A gene encoding a highly expressed spindle body protein of Heliothis armigera entomopoxvirus

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Abstract
The gene encoding the most abundant protein of purified preparations of Heliothis armigera entomopoxvirus (HaEPV) has been cloned and sequenced. The gene sequence encodes a 40.1K polypeptide with a putative N-terminal 20 amino acid leader peptide, and a single potential N-glycosylation site. Analysis of the protein, which has an apparent M r of 50K on polyacrylamide gels, confirmed post-translational loss of the leader peptide, but showed no evidence of glycosylation. The protein is related to others previously described from Choristoneura biennis EPV (63% identity) and Autographa californica nuclear polyhedrosis virus (42% identity). Polyclonal antiserum raised against a bacterial fusion protein containing the majority of the HaEPV protein specifically labelled HaEPV spindle bodies; confocal laser scanning microscopy suggests that the protein is distributed throughout those viral structures.

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