Disease relevance of BICP0

• The immediate-early protein, BICP0, of bovine herpesvirus 1 (BHV-1) transactivates a variety of viral and cellular genes [1].
• The predicted protein, designated BHV-1 infected cell protein 0 (BICP0), contains a zinc finger domain with homology to ICP0 of herpes simplex virus type 1 and protein 61 of varicella-zoster virus, and depending on the promoter, it acts as a strong activator or as a repressor in transient expression assays [2].
• 6. To confirm that ER2.6 encoded the 97-kDa BICP0 protein, a DNA fragment containing BICP0-coding sequences was inserted into the Autographa californica baculovirus genome [2].
• These cell lines may help to further explore the functions of BICP0 as well as to investigate the molecular basis of interactions between herpes- and retroviruses [3].
• Replacement of the BICP22 promoter by cytomegalovirus IE promoter revealed an additional posttranscriptional level of regulation whereby more BICP22 accumulated in cells when functional BICP0 was present [4].

High impact information on BICP0

• Here we provide evidence that PGD(2) impairs the transactivation ability of BICP0 that is necessary for efficient virus replication [1].
• Transactivator protein BICP0 of bovine herpesvirus 1 (BHV-1) is blocked by prostaglandin D2 (PGD2), which points to a mechanism for PGD2-mediated inhibition of BHV-1 replication [1].
• In a yeast two-hybrid cDNA library screening, we found that lipocalin-type prostaglandin D synthase, which catalyzes the production of prostaglandin D(2) (PGD(2)), is a cellular target of BICP0 [1].
• We microinjected Xenopus oocytes with a BICP0 effector plasmid and a promoter-chloramphenicol acetyltransferase plasmid [2].
• Western blots (immunoblots) revealed a BHV-1-specific 97-kDa protein which was detectable during the IE phase and also at later periods of infection, indicating that the kinetics of BICP0 synthesis is consistent with the switch from IER2.9 to ER2 [2].

Chemical compound and disease context of BICP0

• Construction and characterization of a stably transformed HeLa cell line in which the expression of bovine herpesvirus 1 ICP0 (BICP0) is induced by tetracycline [3].

Biological context of BICP0

• Our study identifies a new way ICP0 and BICP0 explore to regulate gene expression [5].
• The immediate early proteins ICP0 and BICP0 from Herpes virus are promiscuous activators of both viral and cellular genes and play a critical role in virus life cycle [5].
• Induced cell lines transactivated the native BICP0 promoter as well as the herpes simplex virus thymidine kinase promoter and the long terminal repeat sequences of human immunodeficiency virus in a dose dependent manner [3].

Anatomical context of BICP0

• Immunofluorescent assays indicated that BICP0 was synthesised in the transformed cell lines solely upon induction of the gene by tetracycline removal [3].

Associations of BICP0 with chemical compounds

• Only cells which had been kept constantly in medium containing tetracycline were able to synthesise BICP0 upon induction [3].

Other interactions of BICP0

• The BICP22 gene promoter itself was not repressed by BICP22; it could be dissected into a proximal region stimulated by BICP0 and a distal region stimulated by BHV-1 alpha-transinducing factor [4].
• The fact that expression of BICP4 and/or BICP0 in A31 cells does not improve the yield of progeny virus from infectious BHV-1 genomic DNA suggests that some more growth restrictions exist beyond the expression of BHV-1 immediate early proteins [6].

References