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Published online ahead of print on 5 August 2009 as doi:10.1099/vir.0.013037-0
Journal of General Virology 2009;90:2840.

A more recent version of this article appeared on December 1, 2009 Originally published as JGV in Press, 10.1099/vir.0.013037-0 on August 5, 2009 J Gen Virol (2009), DOI 10.1099/vir.0.013037-0
© 2009 Society for General Microbiology

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Novel virus-associated proteins encoded by UL112-113 of human cytomegalovirus

Shang-Kwei Wang1,4, Cheng-Hui Hu1, Miao-Chan Lu1, Chang-Yih Duh2, Pao-Chi Liao3 and Yu-Chang Tyan3

1 Department of Microbiology, Institute of Medicine, College of Medicine, Kaohsiung Medical University;
2 Asia-Pacific Ocean Research Center, National Sun Yat-sen University;
3 Department of Environmental and Occupational Health, College of Medicine, National Cheng Kung Uni.

4 E-mail: skwang{at}kmu.edu.tw

Evidence suggests that the products of the human cytomegalovirus (HCMV) UL112-113 genes are involved in viral DNA replication during lytic infection. A polyclonal antibody was raised against the UL112 open reading frame (ORF) to characterise its function in detail. Immunoblots utilising the UL112 antibody identified seven distinct protein bands (p20, p26, p28, p34, p43, p50 and p84) expressed during the HCMV infectious cycle. After screening a cDNA library constructed from cells 72 h after infection with HCMV, only four different cDNA protein-producing constructs were obtained, and their ORFs corresponded to p34, p43, p50 and p84, respectively. The proteins p20, p26 and p28 were further shown to be selectively included within mature HCMV particles, virions, non-infectious enveloped particles, and dense bodies. Immunoaffinity protein purification was used to prepare the samples for liquid chromatography coupled to tandem mass spectrometry. This analysis revealed that p20, p26 and p28 were derived from the UL112 ORF most likely through post-translational proteolytic cleavage.

Received 25 April 2009; accepted 31 July 2009.





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