D. Dall et al., A GENE ENCODING A HIGHLY EXPRESSED SPINDLE BODY PROTEIN OF HELIOTHIS-ARMIGERA ENTOMOPOXVIRUS, Journal of General Virology, 74, 1993, pp. 1811-1818
The gene encoding the most abundant protein of purified preparations o
f Heliothis armigera entomopoxvirus (HaEPV) has been cloned and sequen
ced. The gene sequence encodes a 40.1K polypeptide with a putative N-t
erminal 20 amino acid leader peptide, and a single potential N-glycosy
lation site. Analysis of the protein, which has an apparent M(r) of 50
K on polyacrylamide gels, confirmed post-translational loss of the lea
der peptide, but showed no evidence of glycosylation. The protein is r
elated 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 lab
elled HaEPV spindle bodies; confocal laser scanning microscopy suggest
s that the protein is distributed throughout those viral structures.