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Properties of the Major Nucleocapsid Protein of Heliothis zea Singly Enveloped Nuclear Polyhedrosis Virus

¹ Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, U.K.
NERC Institute of Virology, Mansfield Road, Oxford OX1 3SR

The major nucleocapsid protein of Heliothis zea single nucleocapsid nuclear polyhedrosis virus is a low mol. wt., basic, DNA-binding protein present in the core of the capsid. It is rich in arginine and helix-destabilizing residues and possesses no lysine nor hydrophobic residues. Circular dichroism analysis showed that the protein undergoes a major conformational change in high salt solutions involving the tyrosine side chains. There is sufficient of this protein in the nucleocapsid for all the genome phosphate to be neutralized by arginine residues. A comparison of the protein with similar basic proteins from Spodoptera litura granulosis virus, Oryctes rhinoceros non-occluded baculovirus, and Trichoplusia ni multiple nucleocapsid nuclear polyhedrosis virus showed that they are all arginine-rich, lysine-poor, DNA-binding proteins.

Keywords: DNA-binding protein, nuclear polyhedrosis virus, circular dichroism, amino acid analysis

Received 15 June 1982; accepted 21 September 1982.