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Article ; Online: Hepatitis B virus movement through the hepatocyte: An update.

Prange, Reinhild

2022 Volume 114, Issue 12, Page(s) 325–348

Abstract: Viruses are obligate intracellular pathogens that utilize cellular machinery for many aspects of their propagation and effective egress of virus particles from host cells is one important determinant of virus infectivity. Hijacking host cell processes ... ...

Abstract	Viruses are obligate intracellular pathogens that utilize cellular machinery for many aspects of their propagation and effective egress of virus particles from host cells is one important determinant of virus infectivity. Hijacking host cell processes applies in particular to the hepatitis B virus (HBV), as its DNA genome with about 3 kb in size is one of the smallest viral genomes known. HBV is a leading cause of liver disease and still displays one of the most successful pathogens in human populations worldwide. The extremely successful spread of this virus is explained by its efficient transmission strategies and its versatile particle types, including virions, empty envelopes, naked capsids, and others. HBV exploits distinct host trafficking machineries to assemble and release its particle types including nucleocytoplasmic shuttling transport, secretory, and exocytic pathways, the Endosomal Sorting Complexes Required for Transport pathway, and the autophagy pathway. Understanding how HBV uses and subverts host membrane trafficking systems offers the chance of obtaining new mechanistic insights into the regulation and function of this essential cellular processes. It can also help to identify potential targets for antiviral interventions. Here, I will provide an overview of HBV maturation, assembly, and budding, with a focus on recent advances, and will point out areas where questions remain that can benefit from future studies. Unless otherwise indicated, almost all presented knowledge was gained from cell culture-based, HBV in vitro-replication and in vitro-infection systems.
Language	English
Publishing date	2022-08-30
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.202200060
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Book ; Thesis: Hepatitis-B-Virus-Infektionen

Prange, Reinhild

die Rolle der Virushülle in der Morphogenese, Pathogenese und Prophylaxe

1998

Author's details	von Reinhild Prange
Language	German
Size	III, 114 Bl., Ill., graph. Darst., 30 cm
Publishing country	Germany
Document type	Book ; Thesis
Thesis / German Habilitation thesis	Mainz, Univ., Habil.-Schr., 1998
HBZ-ID	HT012974093
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: Host factors involved in hepatitis B virus maturation, assembly, and egress.

Prange, Reinhild

Medical microbiology and immunology

2012 Volume 201, Issue 4, Page(s) 449–461

Abstract: Hepatitis B virus (HBV) is a major cause of liver disease. Due to the tiny size of its genome, HBV depends on the critical interplay between viral and host factors for the generation of new viral particles from infected cells. Recent work has illuminated ...

Abstract	Hepatitis B virus (HBV) is a major cause of liver disease. Due to the tiny size of its genome, HBV depends on the critical interplay between viral and host factors for the generation of new viral particles from infected cells. Recent work has illuminated a multiplicity of spatially and temporally coordinated virus-host interactions that accompany HBV particle genesis. These interactions include the requirement of cellular chaperones for the maturation of the three viral envelope proteins, the cellular factors involved in dynamic modification, maturation, and intracellular trafficking of the nucleocapsids, and the host components of the multivesicular body (MVB) pathway enabling virion budding at intracellular compartments. Beside infectious virions, HBV produces at least two other types of particles, subviral empty envelope particles and subviral naked capsid particles, likely as a result of the engagement of different host factors by the viral structural proteins. Accordingly, HBV exploits distinct cellular pathways to release its particle types. Here, I review recent progress in these areas of the cell biology of HBV genesis.
MeSH term(s)	Hepatitis B virus/physiology ; Host-Pathogen Interactions ; Humans ; Protein Processing, Post-Translational ; Protein Transport ; Viral Proteins/metabolism ; Virus Assembly ; Virus Release
Chemical Substances	Viral Proteins
Language	English
Publishing date	2012-09-11
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	120933-4
ISSN	1432-1831 ; 0300-8584
ISSN (online)	1432-1831
ISSN	0300-8584
DOI	10.1007/s00430-012-0267-9
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Article: Host Cell Rab GTPases in Hepatitis B Virus Infection.

Zeyen, Lisa / Prange, Reinhild

Frontiers in cell and developmental biology

2018 Volume 6, Page(s) 154

Abstract: Hepatitis B virus (HBV) is a leading cause of liver disease and is presently estimated to infect more than 250 million humans. The extremely successful spread of this virus among the human population is explained by its effective transmission strategies ... ...

