Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1997-12-24
pubmed:abstractText
Envelopment of the hepatitis B virus (HBV) nucleocapsid depends on the large envelope protein L, which is expressed as a transmembrane polypeptide at the endoplasmic reticulum membrane. Previous studies demonstrated that the cytosolic exposure of the N-terminal pre-S domain (174 amino acids) of L was required for virion formation. N-terminal truncations of L up to Arg 103 were tolerated. To map sites in the remaining C-terminal part of pre-S important for virion morphogenesis, a series of 11 L mutants with linker substitutions between Asn 98 and Pro 171 was generated. The mutants formed stable proteins and were secreted in transfected cell cultures, probably as components of subviral hepatitis B surface antigen particles. All four constructs with mutations between Asn 98 and Thr 125 were unable to complement in trans the block in virion formation of an L-negative HBV genome in cotransfected HuH7 cells. These mutants had a transdominant negative effect on virus yield in cotransfections with the wild-type HBV genome. In contrast, all seven mutants with substitutions downstream of Ser 124 were able to envelop the nucleocapsid and to secrete HBV. The sequence between Arg 103 and Ser 124 is highly conserved among different HBV isolates and also between HBV and the woodchuck hepatitis virus. Point mutations in this region introducing alanine residues at conserved positions blocked virion formation, in contrast to mutations at nonconserved residues. These results demonstrate that the pre-S sequence between Arg 103 and Ser 124 has an important function in HBV morphogenesis.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-1522109, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-1629953, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-1893779, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-1992457, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2041095, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2041101, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2304150, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2586518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2676191, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-2885842, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-3039907, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-3683395, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-3787251, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-3981148, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-6180831, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-6492255, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-6621688, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-6842680, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7086958, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7474074, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7736594, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7815496, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7835336, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7892246, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-7925266, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8030212, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8107225, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8131739, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8137119, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8194518, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8207830, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8676448, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-8774681, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-9024817, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-9188617, http://linkedlifedata.com/resource/pubmed/commentcorrection/9371594-9188622
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9350-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:9371594-Alanine, pubmed-meshheading:9371594-Amino Acid Sequence, pubmed-meshheading:9371594-Animals, pubmed-meshheading:9371594-Asparagine, pubmed-meshheading:9371594-Binding Sites, pubmed-meshheading:9371594-COS Cells, pubmed-meshheading:9371594-Gene Deletion, pubmed-meshheading:9371594-Genetic Complementation Test, pubmed-meshheading:9371594-Genome, Viral, pubmed-meshheading:9371594-Hepatitis B Surface Antigens, pubmed-meshheading:9371594-Hepatitis B virus, pubmed-meshheading:9371594-Humans, pubmed-meshheading:9371594-Molecular Sequence Data, pubmed-meshheading:9371594-Mutagenesis, pubmed-meshheading:9371594-Phenotype, pubmed-meshheading:9371594-Proline, pubmed-meshheading:9371594-Protein Precursors, pubmed-meshheading:9371594-Structure-Activity Relationship, pubmed-meshheading:9371594-Tumor Cells, Cultured, pubmed-meshheading:9371594-Viral Envelope Proteins, pubmed-meshheading:9371594-Virion, pubmed-meshheading:9371594-Virus Assembly
pubmed:year
1997
pubmed:articleTitle
A short linear sequence in the pre-S domain of the large hepatitis B virus envelope protein required for virion formation.
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