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In vitro assembly of mosaic hepatitis B virus capsid‐like particles (CLPs): Rescue into CLPs of assembly‐deficient core protein fusions and FRET‐suited CLPs
Author(s) -
Vogel Maren,
Diez Manuel,
Eisfeld Jochen,
Nassal Michael
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.08.044
Subject(s) - capsid , förster resonance energy transfer , heterologous , biophysics , virology , fusion protein , biology , chemistry , microbiology and biotechnology , virus , genetics , gene , fluorescence , recombinant dna , physics , quantum mechanics
Hepatitis B virus core protein self‐assembles into icosahedral, highly immunogenic capsid‐like particles (CLPs) that can serve as molecular platforms for heterologous proteins. Insertion into the centrally located c/e1 epitope leads to surface display, fusion to the C terminus to internal disposition of the foreign domains. However, symmetry‐defined space restrictions on the surface and particularly inside the CLPs limit the size of usable heterologous fusion partners. Further, CLPs carrying differing foreign domains are desirable for applications such as multivalent vaccines, and for structure probing by distance sensitive interactions like fluorescence resonance energy transfer (FRET). Here, we report an in vitro co‐assembly system for such mosaic‐CLPs allowing successful CLP formation with a per se assembly‐deficient fusion protein, and of CLPs from two different fluoroprotein‐carrying fusions that exert FRET in an assembly‐status dependent way.