Intracellular retention of duck hepatitis B virus large surface protein is independent of preS topology.

Abstract:

:The mechanism of intracellular retention for the large surface protein (L) of duck hepatitis B virus (DHBV) was analyzed by examination of the transmembrane topologies and secretory properties of a collection of DHBV L mutants and compared with that of human hepatitis B virus (HBV) L. Our results demonstrate that, in contrast to its HBV counterpart, intracellular retention of DHBV L does not depend on the cytosolic disposition of its preS domain. L mutants with either cytosolic or lumenal preS were mostly retained in the absence of the small surface protein (S), whereas coexpression with S resulted in efficient secretion of both topological forms. Coexpression of the wild-type DHBV L with S resulted in efficient incorporation of L into secreted S + L particles, whereas HBV L was partially excluded from secreted particles under the same conditions. We propose that HBV provides L retention even in the presence of an excess of S, by exclusion of molecules with cytosolic preS domains from secreted particles at the stage of their assembly. DHBV lacks such a retention mechanism due to the absence of topological selection in particulate assembly.

journal_name

Virology

journal_title

Virology

authors

Gazina EV,Lin B,Gallina A,Milanesi G,Anderson DA

doi

10.1006/viro.1997.9015

subject

Has Abstract

pub_date

1998-03-15 00:00:00

pages

266-78

issue

2

eissn

0042-6822

issn

1096-0341

pii

S0042-6822(97)99015-2

journal_volume

242

pub_type

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