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http://purl.uniprot.org/citations/19656886http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19656886http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19656886http://www.w3.org/2000/01/rdf-schema#comment"Borna disease virus (BDV), the prototypic member of the Bornaviridae family within the order Mononegavirales, exhibits high neurotropism and provides an important and unique experimental model system for studying virus-cell interactions within the central nervous system. BDV surface glycoprotein (G) plays a critical role in virus cell entry via receptor-mediated endocytosis, and therefore, G is a critical determinant of virus tissue and cell tropism. However, the specific cell pathways involved in BDV cell entry have not been determined. Here, we provide evidence that BDV uses a clathrin-mediated, caveola-independent cell entry pathway. We also show that BDV G-mediated fusion takes place at an optimal pH of 6.0 to 6.2, corresponding to an early-endosome compartment. Consistent with this finding, BDV cell entry was Rab5 dependent but Rab7 independent and exhibited rapid fusion kinetics. Our results also uncovered a key role for microtubules in BDV cell entry, whereas the integrity and dynamics of actin cytoskeleton were not required for efficient cell entry of BDV."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00990-09"xsd:string
http://purl.uniprot.org/citations/19656886http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00990-09"xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/author"de la Torre J.C."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/author"de la Torre J.C."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/author"Clemente R."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/author"Clemente R."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/pages"10406-10416"xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/pages"10406-10416"xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/title"Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/title"Cell entry of Borna disease virus follows a clathrin-mediated endocytosis pathway that requires Rab5 and microtubules."xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/volume"83"xsd:string
http://purl.uniprot.org/citations/19656886http://purl.uniprot.org/core/volume"83"xsd:string
http://purl.uniprot.org/citations/19656886http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19656886
http://purl.uniprot.org/citations/19656886http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19656886
http://purl.uniprot.org/citations/19656886http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19656886
http://purl.uniprot.org/citations/19656886http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19656886
http://purl.uniprot.org/uniprot/Q8BB27http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/19656886
http://purl.uniprot.org/uniprot/Q8BB27#attribution-82CFF5AC13ED553ACBC9758AB52168F8http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/19656886