Slowly folding surface extension in the prototypic avian hepatitis B virus capsid governs stability.
E. coli
avihepadnavirus
chicken
disordered protein domain
duck hepatitis b virus core protein
elctron cryo microscopy
extension domain
molecular biophysics
structural biology
virus
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
14 08 2020
14 08 2020
Historique:
received:
26
03
2020
accepted:
13
08
2020
pubmed:
17
8
2020
medline:
26
2
2021
entrez:
16
8
2020
Statut:
epublish
Résumé
Hepatitis B virus (HBV) is an important but difficult to study human pathogen. Most basics of the hepadnaviral life-cycle were unraveled using duck HBV (DHBV) as a model although DHBV has a capsid protein (CP) comprising ~260 rather than ~180 amino acids. Here we present high-resolution structures of several DHBV capsid-like particles (CLPs) determined by electron cryo-microscopy. As for HBV, DHBV CLPs consist of a dimeric α-helical frame-work with protruding spikes at the dimer interface. A fundamental new feature is a ~ 45 amino acid proline-rich extension in each monomer replacing the tip of the spikes in HBV CP. In vitro, folding of the extension takes months, implying a catalyzed process in vivo. DHBc variants lacking a folding-proficient extension produced regular CLPs in bacteria but failed to form stable nucleocapsids in hepatoma cells. We propose that the extension domain acts as a conformational switch with differential response options during viral infection.
Identifiants
pubmed: 32795390
doi: 10.7554/eLife.57277
pii: 57277
pmc: PMC7455244
doi:
pii:
Substances chimiques
Capsid Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : BO1150/17-1
Pays : International
Organisme : Deutsche Forschungsgemeinschaft
ID : INST 92/903-1FUGG
Pays : International
Organisme : Deutsche Forschungsgemeinschaft
ID : Na154/9-4
Pays : International
Informations de copyright
© 2020, Makbul et al.
Déclaration de conflit d'intérêts
CM, MN, BB No competing interests declared
Références
Arch Microbiol. 1995 May;163(5):357-65
pubmed: 7540828
Nature. 1997 Mar 6;386(6620):91-4
pubmed: 9052787
J Virol. 2007 Dec;81(23):13230-4
pubmed: 17881436
J Virol. 1990 Jul;64(7):3249-58
pubmed: 2352324
J Virol. 2018 Jun 13;92(13):
pubmed: 29669831
J Mol Graph Model. 2005 Jan;23(4):347-54
pubmed: 15670955
Gut. 2015 Dec;64(12):1972-84
pubmed: 26048673
Cell Host Microbe. 2017 Sep 13;22(3):387-399.e6
pubmed: 28867387
Antiviral Res. 2015 Sep;121:82-93
pubmed: 26129969
Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9556-61
pubmed: 9275161
Cell. 1982 Jun;29(2):403-15
pubmed: 6180831
Nucleic Acids Res. 2019 Jan 8;47(D1):D427-D432
pubmed: 30357350
J Virol. 1984 Mar;49(3):782-92
pubmed: 6699938
Nature. 1979 Oct 25;281(5733):646-50
pubmed: 399327
Virology. 2006 Sep 30;353(2):443-50
pubmed: 16837020
J Mol Biol. 1992 Jun 20;225(4):1013-25
pubmed: 1613786
J Virol. 2011 Sep;85(18):9300-13
pubmed: 21752921
EMBO J. 2002 Mar 1;21(5):876-84
pubmed: 11867516
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
J Struct Biol. 2012 Sep;179(3):269-78
pubmed: 21963794
Cell. 1986 Nov 7;47(3):451-60
pubmed: 3768961
J Struct Biol. 2015 Nov;192(2):216-21
pubmed: 26278980
Viruses. 2017 May 22;9(5):
pubmed: 28531167
Nature. 1997 Mar 6;386(6620):88-91
pubmed: 9052786
Viruses. 2017 Apr 03;9(4):
pubmed: 28368357
Antiviral Res. 2018 Jan;149:211-220
pubmed: 29183719
Nat Rev Drug Discov. 2019 Nov;18(11):827-844
pubmed: 31455905
Ultramicroscopy. 2019 Aug;203:145-154
pubmed: 30738626
PLoS Pathog. 2010 Sep 02;6(9):e1001082
pubmed: 20824087
Intrinsically Disord Proteins. 2013 Apr 1;1(1):e24360
pubmed: 28516008
J Virol. 1996 Jul;70(7):4646-54
pubmed: 8676491
Adv Virus Res. 2004;63:1-70
pubmed: 15530560
Cell. 1994 Jun 17;77(6):943-50
pubmed: 8004680
J Viral Hepat. 2019 Jul;26(7):786-794
pubmed: 30803126
Mol Cell. 1999 Jun;3(6):771-80
pubmed: 10394365
J Virol. 1990 Jul;64(7):3319-30
pubmed: 2191149
Intrinsically Disord Proteins. 2013 Apr 1;1(1):e24684
pubmed: 28516010
Methods Mol Biol. 2013;946:1-13
pubmed: 23179822
J Mol Biol. 2018 Dec 7;430(24):4941-4954
pubmed: 30539760
PLoS Pathog. 2008 Dec;4(12):e1000230
pubmed: 19057662
J Virol. 1989 Jul;63(7):2995-3000
pubmed: 2724419
Methods Mol Biol. 2018;1776:503-531
pubmed: 29869263
J Immunol Methods. 2013 Aug 30;394(1-2):10-21
pubmed: 23624043
EMBO J. 2007 Sep 19;26(18):4160-7
pubmed: 17762862
Antimicrob Agents Chemother. 2018 Sep 24;62(10):
pubmed: 30012770
Viruses. 2017 Jan 21;9(1):
pubmed: 28117723
Elife. 2018 Jan 29;7:
pubmed: 29377794
Elife. 2018 Nov 09;7:
pubmed: 30412051
J Virol. 1990 Feb;64(2):613-20
pubmed: 2153228
Structure. 1995 Oct 15;3(10):1009-19
pubmed: 8589996
EMBO J. 2011 Aug 31;30(17):3481-500
pubmed: 21878991
J Med Chem. 2016 Nov 10;59(21):9622-9644
pubmed: 27409354
Mol Cell. 2006 Jun 23;22(6):843-850
pubmed: 16793552
Curr Opin Struct Biol. 2020 Jun;62:9-13
pubmed: 31783325
Commun Biol. 2019 Jun 19;2:218
pubmed: 31240256
Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15821-6
pubmed: 16247012
Annu Rev Virol. 2016 Sep 29;3(1):429-451
pubmed: 27482896
Nat Methods. 2017 Apr;14(4):331-332
pubmed: 28250466
PLoS Pathog. 2018 Dec 19;14(12):e1007488
pubmed: 30566530
J Virol. 2016 Aug 12;90(17):7920-33
pubmed: 27334580
J Virol. 2007 Dec;81(23):13218-29
pubmed: 17881438