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Characterization of human cytomegalovirus UL145 and UL136 genes in low-passage clinical isolates from infected Chinese infants.

Wang B, Hu JJ, Yan CF, Su HH, Ding JC, Guo YY, Ye N, Zhang SQ, Zhang XZ, Zhou SF - Med. Sci. Monit. (2011)

Bottom Line: The mRNA expression of both UL145 and UL136 was confirmed by reverse transcription (RT-PCR) assays.Both UL145 and UL136 are highly conserved.UL145 may act as an intranuclear regulating factor by direct binding to DNA, while UL136 may be a membrane receptor involving signal transduction.

View Article: PubMed Central - PubMed

Affiliation: Department of Pediatrics, Guangdong Women and Children's Hospital, Guangzhou, China. gzwbo@yahoo.com.cn

ABSTRACT

Background: Human cytomegalovirus (HCMV) is a leading cause of morbidity and mortality in immunocompromised individuals. The unique long b' (ULB') region of HCMV contains at least 19 open reading frames (ORFs); however, little is known about the function of UL145 and UL136. We characterized UL145 and UL136 in low-passage clinical isolates from Chinese infants.

Material/methods: The clinical strains of HCMV were recovered from the urine from HCMV-infected infants. Human embryonic lung fibroblasts (HELFs) were infected with clinical isolates of HCMV, and the viral DNA and mRNA for UL145 and UL136 were analyzed by polymerase chain reaction (PCR) and sequencing techniques. We also predicted the structure and function of UL145 and UL136 proteins.

Results: Sixty-two Chinese infants infected with HCMV were recruited into this study and the clinical isolates were recovered from the urine. Two strains among the low-passage isolates, D2 and D3, were obtained. The UL145 and UL136 sequences were deposited with GenBank under accession numbers of DQ180367, DQ180381, DQ180377, and DQ180389. The mRNA expression of both UL145 and UL136 was confirmed by reverse transcription (RT-PCR) assays. UL145 was predicted to contain 1 protein kinase C phosphorylation site, 2 casein kinase II phosphorylation sites and a zinc finger structure. UL136 was predicted to contain a protein kinase C phosphorylation site, N-myristoylation site, cAMP- and cGMP-dependent protein kinase phosphorylation site and tyrosine kinase II phosphorylation site. Both UL145 and UL136 are highly conserved.

Conclusions: UL145 may act as an intranuclear regulating factor by direct binding to DNA, while UL136 may be a membrane receptor involving signal transduction.

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Related in: MedlinePlus

Comparison of the open reading frame (ORF) of the UL145 gene among various strains.
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f3-medscimonit-17-8-cr423: Comparison of the open reading frame (ORF) of the UL145 gene among various strains.

Mentions: The UL145 open reading frame (ORF) sequence of D2 and D3 strains had high homology with 10 strains from GenBank, including T9, T8, 9J, 20M, T27, T49, U253, 8J, T25 and T50 (Figure 3). The UL136 ORF sequence of D2 and D3 showed high homology with 11 strains (4J, 51C, 39J, 33J, 63J, 22M, 10J, 32C, 29C, 27C, and Toledo) (Figure 4).


Characterization of human cytomegalovirus UL145 and UL136 genes in low-passage clinical isolates from infected Chinese infants.

Wang B, Hu JJ, Yan CF, Su HH, Ding JC, Guo YY, Ye N, Zhang SQ, Zhang XZ, Zhou SF - Med. Sci. Monit. (2011)

Comparison of the open reading frame (ORF) of the UL145 gene among various strains.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3539624&req=5

f3-medscimonit-17-8-cr423: Comparison of the open reading frame (ORF) of the UL145 gene among various strains.
Mentions: The UL145 open reading frame (ORF) sequence of D2 and D3 strains had high homology with 10 strains from GenBank, including T9, T8, 9J, 20M, T27, T49, U253, 8J, T25 and T50 (Figure 3). The UL136 ORF sequence of D2 and D3 showed high homology with 11 strains (4J, 51C, 39J, 33J, 63J, 22M, 10J, 32C, 29C, 27C, and Toledo) (Figure 4).

Bottom Line: The mRNA expression of both UL145 and UL136 was confirmed by reverse transcription (RT-PCR) assays.Both UL145 and UL136 are highly conserved.UL145 may act as an intranuclear regulating factor by direct binding to DNA, while UL136 may be a membrane receptor involving signal transduction.

View Article: PubMed Central - PubMed

Affiliation: Department of Pediatrics, Guangdong Women and Children's Hospital, Guangzhou, China. gzwbo@yahoo.com.cn

ABSTRACT

Background: Human cytomegalovirus (HCMV) is a leading cause of morbidity and mortality in immunocompromised individuals. The unique long b' (ULB') region of HCMV contains at least 19 open reading frames (ORFs); however, little is known about the function of UL145 and UL136. We characterized UL145 and UL136 in low-passage clinical isolates from Chinese infants.

Material/methods: The clinical strains of HCMV were recovered from the urine from HCMV-infected infants. Human embryonic lung fibroblasts (HELFs) were infected with clinical isolates of HCMV, and the viral DNA and mRNA for UL145 and UL136 were analyzed by polymerase chain reaction (PCR) and sequencing techniques. We also predicted the structure and function of UL145 and UL136 proteins.

Results: Sixty-two Chinese infants infected with HCMV were recruited into this study and the clinical isolates were recovered from the urine. Two strains among the low-passage isolates, D2 and D3, were obtained. The UL145 and UL136 sequences were deposited with GenBank under accession numbers of DQ180367, DQ180381, DQ180377, and DQ180389. The mRNA expression of both UL145 and UL136 was confirmed by reverse transcription (RT-PCR) assays. UL145 was predicted to contain 1 protein kinase C phosphorylation site, 2 casein kinase II phosphorylation sites and a zinc finger structure. UL136 was predicted to contain a protein kinase C phosphorylation site, N-myristoylation site, cAMP- and cGMP-dependent protein kinase phosphorylation site and tyrosine kinase II phosphorylation site. Both UL145 and UL136 are highly conserved.

Conclusions: UL145 may act as an intranuclear regulating factor by direct binding to DNA, while UL136 may be a membrane receptor involving signal transduction.

Show MeSH
Related in: MedlinePlus