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http://purl.uniprot.org/citations/17376925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17376925http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17376925http://www.w3.org/2000/01/rdf-schema#comment"The N-terminal pre-S domain of the large hepatitis B virus (HBV) envelope protein plays a pivotal role at the initial step of the viral entry pathway. In the present study, the entire pre-S domain was mapped for infectivity determinants, following a reverse-genetics approach and using in vitro infection assays with hepatitis delta virus (HDV) or HBV particles. The results demonstrate that lesions created within the N-terminal 75 amino acids of the pre-S region abrogate infectivity, whereas mutations between amino acids 76 and 113, overlapping the matrix domain, had no effect. In contrast to the results of a recent study (L. Stoeckl, A. Funk, A. Kopitzki, B. Brandenburg, S. Oess, H. Will, H. Sirma, and E. Hildt, Proc. Natl. Acad. Sci. 103:6730-6734, 2006), the deletion of a cell membrane translocation motif (TLM) located between amino acids 148 and 161 at the C terminus of pre-S2 did not interfere with the infectivity of the resulting HDV or HBV mutants. Furthermore, a series of large deletions overlapping the pre-S2 domain were compatible with infectivity, although the efficiency of infection was reduced when the deletions extended to the pre-S1 domain. Overall, the results demonstrate that the activity of the pre-S domain at viral entry solely depends on the integrity of its first 75 amino acids and thus excludes any function of the matrix domain or TLM."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00096-07"xsd:string
http://purl.uniprot.org/citations/17376925http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00096-07"xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/author"Sureau C."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/author"Sureau C."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/author"Blanchet M."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/author"Blanchet M."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/pages"5841-5849"xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/pages"5841-5849"xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/title"Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/title"Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues."xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/17376925http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/17376925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17376925
http://purl.uniprot.org/citations/17376925http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17376925
http://purl.uniprot.org/citations/17376925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17376925
http://purl.uniprot.org/citations/17376925http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17376925
http://purl.uniprot.org/uniprot/P03138http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17376925
http://purl.uniprot.org/uniprot/P03138#attribution-37F1C618B039BE3B3F28D9F3FCC23C1Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/17376925