| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6142654 | Virus Research | 2014 | 6 Pages |
Abstract
The UL133-UL138 locus in the unique long bâ² (ULbâ²) region of the human cytomegalovirus (HCMV) genome is considered to play certain roles in viral replication, dissemination and latency in a host cell type-dependent manner. Here we characterized the proteins encoded by UL136, one of the open reading frames (ORFs) in the locus. Comparative sequence analysis of UL136 among clinical isolates and laboratory strains indicates that its predicted amino-acid sequence is highly conserved. A polyclonal antibody against UL136 proteins (pUL136s) was raised against its carboxy-terminal region and this antibody specifically recognized at least five UL136-encoded protein isoforms of 29-17Â kDa both in HCMV-infected cells and in cells transfected with a construct expressing pUL136. Immunofluorescence analysis with this antibody revealed localization of pUL136 in the Golgi apparatus. Analysis of several pUL136 mutants indicated that the putative transmembrane domain of pUL136 is required for its Golgi localization. Mutational analysis of multiple AUG codons in UL136 demonstrated that translation initiation from these AUG codons contributes in the generation of pUL136 isoforms.
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Authors
Huanan Liao, Jung-Hyun Lee, Rikita Kondo, Marei Katata, Ken-Ichi Imadome, Kenji Miyado, Naoki Inoue, Shigeyoshi Fujiwara, Hiroyuki Nakamura,