covid:7379b8c28321b7f9c78d2b4d35109a87b35cf883#body_text
is schema:about of	named entity 'replication cycle' named entity 'infection' named entity 'Coronavirus' named entity 'M protein' named entity 'viral envelope' named entity 'assembly' named entity 'M protein' covid:arg/7379b8c28321b7f9c78d2b4d35109a87b35cf883 named entity 'cellular' named entity 'M protein' named entity 'coronavirus' named entity 'Interaction' named entity 'agent' named entity 'led' named entity 'yeast two-hybrid screen' named entity 'actively' named entity 'disruption' named entity 'early stages' named entity 'Budding' named entity 'virion' named entity 'processes' named entity 'Interaction' named entity 'coimmunoprecipitation' named entity 'protein' named entity 'viral envelope' named entity 'virion' named entity 'viral RNA replication' named entity 'coronavirus' named entity 'virus' named entity 'A159' named entity 'virion' named entity 'mutation' named entity 'Assembly and Budding' named entity 'viral' named entity 'block' named entity 'actin' named entity 'primers' named entity 'peroxidase' named entity 'chloroform' named entity 'virions' named entity 'protein' named entity 'IBV' named entity 'SARS-CoV' named entity 'viral envelope proteins' named entity 'MD4' named entity 'subgenomic' named entity 'MD2' named entity 'interact' named entity 'Myc' named entity 'clone' named entity 'MD5' named entity 'protein' named entity 'protein' named entity 'protein' named entity 'actin' named entity 'primers' named entity 'ligated' named entity 'actin' named entity 'protein' named entity 'actin' named entity 'power station' named entity 'nucleocapsid' named entity 'gene' named entity 'Golgi apparatus' named entity 'actin filaments' named entity 'actin' named entity 'supernatants' named entity 'yeast two-hybrid screening' named entity 'transcription' named entity 'actin' named entity 'protein' named entity 'DMSO' named entity 'reverse-transcribed' named entity 'amino acid sequence' named entity 'RNA'

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