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Journal of Virology, July 2000, p. 6126-6131, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Identification of the Lymantria dispar
Nucleopolyhedrovirus Envelope Fusion Protein Provides Evidence for a
Phylogenetic Division of the Baculoviridae
Margot N.
Pearson,
Christoph
Groten, and
George F.
Rohrmann*
Department of Microbiology, Oregon State
University, Corvallis, Oregon 97331-3804
Received 18 January 2000/Accepted 3 April 2000
The complete genome sequences of a number of diverse members of the
Baculoviridae including both nucleopolyhedroviruses (NPVs) and granuloviruses (GVs) revealed that they lack a homolog of GP64, the
envelope fusion protein of the budded form of Autographa californica multinucleocapsid NPV (AcMNPV) and its
close relatives. Computer-assisted analyses of the genome of one of
these viruses, Lymantria dispar MNPV (LdMNPV),
revealed a single open reading frame (ld130) whose product
had the predicted properties of a membrane protein. Characterization of
the localization of the products of the full-length ld130
gene and of an ld130-enhanced green fluorescent protein
gene (egfp) fusion using both immunofluorescence and
fluorescence microscopy revealed that LD130 accumulates at the plasma
membranes of cells infected with LdMNPV or transfected with
ld130-egfp. In addition, cells transfected with either
ld130 or ld130-egfp or infected with
wild-type virus undergo membrane fusion at pH 5. Western blot
analyses indicate that LD130 is present in infected cells as an 83-kDa
protein and is also present in budded virions as a protein doublet
containing bands of 81 and 83 kDa. Tunicamycin treatment of infected
cells resulted in an immunoreactive band of about 72 kDa, indicating
that LD130 is N-glycosylated. Whereas the distribution of
gp64 appears to be confined to a relatively closely related
group of NPVs, homologs of ld130 are present in a diverse
number of both NPVs and GVs. This suggests that LD130 may be the
primordial baculovirus envelope fusion protein.
*
Corresponding author. Mailing address: Department of
Microbiology, Nash Hall 220, Oregon State University, Corvallis, OR
97331-7301. Phone: (541) 737-1793. Fax: (541) 737-0496. E-mail:
rohrmann{at}bcc.orst.edu.

Technical report 11650 from the Oregon State University
Agricultural Experiment
Station.
Journal of Virology, July 2000, p. 6126-6131, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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