Comparative properties of the inclusion body proteins of the nucleopolyhedrosis viruses ofNeodiprion sertifer andLymantria dispar

Abstract

A comparison was made on the properties of the inclusion body proteins of two insect viruses: the nucleopolyhedrosis viruses of the European pine sawfly, Neodiprion sertifer, Geoffroy, and the gypsy moth, Lymantria dispar, Linnaeus. The inclusion body proteins were characterized by the following parameters: amino acid composition, polyacrylamide gel electrophoresis in the absence and presence of sodium dodecyl sulfate--mercaptoethanol, isoelectric focusing, and alkaline protease activity. The properties of the inclusion body proteins of the two viruses were similar in many respects, but clear differences were observed. A principal difference was the absence of alkaline protease activity associated with the inclusion body proteins of N. sertifer nucleopolyhedrosis virus.

Characterization of Gypsy Moth ( Lymantria dispar ) Nuclear Polyhedrosis Virus

“…In addition to studies to evaluate LdNPV as a biological control agent, LdNPV has been physically characterized. The viral structural proteins have been studied by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) (15,19,20,27), whereas the occlusion body (OB) protein has been dealt with separately by several workers (1,4,16). The viral DNA of the Hamden isolate has been partially characterized by restriction endonuclease analysis (17,21).…”

“…A portion of the purified OBs was heated in a water bath at 800C for 2 h to inactivate the alkaline protease associated with the virus preparation. Protease inactivation was monitored with a modification of the protease assay suggested by Brown et al (1). Approximately 108 OBs were dissolved in 1 ml of 50 mM Na2CO3…”