Cleavage of bovine adenovirus type 3 non-structural 100K protein by protease is required for nuclear localization in infected cells but is not essential for virus replication.

@article{Makadiya2015CleavageOB,
  title={Cleavage of bovine adenovirus type 3 non-structural 100K protein by protease is required for nuclear localization in infected cells but is not essential for virus replication.},
  author={Niraj Makadiya and Amit Gaba and Suresh K. Tikoo},
  journal={The Journal of general virology},
  year={2015},
  volume={96 9},
  pages={
          2749-63
        }
}
The L6 region of bovine adenovirus type 3 (BAdV-3) encodes a non-structural protein named 100K. Rabbit antiserum raised against BAdV-3 100K recognized a protein of 130 kDa at 12-24 h and proteins of 130, 100, 95 and 15 kDa at 36-48 h after BAdV-3 infection. The 100K species localized to the nucleus and the cytoplasm of BAdV-3-infected cells. In contrast, 100K localized predominantly to the cytoplasm of the transfected cells. However, BAdV-3 infection of cells transfected with 100K-enhanced… 
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References

SHOWING 1-10 OF 36 REFERENCES
Role of bovine adenovirus-3 33K protein in viral replication.
Mapping of nuclear import signal and importin α3 binding regions of 52K protein of bovine adenovirus-3.
Characterization and nuclear localization of the fiber protein encoded by the late region 7 of bovine adenovirus type 3
TLDR
The recombinant BAdV-3 expressing mutant fiber containing 16EAEE19 instead of 16KAKR19 was unable to replicate efficiently in Madin-Darby bovine kidney cells, suggesting that the NLS of fiber carries out important in vivo functions.
Interaction of bovine adenovirus-3 33K protein with other viral proteins.
Processing of the L1 52/55k Protein by the Adenovirus Protease: a New Substrate and New Insights into Virion Maturation
TLDR
The results support a model in which the role of L1 52/55k protein during assembly consists in tethering the viral core to the icosahedral shell and in which maturation proceeds simultaneously with packaging, before the viral particle is sealed.
The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growth
TLDR
The herpes simplex virus type 1 protease and related proteins are involved in the assembly of viral capsids and the function of Na, at least in part, is to direct the catalytic domain N(o) to the nucleus.
Arginine Methylation of Human Adenovirus Type 5 L4 100-Kilodalton Protein Is Required for Efficient Virus Production
TLDR
Data indicate that PRMT1-catalyzed arginine methylation in the RGG boxes regulates the binding of L4-100K to hexon and promotes the capsid assembly of the structural protein as well as modulating TL-mRNA interaction.
Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity
TLDR
Reconstitute proteinase activity in vitro with three purified viral components: the recombinant endoprotease protein; an 11-amino-acid peptide that originates from the carboxy terminus of pVI, the precursor to virion component VI; and adenovirus DNA.
Specific interactions of the adenovirus proteinase with the viral DNA, an 11-amino-acid viral peptide, and the cellular protein actin
TLDR
The interaction of AVP with two viral cofactors and with a cellular cofactor, actin, is characterized by quantitative analyses and the results are consistent with a specific model for the regulation of A VP.
Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein.
  • T. Chambers, R. Weir, +4 authors C. Rice
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1990
Sequence homology and molecular modeling studies have suggested that the N-terminal one-third of the flavirvirus nonstructural protein NS3 functions as a trypsin-like serine protease. To examine the…
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