Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and γ2-Adaptin

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Published inJournal of Virology Vol. 81; no. 17; pp. 9050 - 9060
Main Authors LAMBERT, Carsten, DORING, Tatjana, PRANGE, Reinhild
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.09.2007
Subjects
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Genome and Regulation of Viral Gene Expression
Microbiology
Miscellaneous
Virology
Virus
Orthohepadnavirus
Hepatitis B virus
Hepadnaviridae
Virology
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Abstract Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JVI .asm.org, visit: JVI       
AbstractList Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host proteins, the ubiquitin-interacting adaptor γ2-adaptin and the Nedd4 ubiquitin ligase. Here, we demonstrate that HBV release also requires the cellular machinery that generates internal vesicles of multivesicular bodies (MVBs). In order to perturb the MVB machinery in HBV-replicating liver cells, we used ectopic expression of dominant-negative mutants of different MVB components, like the ESCRT-III complex-forming CHMP proteins and the Vps4 ATPases. Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPase-defective Vps4A or Vps4B mutants, HBV assembly and egress were potently blocked. Each of the MVB inhibitors arrested virus particle maturation by entrapping the viral core and large and small envelope proteins in detergent-insoluble membrane structures that closely resembled aberrant endosomal class E compartments. In contrast, HBV subvirus particle release was not affected by MVB inhibitors, hinting at different export routes used by viral and subviral particles. To further define the role γ2-adaptin plays in HBV formation, we examined the effects of its overexpression in virus-replicating cells. Intriguingly, excess γ2-adaptin blocked HBV production in a manner similar to the actions of CHMP and Vps4 mutants. Moreover, overexpressed γ2-adaptin perturbed the endosomal morphology and diminished the budding of a retroviral Gag protein, implying that it may act as a principal inhibitor of the MVB sorting pathway. Together, these results demonstrate that HBV exploits the MVB machinery with the aid of γ2-adaptin.
ABSTRACT Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host proteins, the ubiquitin-interacting adaptor γ2-adaptin and the Nedd4 ubiquitin ligase. Here, we demonstrate that HBV release also requires the cellular machinery that generates internal vesicles of multivesicular bodies (MVBs). In order to perturb the MVB machinery in HBV-replicating liver cells, we used ectopic expression of dominant-negative mutants of different MVB components, like the ESCRT-III complex-forming CHMP proteins and the Vps4 ATPases. Upon coexpression of mutated CHMP3, CHMP4B, or CHMP4C forms, as well as of ATPase-defective Vps4A or Vps4B mutants, HBV assembly and egress were potently blocked. Each of the MVB inhibitors arrested virus particle maturation by entrapping the viral core and large and small envelope proteins in detergent-insoluble membrane structures that closely resembled aberrant endosomal class E compartments. In contrast, HBV subvirus particle release was not affected by MVB inhibitors, hinting at different export routes used by viral and subviral particles. To further define the role γ2-adaptin plays in HBV formation, we examined the effects of its overexpression in virus-replicating cells. Intriguingly, excess γ2-adaptin blocked HBV production in a manner similar to the actions of CHMP and Vps4 mutants. Moreover, overexpressed γ2-adaptin perturbed the endosomal morphology and diminished the budding of a retroviral Gag protein, implying that it may act as a principal inhibitor of the MVB sorting pathway. Together, these results demonstrate that HBV exploits the MVB machinery with the aid of γ2-adaptin.