Abstract	Hepatitis B virus (HBV) is a leading cause of liver disease and is presently estimated to infect more than 250 million humans. The extremely successful spread of this virus among the human population is explained by its effective transmission strategies and its manifold particle types, including virions, empty envelopes and naked capsids. Due to its tiny genome, HBV depends on cellular machineries to thrive in infected hepatocytes. To enter, traverse and exit the cell, HBV exploits host membrane trafficking pathways, including intracellular highways directed by Rab GTPases. Here, we review recent discoveries focused on how HBV co-opts and perturbs host Rab GTPase functions with an emphasis on Rab7A- and Rab33B-mediated trafficking pathways. Rab7A plays bidirectional roles in the viral life cycle, as it promotes the endocytic uptake of HBV in early stages, but restricts exocytic virion release in late stages. In intermediate stages of HBV propagation, Rab33B is needed to guide the assembly of replicative progeny nucleocapsids. Rab33B acts together with its Atg5-12/16L1 effector, a protein complex required for autophagosome formation, suggesting the concept that HBV exploits this Rab/effector complex as an assembly scaffold and machine. We also discuss whether Rab-directed trafficking pathways engaged by HBV may be applicable to other virus families. Identification of overlapping Rab functions may offer new chances to develop broad-spectrum host-targeted antiviral strategies.
Language	English
Publishing date	2018-11-19
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2018.00154
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Article ; Online: Hepatitis B Virus Exploits ERGIC-53 in Conjunction with COPII to Exit Cells.

Zeyen, Lisa / Döring, Tatjana / Prange, Reinhild

Cells

2020 Volume 9, Issue 8

Abstract: Several decades after its discovery, the hepatitis B virus (HBV) still displays one of the most successful pathogens in human populations worldwide. The identification and characterization of interactions between cellular and pathogenic components are ... ...

Abstract	Several decades after its discovery, the hepatitis B virus (HBV) still displays one of the most successful pathogens in human populations worldwide. The identification and characterization of interactions between cellular and pathogenic components are essential for the development of antiviral treatments. Due to its small-sized genome, HBV highly depends on cellular functions to produce and export progeny particles. Deploying biochemical-silencing methods and molecular interaction studies in HBV-expressing liver cells, we herein identified the cellular ERGIC-53, a high-mannose-specific lectin, and distinct components of the endoplasmic reticulum (ER) export machinery COPII as crucial factors of viral trafficking and egress. Whereas the COPII subunits Sec24A, Sec23B and Sar1 are needed for both viral and subviral HBV particle exit, ERGIC-53 appears as an exclusive element of viral particle propagation, therefore interacting with the N146-glycan of the HBV envelope in a productive manner. Cell-imaging studies pointed to ER-derived, subcellular compartments where HBV assembly initiates. Moreover, our findings provide evidence that HBV exploits the functions of ERGIC-53 and Sec24A after the envelopment of nucleocapsids at these compartments in conjunction with endosomal sorting complexes required for transport (ESCRT) components. These data reveal novel insights into HBV assembly and trafficking, illustrating therapeutic prospects for intervening with the viral life cycle.
MeSH term(s)	COP-Coated Vesicles/metabolism ; Cell Line, Tumor ; Endoplasmic Reticulum/metabolism ; Endosomal Sorting Complexes Required for Transport/metabolism ; Hepatitis B/metabolism ; Hepatitis B/virology ; Hepatitis B virus/metabolism ; Hepatocytes/metabolism ; Hepatocytes/virology ; Humans ; Mannose-Binding Lectins/genetics ; Mannose-Binding Lectins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Protein Transport/genetics ; Transfection ; Vesicular Transport Proteins/metabolism ; Virion/metabolism
Chemical Substances	Endosomal Sorting Complexes Required for Transport ; LMAN1 protein, human ; Mannose-Binding Lectins ; Membrane Proteins ; SEC24A protein, human ; Vesicular Transport Proteins
Keywords	covid19
Language	English
Publishing date	2020-08-12
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells9081889
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Article ; Online: Hepatitis B subviral envelope particles use the COPII machinery for intracellular transport via selective exploitation of Sec24A and Sec23B.

Zeyen, Lisa / Döring, Tatjana / Stieler, Jens T / Prange, Reinhild

Cellular microbiology

2020 Volume 22, Issue 6, Page(s) e13181

Abstract: Hepatitis B virus (HBV) is a leading cause of liver disease. Its success as a human pathogen is related to the immense production of subviral envelope particles (SVPs) contributing to viral persistence by interfering with immune functions. To explore ... ...

