Research Support, Non-U.S. Gov't
- Requirement of the N-terminal residues of human cytomegalovirus UL112-113 proteins for viral growth and oriLyt-dependent DNA replication
-
Young-Eui Kim , Mi Young Park , Kyeong Jin Kang , Tae Hee Han , Chan Hee Lee , Jin-Hyun Ahn
-
J. Microbiol. 2015;53(8):561-569. Published online July 31, 2015
-
DOI: https://doi.org/10.1007/s12275-015-5301-3
-
-
50
View
-
0
Download
-
5
Crossref
-
Abstract
-
The UL112-113 region of the human cytomegalovirus (HCMV)
genome encodes four phosphoproteins of 34, 43, 50, and 84
kDa that promote viral DNA replication. Co-transfection
assays have demonstrated that self-interaction of these proteins
via the shared N-termini is necessary for their intranuclear
distribution as foci and for the efficient relocation
of a viral DNA polymerase processivity factor (UL44) to the
viral replication sites. However, the requirement of UL112-
113 N-terminal residues for viral growth and DNA replication
has not been fully elucidated. Here, we investigated
the effect of deletion of the N-terminal regions of UL112-
113 proteins on viral growth and oriLyt-dependent DNA
replication. A deletion of the entire UL112 region or the region
encoding the 25 N-terminal amino-acid residues from
the HCMV (Towne strain) bacmid impaired viral growth
in bacmid-transfected human fibroblast cells, indicating their
requirement for viral growth. In co-immunoprecipitation
assays using the genomic gene expressing the four UL112-
113 proteins together, the 25 N-terminal amino-acid residues
were found to be necessary for stable expression of UL112-
113 proteins and their self-interaction. These residues were
also required for efficient binding to and relocation of UL44,
but not for interaction with IE2, an origin-binding transcription
factor. In co-transfection/replication assays, replication
of the oriLyt-containing plasmid was promoted by
expression of intact UL112-113 proteins, but not by the expression
of 25-amino-acid residue-deleted proteins. Our
results
demonstrate that the 25 N-terminal amino-acid residues
of UL112-113 proteins that mediate self-interaction
contribute to viral growth by promoting their binding to
UL44 and the initiation of oriLyt-dependent DNA replication.
-
Citations
Citations to this article as recorded by

- Insights into the Transcriptome of Human Cytomegalovirus: A Comprehensive Review
Janine Zeng, Di Cao, Shaomin Yang, Dabbu Kumar Jaijyan, Xiaolian Liu, Songbin Wu, Ruth Cruz-Cosme, Qiyi Tang, Hua Zhu
Viruses.2023; 15(8): 1703. CrossRef - The human cytomegalovirus decathlon: Ten critical replication events provide opportunities for restriction
Declan L. Turner, Rommel A. Mathias
Frontiers in Cell and Developmental Biology.2022;[Epub] CrossRef - Degradation of SAMHD1 Restriction Factor Through Cullin-Ring E3 Ligase Complexes During Human Cytomegalovirus Infection
Seokhwan Hyeon, Myoung Kyu Lee, Young-Eui Kim, Gwang Myeong Lee, Jin-Hyun Ahn
Frontiers in Cellular and Infection Microbiology.2020;[Epub] CrossRef - Primary lymphocyte infection models for KSHV and its putative tumorigenesis mechanisms in B cell lymphomas
Sangmin Kang, Jinjong Myoung
Journal of Microbiology.2017; 55(5): 319. CrossRef - Differential Requirement of Human Cytomegalovirus UL112-113 Protein Isoforms for Viral Replication
Tim Schommartz, Jiajia Tang, Rebekka Brost, Wolfram Brune, Klaus Frueh
Journal of Virology.2017;[Epub] CrossRef