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Author Carsten Lambert
Tatjana Döring
Reinhild Prange
AuthorAffiliation Department of Medical Microbiology and Hygiene, Johannes Gutenberg-Universität Mainz, D-55101 Mainz, Germany
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Cites_doi 10.1016/j.virol.2005.09.044
10.3748/wjg.v13.i1.22
10.1091/mbc.11.1.227
10.1016/S0092-8674(03)00714-1
10.1128/JVI.77.17.9173-9182.2003
10.1128/jvi.52.2.396-402.1984
10.1128/jvi.64.2.613-620.1990
10.1016/S0014-5793(98)01083-7
10.1034/j.1600-0854.2003.00135.x
10.1016/S1534-5807(02)00219-8
10.1056/NEJMra031087
10.1128/JVI.79.16.10460-10466.2005
10.1242/jcs.00213
10.1074/jbc.273.38.24693
10.1128/JVI.01049-06
10.1016/S0092-8674(01)00506-2
10.1146/annurev.cellbio.20.010403.102350
10.1128/JVI.02741-06
10.1083/jcb.118.6.1305
10.1074/jbc.M509317200
10.1016/S0092-8674(01)00434-2
10.1073/pnas.2133846100
10.1074/jbc.M413968200
10.1074/jbc.274.9.5385
10.1006/viro.2000.0268
10.1128/JVI.75.11.5343-5351.2001
10.3748/wjg.v13.i1.65
10.1083/jcb.200408155
10.1074/jbc.M100956200
10.1042/BJ20041227
10.1074/jbc.M413735200
10.1159/000024970
10.1016/j.virol.2006.07.018
10.1016/j.cell.2004.12.023
10.1128/JVI.74.24.11472-11478.2000
10.1016/j.tcb.2006.04.004
10.1074/jbc.M603517200
10.1016/S1534-5807(02)00220-4
10.1016/j.jmb.2006.04.017
10.1016/S0092-8674(03)00653-6
10.1016/j.tim.2004.05.004
10.1074/jbc.M202838200
10.1091/mbc.12.10.2907
10.1038/sj.onc.1207436
10.1083/jcb.200304008
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Keywords Virus
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Hepadnaviridae
Virology
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Notes Corresponding author. Mailing address: Department of Medical Microbiology and Hygiene, University of Mainz, Augustusplatz, D-55101 Mainz, Germany. Phone: 49-6131-3936750. Fax: 49-6131-3932359. E-mail: prange@mail.uni-mainz.de
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e_1_3_2_27_2
e_1_3_2_28_2
e_1_3_2_29_2
e_1_3_2_41_2
e_1_3_2_40_2
e_1_3_2_20_2
e_1_3_2_43_2
e_1_3_2_21_2
e_1_3_2_42_2
e_1_3_2_22_2
e_1_3_2_45_2
e_1_3_2_23_2
e_1_3_2_44_2
e_1_3_2_24_2
e_1_3_2_25_2
e_1_3_2_46_2
e_1_3_2_9_2
e_1_3_2_15_2
e_1_3_2_38_2
e_1_3_2_8_2
e_1_3_2_16_2
e_1_3_2_37_2
e_1_3_2_7_2
e_1_3_2_17_2
e_1_3_2_6_2
e_1_3_2_18_2
e_1_3_2_39_2
e_1_3_2_19_2
e_1_3_2_30_2
e_1_3_2_32_2
e_1_3_2_10_2
e_1_3_2_31_2
e_1_3_2_5_2
e_1_3_2_11_2
e_1_3_2_34_2
e_1_3_2_4_2
e_1_3_2_12_2
e_1_3_2_33_2
e_1_3_2_3_2
e_1_3_2_13_2
e_1_3_2_36_2
e_1_3_2_2_2
e_1_3_2_14_2
e_1_3_2_35_2
References_xml – ident: e_1_3_2_4_2
  doi: 10.1016/j.virol.2005.09.044
– ident: e_1_3_2_13_2
  doi: 10.3748/wjg.v13.i1.22
– ident: e_1_3_2_5_2
  doi: 10.1091/mbc.11.1.227
– ident: e_1_3_2_44_2
  doi: 10.1016/S0092-8674(03)00714-1
– ident: e_1_3_2_14_2
  doi: 10.1128/JVI.77.17.9173-9182.2003
– ident: e_1_3_2_17_2
  doi: 10.1128/jvi.52.2.396-402.1984
