The basic DNA-binding protein of Bombyx mori nuclear polyhedrosis virus: the existence of an additional arginine repeat

Abstract

The basic DNA-binding protein of the Bombyx mori nuclear polyhedrosis virus (BmNPV) was purified by HPLC and a sequence of 45 amino acids from the N-terminus was determined. There were no detectable modifications such as N-terminal blockage, glycosylation, or phosphorylation. The amino acid sequence showed high homology to the predicted amino acid sequences of the basic proteins of Autographa californica NPV (AcNPV) and Orgyia pseudotsugata NPV (OpNPV) (90 and 76%, respectively), however, the BmNPV basic protein possessed an additional sequence of 10 amino acids. A DNA fragment encoding the basic protein was identified in a BmNPV DNA library by screening for possible DNA sequences coding for the basic protein's amino acid sequence. The nucleotide sequence of the basic protein of BmNPV was more similar to that of AcNPV (97%) than to that of OpNPV (62%). Homology plot analysis of the nucleotide sequence indicates that the BmNPV basic protein internal repeat evolved very recently.