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Human cytomegalovirus UL138 open reading frame is highly conserved in clinical strains / 中国医学科学杂志(英文版)
Chinese Medical Sciences Journal ; (4): 107-111, 2009.
Article in English | WPRIM | ID: wpr-302639
ABSTRACT
<p><b>OBJECTIVE</b>To investigate the variability of human cytomegalovirus (HCMV) UL138 open reading frame (ORF) in clinical strains.</p><p><b>METHODS</b>HCMV UL138 ORF was amplified by polymerase chain reaction (PCR) and PCR amplification products were sequenced directly, and the data were analyzed in 19 clinical strains.</p><p><b>RESULTS</b>UL138 ORF in all 30 clinical strains was amplified successfully. Compared with that of Toledo strain, the nucleotide and amino acid sequence identities of UL138 ORF in all strains were 97.41% to 99.41% and 98.24% to 99.42%, respectively. All of the nucleotide mutations were substitutions. The spatial structure and post-translational modification sites of UL138 encoded proteins were conserved. The result of phylogenetic tree showed that HCMV UL138 sequence variations were not definitely related with different clinical symptoms.</p><p><b>CONCLUSION</b>HCMV UL138 ORF in clinical strains is high conservation, which might be helpful for UL138 encoded protein to play a role in latent infection of HCMV.</p>
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Viral Proteins / Molecular Sequence Data / Chemistry / Open Reading Frames / Sequence Alignment / Amino Acid Sequence / Classification / Protein Structure, Secondary / Cytomegalovirus Infections Limits: Humans Language: English Journal: Chinese Medical Sciences Journal Year: 2009 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Viral Proteins / Molecular Sequence Data / Chemistry / Open Reading Frames / Sequence Alignment / Amino Acid Sequence / Classification / Protein Structure, Secondary / Cytomegalovirus Infections Limits: Humans Language: English Journal: Chinese Medical Sciences Journal Year: 2009 Type: Article