– ident: e_1_3_2_37_2
  doi: 10.1128/jvi.64.2.613-620.1990
– ident: e_1_3_2_26_2
  doi: 10.1016/S0014-5793(98)01083-7
– ident: e_1_3_2_40_2
  doi: 10.1034/j.1600-0854.2003.00135.x
– ident: e_1_3_2_3_2
  doi: 10.1016/S1534-5807(02)00219-8
– ident: e_1_3_2_11_2
  doi: 10.1056/NEJMra031087
– ident: e_1_3_2_20_2
  doi: 10.1128/JVI.79.16.10460-10466.2005
– ident: e_1_3_2_10_2
  doi: 10.1242/jcs.00213
– ident: e_1_3_2_43_2
  doi: 10.1074/jbc.273.38.24693
– ident: e_1_3_2_25_2
  doi: 10.1128/JVI.01049-06
– ident: e_1_3_2_12_2
  doi: 10.1016/S0092-8674(01)00506-2
– ident: e_1_3_2_32_2
  doi: 10.1146/annurev.cellbio.20.010403.102350
– ident: e_1_3_2_34_2
  doi: 10.1128/JVI.02741-06
– ident: e_1_3_2_18_2
  doi: 10.1083/jcb.118.6.1305
– ident: e_1_3_2_8_2
  doi: 10.1074/jbc.M509317200
– ident: e_1_3_2_21_2
  doi: 10.1016/S0092-8674(01)00434-2
– ident: e_1_3_2_31_2
  doi: 10.1073/pnas.2133846100
– ident: e_1_3_2_27_2
  doi: 10.1074/jbc.M413968200
– ident: e_1_3_2_46_2
  doi: 10.1074/jbc.274.9.5385
– ident: e_1_3_2_28_2
  doi: 10.1006/viro.2000.0268
– ident: e_1_3_2_16_2
  doi: 10.1128/JVI.75.11.5343-5351.2001
– ident: e_1_3_2_7_2
  doi: 10.3748/wjg.v13.i1.65
– ident: e_1_3_2_30_2
  doi: 10.1083/jcb.200408155
– ident: e_1_3_2_24_2
  doi: 10.1074/jbc.M100956200
– ident: e_1_3_2_45_2
  doi: 10.1042/BJ20041227
– ident: e_1_3_2_39_2
  doi: 10.1074/jbc.M413735200
– ident: e_1_3_2_33_2
  doi: 10.1159/000024970
– ident: e_1_3_2_22_2
  doi: 10.1016/j.virol.2006.07.018
– ident: e_1_3_2_9_2
  doi: 10.1016/j.cell.2004.12.023
– ident: e_1_3_2_29_2
  doi: 10.1128/JVI.74.24.11472-11478.2000
– ident: e_1_3_2_41_2
  doi: 10.1016/j.tcb.2006.04.004
– ident: e_1_3_2_38_2
  doi: 10.1074/jbc.M603517200
– ident: e_1_3_2_2_2
  doi: 10.1016/S1534-5807(02)00220-4
– ident: e_1_3_2_15_2
  doi: 10.1016/j.jmb.2006.04.017
– ident: e_1_3_2_42_2
  doi: 10.1016/S0092-8674(03)00653-6
– ident: e_1_3_2_36_2
  doi: 10.1016/j.tim.2004.05.004
– ident: e_1_3_2_23_2
  doi: 10.1074/jbc.M202838200
– ident: e_1_3_2_6_2
  doi: 10.1091/mbc.12.10.2907
– ident: e_1_3_2_19_2
  doi: 10.1038/sj.onc.1207436
– ident: e_1_3_2_35_2
  doi: 10.1083/jcb.200304008
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Snippet Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
ABSTRACT Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two...
Hepatitis B virus (HBV) is an enveloped DNA virus that presumably buds at intracellular membranes of infected cells. HBV budding involves two endocytic host...
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SubjectTerms Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Genome and Regulation of Viral Gene Expression
Microbiology
Miscellaneous
Virology
Title Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and γ2-Adaptin
URI http://jvi.asm.org/content/81/17/9050.abstract
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