19846526

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0019185, umls-concept:C0033684, umls-concept:C0392747, umls-concept:C0439855, umls-concept:C0542341, umls-concept:C0596901, umls-concept:C0598312, umls-concept:C0851285, umls-concept:C1554963
pubmed:issue	1
pubmed:dateCreated	2009-12-16
pubmed:abstractText	Positive-strand RNA viruses induce modifications of cytoplasmic membranes to form replication complexes. For coronaviruses, replicase nonstructural protein 4 (nsp4) has been proposed to function in the formation and organization of replication complexes. Murine hepatitis virus (MHV) nsp4 is glycosylated at residues Asn176 (N176) and N237 during plasmid expression of nsp4 in cells. To test if MHV nsp4 residues N176 and N237 are glycosylated during virus replication and to determine the effects of N176 and N237 on nsp4 function and MHV replication, alanine substitutions of nsp4 N176, N237, or both were engineered into the MHV-A59 genome. The N176A, N237A, and N176A/N237A mutant viruses were viable, and N176 and N237 were glycosylated during infection of wild-type (wt) and mutant viruses. The nsp4 glycosylation mutants exhibited impaired virus growth and RNA synthesis, with the N237A and N176A/N237A mutant viruses demonstrating more profound defects in virus growth and RNA synthesis. Electron microscopic analysis of ultrastructure from infected cells demonstrated that the nsp4 mutants had aberrant morphology of virus-induced double-membrane vesicles (DMVs) compared to those infected with wt virus. The degree of altered DMV morphology directly correlated with the extent of impairment in viral RNA synthesis and virus growth of the nsp4 mutant viruses. The results indicate that nsp4 plays a critical role in the organization and stability of DMVs. The results also support the conclusion that the structure of DMVs is essential for efficient RNA synthesis and optimal replication of coronaviruses.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/R01 AI050083-06A2, http://linkedlifedata.com/resource/pubmed/grant/R01 AI050083-07
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0113724
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ns4 protein, mouse hepatitis virus, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral, http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins
pubmed:status	MEDLINE
pubmed:month	Jan
pubmed:issn	1098-5514
pubmed:author	pubmed-author:BeachboardDia CDC, pubmed-author:CoxReagan GRG, pubmed-author:DenisonMark RMR, pubmed-author:DoyleJoshua DJD, pubmed-author:GadlageMark JMJ, pubmed-author:SparksJennifer SJS, pubmed-author:StobartChristopher CCC
pubmed:issnType	Electronic
pubmed:volume	84
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	280-90
pubmed:dateRevised	2010-12-3
pubmed:meshHeading	pubmed-meshheading:19846526-Coronaviridae, pubmed-meshheading:19846526-Glycosylation, pubmed-meshheading:19846526-Intracellular Membranes, pubmed-meshheading:19846526-Microscopy, Electron, pubmed-meshheading:19846526-Murine hepatitis virus, pubmed-meshheading:19846526-Mutant Proteins, pubmed-meshheading:19846526-Mutation, Missense, pubmed-meshheading:19846526-RNA, Viral, pubmed-meshheading:19846526-Viral Nonstructural Proteins, pubmed-meshheading:19846526-Virus Replication
pubmed:year	2010
pubmed:articleTitle	Murine hepatitis virus nonstructural protein 4 regulates virus-induced membrane modifications and replication complex function.
pubmed:affiliation	Department of Pediatrics, Vanderbilt University Medical Center, D6217 MCN, 1161 21st Ave. S., Nashville, TN 37232-2581. mark.denison@vanderbilt.edu.
pubmed:publicationType	Journal Article