rdf:type |
|
lifeskim:mentions |
umls-concept:C0007673,
umls-concept:C0011220,
umls-concept:C0017262,
umls-concept:C0057317,
umls-concept:C0162735,
umls-concept:C0185117,
umls-concept:C0205314,
umls-concept:C0370215,
umls-concept:C0392747,
umls-concept:C0679622,
umls-concept:C1880355,
umls-concept:C2911684
|
pubmed:dateCreated |
1993-10-18
|
pubmed:abstractText |
None of the mutations so far discovered in several hepatitis delta virus (HDV) isolates appears to determine important changes in HDV specific protein (HDAg) expression, except for a putative mutation at nucleotide 1012 converting an amber stop codon (TAG) to a codon for tryptophan (TGG). Here we present the characterization of an HDV obtained from the liver of a woodchuck inoculated with sera from fulminant HDV patients in Central African Republic (CAR). By restriction enzyme analysis and sequencing of HDAg-coding region cDNA clones, we found that this HDV isolate bears a novel mutation (T to A) at nucleotide 1013 which converts the amber stop codon (TAG) to a codon for lysine (AAG). Comparison of these nucleotide sequences with those available from American, Japanese, Taiwanese, French, Italian and Nauru isolates showed a variability of 1.7 to 21.5% and 1.9 to 28.7% at the nucleic acid and amino acid levels, respectively. The HDAg-encoding sequence of the CAR isolate is closely related to that of the Italian HDV isolate. The in vitro expression of this HDV isolate resulted in a unique HDAg species (28K) which was identical with that characterized in vivo.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0022-1317
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
74 ( Pt 9)
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1827-35
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:8376962-Amino Acid Sequence,
pubmed-meshheading:8376962-Animals,
pubmed-meshheading:8376962-Antigens, Viral,
pubmed-meshheading:8376962-Base Sequence,
pubmed-meshheading:8376962-Blotting, Northern,
pubmed-meshheading:8376962-Blotting, Southern,
pubmed-meshheading:8376962-Central African Republic,
pubmed-meshheading:8376962-Cloning, Molecular,
pubmed-meshheading:8376962-DNA, Viral,
pubmed-meshheading:8376962-Hepatitis Delta Virus,
pubmed-meshheading:8376962-Hepatitis delta Antigens,
pubmed-meshheading:8376962-Humans,
pubmed-meshheading:8376962-Liver,
pubmed-meshheading:8376962-Marmota,
pubmed-meshheading:8376962-Molecular Sequence Data,
pubmed-meshheading:8376962-Open Reading Frames,
pubmed-meshheading:8376962-Point Mutation,
pubmed-meshheading:8376962-Polymerase Chain Reaction,
pubmed-meshheading:8376962-RNA, Viral,
pubmed-meshheading:8376962-Restriction Mapping,
pubmed-meshheading:8376962-Sequence Homology, Amino Acid,
pubmed-meshheading:8376962-Sequence Homology, Nucleic Acid
|
pubmed:year |
1993
|
pubmed:articleTitle |
Discovery of a novel point mutation changing the HDAg expression of a hepatitis delta virus isolate from Central African Republic.
|
pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale (INSERM) U 271, Lyon, France.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|