Elucidation of the role of Ebp1 (EbB3 binding protein ) on the Rinderpest virus life cycle
Rinderpest virus (RPV) has a single-strand, non-segmented, negative-polarity RNA genome and is thus classified within the order Mononegavirales, family Paramyxoviridae, subfamily Paramyxovirinae, genus Morbillivirus, which also includes human Measles virus, Canine and Phocine distemper viruses, Peste-des-petits-ruminants virus and the more recently isolated cetacean morbilliviruses (Barrett, 2001). Paramyxoviruses replicate in the cytoplasm of infected cells and in general encodes for six genes which are tandemly arranged. Transcription is initiated at the 3” end resulting in the production of a 55 nt leader sequence followed by the transcription of Nucleocapsid protein (NP or N), Phosphoprotein (P/C/V), Matrix (M), Fusion protein (F), Hemagglutinin (HA) and the Large protein (L). Viral RNA dependent RNA polymerase is composed of L and P proteins although recent evidences suggest the formation of a tripartite LNP complex performing the replication alone.
EBP1 was identified as a protein that interacts with the ErbB-3 receptor and possibly contributes to transducing growth regulatory signals. The existence of EBP1 homologs across species from simple eukaryotes to humans and its wide tissue expression pattern suggest that EBP1 acts as a general signaling molecule. EBP1 is localized to the cytoplasm and to the nucleolus, and that its nucleolar localization requires amino-acid sequences present at both the amino- and carboxy-terminus of the molecule.EBP1 overexpression inhibits proliferation of human fibroblasts, and that this effect is linked to its nucleolar localization. EBP1 is part of ribonucleoprotein complexes and associates with different rRNA species. It is becoming clear that cell growth and proliferation are actively coordinated with rRNA processing and ribosome assembly. Many...