Journal
MEDICAL MICROBIOLOGY AND IMMUNOLOGY
Volume 200, Issue 3, Pages 203-208Publisher
SPRINGER
DOI: 10.1007/s00430-011-0196-z
Keywords
Herpes simplex virus 1; UL14; Yeast two-hybrid; Co-localization; Co-immunoprecipitation
Categories
Funding
- Chinese Academy of Sciences [20071010-141]
- National Natural Science Foundation of China [30870120, 30900059, 81000736]
- Major State Basic Research Development Program of China [2010CB530105, 2011CB504802]
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The UL14 protein of herpes simplex virus type 1 (HSV-1) is highly conserved in herpesvirus family. However, its exact function during the HSV-1 replication cycle is little known. In the present study, a high throughput yeast two-hybrid system was employed to screen the cellular factors interacting with UL14, and five target candidates were yielded: (1) TSC22 domain family protein 3 (TSC22D3); (2) Mediator of RNA polymerase II transcription subunit 8 isoform 1(MED8); (3) Runt-related transcription factor 3 (RUNX3); (4) Arrestin beta-2 (ARRB2); (5) Cereblon (CRBN). Indirect immunofluorescent assay showed that both TSC22D3 and MED8 co-localized with UL14. Co-immunoprecipitation assay demonstrated that UL14 could be immunoprecipitated by TSC22D3, suggesting that UL14 interacted with TSC22D3 under physiological condition. In summary, this study opened up new avenues toward delineating the function and physiological significance of UL14 during the HSV-1 replication cycle.
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