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To identify the protein encoded by the L7 region of bovine adenovirus-3 (BAdV-3), specific antisera were raised by immunizing rabbits with bacterial fusion proteins encoding the N-terminus or C-terminus of the BAdV-3 fiber protein. Immunoprecipitation and Western blot analysis confirmed that the fiber is expressed as a 102 kDa glycoprotein, which is localized to the nucleus of infected cells. To identify the nuclear localization signals (NLS), BAdV-3 fiber deletion mutants and GFP/β-galactosidase fusion proteins were expressed in transfected cells, and subcellular localization was visualized by immunofluorescence microscopy. Analysis of deletion mutants localized the NLS to the N-terminal 41 amino acids. Analysis of the N-terminal 41 amino acids identified a cluster of basic residues between amino acid 14 and 20. Substitution of the basic residues ( 16 KAKR 19 ) with acidic residues ( 16 EAEE 19 ) resulted in the accumulation of fiber in the cytoplasm. However, 16 KAKR 19 or 12 VYPYKAKRPNI 22 were not sufficient for efficient transport of a cytoplasmic protein GFP/β-galactosidase to the nucleus. The recombinant BAdV-3 expressing mutant fiber containing 16 EAEE 19 instead of 16 KAKR 19 was unable to replicate efficiently in Madin-Darby bovine kidney cells, suggesting that the NLS of fiber carries out important in vivo functions.
Archives of Virology – Springer Journals
Published: Sep 1, 2004
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