Abstract:
:The Hepatitis B virus Precore protein, present in the secretory pathway as the HBeAg precursor, can associate in the cytoplasm with the Core protein to form heterocapsids, likely to favor viral persistence. Core and Precore proteins share their primary sequence except for ten additional aminoacids at the N-terminus of Precore. To address the role of this propeptide sequence in the formation of Precore heterocapsids, we designed a Precore mutant in which the two propeptide tryptophans are replaced by glycines. This mutant retains the properties of the wild-type Precore, notably cell trafficking and ability to interact with Core. However, it is not incorporated into heterocapsids and forms stable dimers distinct from the labile HBe dimers and the presumably Core-like dimers assembled into heterocapsids. Our data highlights the essential role of Precore׳s propeptide in switching between different conformations for different functions and pinpoint the propeptide Tryptophan residues as central in these properties.
journal_name
Virologyjournal_title
Virologyauthors
Duriez M,Thouard A,Bressanelli S,Rossignol JM,Sitterlin Ddoi
10.1016/j.virol.2014.06.013subject
Has Abstractpub_date
2014-08-01 00:00:00pages
273-82eissn
0042-6822issn
1096-0341pii
S0042-6822(14)00274-8journal_volume
462-463pub_type
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