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Journal of Virology, March 2000, p. 2455-2458, Vol. 74, No. 5
Macfarlane Burnet Centre for Medical
Research, Fairfield, Victoria, Australia,1 and
Zentrum für Molekulare Biologie, Universität
Heidelberg, 69120 Heidelberg, Germany2
Received 7 September 1999/Accepted 30 November 1999
A unique feature of the large hepadnavirus envelope protein (L) is
its mixed transmembrane topology, resulting from partial posttranslational translocation of the pre-S domain. Using protease protection analysis, we demonstrate for duck hepatitis B virus an
essential role for the small envelope protein (S) in this process, providing the first experimental evidence for an S translocation channel. Further analysis revealed that the presumed cytoplasmic loop
between TM1 and TM2 in the C-terminal S domain is membrane embedded and
protrudes to the particle surface. These data suggest that some L
molecules form a highly folded, potentially spring-loaded topology with
five membrane-spanning regions and a membrane-traversing pre-S chain.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Hepadnavirus Envelope Topology: Insertion of a Loop
Region in the Membrane and Role of S in L Protein
Translocation
*
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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