HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Grgacic, E. V. L. Search for Related Content PubMed PubMed Citation Articles by Grgacic, E. V. L. Agricola Articles by Grgacic, E. V. L.

Identification of structural determinants of the first transmembrane domain of the small envelope protein of duck hepatitis B virus essential for particle morphogenesis

Australian Centre for Hepatitis Virology, Macfarlane Burnet Institute for Medical Research and Public Health, Yarra Bend Road, Fairfield 3078, Victoria, Australia¹

Author for correspondence: Elizabeth Grgacic. Fax +61 3 9282 2100. e-mail grgacic{at}burnet.edu.au

The envelope of duck hepatitis B virus (DHBV) consists of the small (S) and large (L) envelope proteins, which share a common C-terminal multispanning transmembrane region but differ by the long N-terminal pre-S domain of L, which is essential for interactions with both the receptor and nucleocapsid. To achieve these dual functions, L acquires mixed topologies through S-dependent post-translational translocation of its pre-S domain. This study has examined the role of S in this unusual mechanism of translocation by analysis of the -helical transmembrane domains and their potential to engage in lateral interactions for envelope assembly. Through mutagenesis in constructs expressing the S and L envelope proteins independently, transmembrane domain 1 was identified as an essential structural determinant in S. Two polar residues in this helix were identified as contributing to L protein translocation through the assembly of S into particles, implying that the topological switch of L is part of the assembly and maturation process. The same domain in L was shown to be dispensable for L translocation and assembly, suggesting that transmembrane domain 1 of L and S have different functional roles and structural arrangements on the assembled particle. The conservation in all hepadnavirus envelope proteins of two polar residues at positions 24 and 27 of transmembrane domain 1, the former positively charged, points to this being a common determinant in particle morphogenesis for all hepadnaviruses.

This article has been cited by other articles:

				J. Chojnacki, D. A. Anderson, and E. V. L. Grgacic A Hydrophobic Domain in the Large Envelope Protein Is Essential for Fusion of Duck Hepatitis B Virus at the Late Endosome J. Virol., December 1, 2005; 79(23): 14945 - 14955. [Abstract] [Full Text] [PDF]

				E. V. L. Grgacic and D. A. Anderson St, a Truncated Envelope Protein Derived from the S Protein of Duck Hepatitis B Virus, Acts as a Chaperone for the Folding of the Large Envelope Protein J. Virol., May 1, 2005; 79(9): 5346 - 5352. [Abstract] [Full Text] [PDF]

				C. Lambert, S. Mann, and R. Prange Assessment of determinants affecting the dual topology of hepadnaviral large envelope proteins J. Gen. Virol., May 1, 2004; 85(5): 1221 - 1225. [Abstract] [Full Text] [PDF]