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Journal of Virology, June 2000, p. 5116-5122, Vol. 74, No. 11
Macfarlane Burnet Centre for Medical Research
and Australian Centre for Hepatitis Virology, Fairfield 3078, Victoria, Australia,1 and Microbiology
and Zentrum für Molekulare Biologie, Universität
Heidelberg, 69120 Heidelberg, Germany2
Received 10 December 1999/Accepted 7 March 2000
We have examined the structure and fusion potential of the duck
hepatitis B virus (DHBV) envelope proteins by treating subviral particles with deforming agents known to release envelope proteins of
viruses from a metastable to a fusion-active state. Exposure of DHBV
particles to low pH triggered a major structural change in the large
envelope protein (L), resulting in exposure of trypsin sites within its
S domain but without affecting the same region in the small surface
protein (S) subunits. This conformational change was associated with
increased hydrophobicity of the particle surface, most likely arising
from surface exposure of the hydrophobic first transmembrane domain
(TM1). In the hydrophobic conformation, DHBV particles were able to
bind to liposomes and intact cells, while in their absence these
particles aggregated, resulting in viral inactivation. These results
suggests that some L molecules are in a spring-loaded metastable state
which, when released, exposes a previously hidden hydrophobic domain, a
transition potentially representing the fusion-active state of the envelope.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
A Metastable Form of the Large Envelope Protein of
Duck Hepatitis B Virus: Low-pH Release Results in a Transition to a
Hydrophobic, Potentially Fusogenic Conformation
*
Corresponding author. Mailing address: Macfarlane
Burnet Centre for Medical Research, Yarra Bend Rd., P.O. Box 254, Fairfield, Victoria 3078, Australia. Phone: 61 3 9282 2109. Fax: 61 3 9282 2100. E-mail: grgacic{at}burnet.edu.au.
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