Abstract	Hepatitis B virus (HBV) is a leading cause of liver disease. Its success as a human pathogen is related to the immense production of subviral envelope particles (SVPs) contributing to viral persistence by interfering with immune functions. To explore cellular pathways involved in SVP formation and egress, we investigated host-pathogen interactions. Yeast-based proteomics revealed Sec24A, a component of the coat protein complex II (COPII), as an interaction partner of the HBV envelope S domain. To understand how HBV co-opts COPII as a proviral machinery, we studied roles of key Sec proteins in HBV-expressing liver cells. Silencing of Sar1, Sec23, and Sec24, which promote COPII assembly concomitant with cargo loading, strongly diminished endoplasmic reticulum (ER) envelope export and SVP secretion. By analysing Sec paralog specificities, we unexpectedly found that the HBV envelope is a selective interaction partner of Sec24A and Sec23B whose functions could not be substituted by their related isoforms. In support, we found that HBV replication upregulated Sec24A and Sec23B transcription. Furthermore, HBV encountered the Sec24A/Sec23B complex via an interaction that involved the N-terminal half of Sec24A and a di-arginine motif of its S domain, mirroring a novel ER export code. Accordingly, an interference with the COPII/HBV cross-talk might display a tool to effectively inhibit SVP release.
MeSH term(s)	Biological Transport/physiology ; COP-Coated Vesicles/metabolism ; Cell Line ; Endoplasmic Reticulum/metabolism ; Hepatitis B/metabolism ; Hepatitis B virus/metabolism ; Hepatocytes/metabolism ; Host-Pathogen Interactions ; Humans ; Protein Isoforms ; RNA, Small Interfering ; Vesicular Transport Proteins/metabolism
Chemical Substances	Protein Isoforms ; RNA, Small Interfering ; SEC23B protein, human ; SEC24A protein, human ; Vesicular Transport Proteins
Language	English
Publishing date	2020-02-15
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/cmi.13181
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Article ; Online: ESCRT Requirements for Murine Leukemia Virus Release.

Bartusch, Christina / Prange, Reinhild

Viruses

2016 Volume 8, Issue 4, Page(s) 103

Abstract: The Murine Leukemia Virus (MLV) is a gammaretrovirus that hijack host components of the endosomal sorting complex required for transport (ESCRT) for budding. To determine the minimal requirements for ESCRT factors in MLV viral and viral-like particles ( ... ...

Abstract	The Murine Leukemia Virus (MLV) is a gammaretrovirus that hijack host components of the endosomal sorting complex required for transport (ESCRT) for budding. To determine the minimal requirements for ESCRT factors in MLV viral and viral-like particles (VLP) release, an siRNA knockdown screen of ESCRT(-associated) proteins was performed in MLV-producing human cells. We found that MLV VLPs and virions primarily engage the ESCRT-I factor Tsg101 and marginally the ESCRT-associated adaptors Nedd4-1 and Alix to enter the ESCRT pathway. Conversely, the inactivation of ESCRT-II had no impact on VLP and virion egress. By analyzing the effects of individual ESCRT-III knockdowns, VLP and virion release was profoundly inhibited in CHMP2A- and CHMP4B-knockdown cells. In contrast, neither the CHMP2B and CHMP4A isoforms nor CHMP3, CHMP5, and CHMP6 were found to be essential. In case of CHMP1, we unexpectedly observed that the CHMP1A isoform was specifically required for virus budding, but dispensable for VLP release. Hence, MLV utilizes only a subset of ESCRT factors, and viral and viral-like particles differ in ESCRT-III factor requirements.
MeSH term(s)	Animals ; Cell Line ; Endosomal Sorting Complexes Required for Transport/genetics ; Endosomal Sorting Complexes Required for Transport/metabolism ; Gene Expression ; Gene Knockdown Techniques ; Gene Order ; Gene Products, gag/genetics ; Gene Products, gag/metabolism ; Genetic Vectors/genetics ; Humans ; Leukemia Virus, Murine/physiology ; Mice ; Retroviridae Infections/metabolism ; Retroviridae Infections/virology ; Virus Release
Chemical Substances	Endosomal Sorting Complexes Required for Transport ; Gene Products, gag
Language	English
Publishing date	2016-04-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v8040103
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Article ; Online: Hepatitis B Virus Subverts the Autophagy Elongation Complex Atg5-12/16L1 and Does Not Require Atg8/LC3 Lipidation for Viral Maturation.

