The bovine leukemia virus nucleocapsid (BLV-NC) protein serves as a nucleic acid chaperone in the viral life cycle by facilitating processes such as reverse transcription, viral packaging, and primer placement on viral DNA. BLV-NC was cloned into the pET 32a expression vector for the expression of BLV NC as a thioredoxin fusion protein with a TEV protease cleavage site. The Trx-BLV-NC was then over-expressed and purified using HPLC. After thioredoxin cleavage and further purification, fluorescence spectroscopy was used to characterize nucleic acid binding and chaperone activity.

Cloning, purification, and nucleic acid binding properties of bovine leukemia virus nucleocapsid protein

243rd National Meeting (2012)

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