RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/21768361http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21768361http://www.w3.org/2000/01/rdf-schema#comment"Human cytomegalovirus induces and requires fatty acid synthesis. This suggests an essential role for lipidome remodeling in viral replication. We used mass spectrometry to quantify glycerophospholipids in mock-infected and virus-infected fibroblasts, as well as in virions. Although the lipid composition of mock-infected and virus-infected fibroblasts was similar, virions were markedly different. The virion envelope contained twofold more phosphatidylethanolamines and threefold less phosphatidylserines than the host cell. This indicates that the virus buds from a membrane with a different lipid composition from the host cell as a whole. Compared with published datasets, the virion envelope showed the greatest similarity to the synaptic vesicle lipidome. Synaptosome-associated protein of 25 kDa (SNAP-25) is a component of the complex that mediates exocytosis of synaptic vesicles in neurons; and its homolog, SNAP-23, functions in exocytosis in many other cell types. Infection induced the relocation of SNAP-23 to the cytoplasmic viral assembly zone, and knockdown of SNAP-23 inhibited the production of virus. We propose that cytomegalovirus capsids acquire their envelope by budding into vesicles with a lipid composition similar to that of synaptic vesicles, which subsequently fuse with the plasma membrane to release virions from the cell."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1109796108"xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Shenk T."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Brown H.A."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Rabinowitz J.D."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Liu S.T."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Milne S.B."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Myers D.S."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Ivanova P."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/author"Sharon-Friling R."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/pages"12869-12874"xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/title"Synaptic vesicle-like lipidome of human cytomegalovirus virions reveals a role for SNARE machinery in virion egress."xsd:string
http://purl.uniprot.org/citations/21768361http://purl.uniprot.org/core/volume"108"xsd:string
http://purl.uniprot.org/citations/21768361http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21768361
http://purl.uniprot.org/citations/21768361http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21768361
http://purl.uniprot.org/uniprot/#_A8K287-mappedCitation-21768361http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21768361
http://purl.uniprot.org/uniprot/#_O00161-mappedCitation-21768361http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21768361
http://purl.uniprot.org/uniprot/A8K287http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21768361
http://purl.uniprot.org/uniprot/O00161http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21768361