Döring, Tatjana / Zeyen, Lisa / Bartusch, Christina / Prange, Reinhild

Journal of virology

2018 Volume 92, Issue 7

Abstract: Previous studies indicated that hepatitis B virus (HBV) stimulates autophagy to favor its production. To understand how HBV co-opts autophagy as a proviral machinery, we studied the roles of key autophagy proteins in HBV-replicating liver cell cultures. ... ...

Abstract	Previous studies indicated that hepatitis B virus (HBV) stimulates autophagy to favor its production. To understand how HBV co-opts autophagy as a proviral machinery, we studied the roles of key autophagy proteins in HBV-replicating liver cell cultures. RNA interference-mediated silencing of Atg5, Atg12, and Atg16L1, which promote autophagophore expansion and LC3 membrane conjugation, interfered with viral core/nucleocapsid (NC) formation/stability and strongly diminished virus yields. Concomitantly, the core/NC membrane association and their sorting to envelope-positive compartments were perturbed. A close inspection of the HBV/autophagy cross talk revealed that the virus depended on Atg12 covalently conjugated to Atg5. In support of this finding, HBV required the E2-like enzymes Atg10 and Atg3, which catalyze or facilitate Atg5-12 conjugation, respectively. Atg10 and Atg3 knockdowns decreased HBV production, while Atg3 overexpression increased virus yields. Mapping analyses demonstrated that the HBV core protein encountered the Atg5-12/16L1 complex via interaction with the intrinsically disordered region of the Atg12 moiety that is dispensable for autophagy function. The role of Atg12 in HBV replication was confirmed by its incorporation into virions. Although the Atg5-12/16L1 complex and Atg3 are essential for LC3 lipidation and, thus, for autophagosome maturation and closure, HBV propagation did not require LC3. Silencing of LC3B, the most abundant LC3 isoform, did not inhibit but rather augmented virus production. Similar augmenting effects were obtained upon overexpression of a dominant negative mutant of Atg4B that blocked the lipid conjugation of the LC3 isoforms and their GABARAP paralogues. Together, our data indicate that HBV subverts early, nondegradative autophagy components as assembly scaffolds, thereby concurrently avoiding autophagosomal destruction.
MeSH term(s)	Autophagy ; Autophagy-Related Protein 12/genetics ; Autophagy-Related Protein 12/metabolism ; Autophagy-Related Protein 5/genetics ; Autophagy-Related Protein 5/metabolism ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Cell Line, Tumor ; Gene Knockdown Techniques ; Hepatitis B/genetics ; Hepatitis B/metabolism ; Hepatitis B/pathology ; Hepatitis B virus/physiology ; Humans ; Microtubule-Associated Proteins/genetics ; Microtubule-Associated Proteins/metabolism ; Multiprotein Complexes/genetics ; Multiprotein Complexes/metabolism ; Virus Replication/physiology
Chemical Substances	ATG12 protein, human ; ATG16L1 protein, human ; ATG5 protein, human ; Autophagy-Related Protein 12 ; Autophagy-Related Protein 5 ; Autophagy-Related Protein 8 Family ; Autophagy-Related Proteins ; GABARAPL2 protein, human ; MAP1LC3A protein, human ; Microtubule-Associated Proteins ; Multiprotein Complexes
Language	English
Publishing date	2018-03-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01513-17
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Article ; Online: Rab33B and its autophagic Atg5/12/16L1 effector assist in hepatitis B virus naked capsid formation and release.

Döring, Tatjana / Prange, Reinhild

Cellular microbiology

2015 Volume 17, Issue 5, Page(s) 747–764

Abstract: Hepatitis B virus morphogenesis is accompanied by the production and release of non-enveloped capsids/nucleocapsids. Capsid particles are formed inside the cell cytosol by multimerization of core protein subunits and ultimately exported in an uncommon ... ...

Abstract	Hepatitis B virus morphogenesis is accompanied by the production and release of non-enveloped capsids/nucleocapsids. Capsid particles are formed inside the cell cytosol by multimerization of core protein subunits and ultimately exported in an uncommon coatless state. Here, we investigated potential roles of Rab GTPases in capsid formation and trafficking by using RNA interference and overexpression studies. Naked capsid release does not require functions of the endosome-associated Rab5, Rab7 and Rab27 proteins, but depends on functional Rab33B, a GTPase participating in autophagosome formation via interaction with the Atg5-Atg12/Atg16L1 complex. During capsid formation, Rab33B acts in conjunction with its effector, as silencing of Atg5, Atg12 and Atg16L1 also impaired capsid egress. Analysis of capsid maturation steps revealed that Rab33B and Atg5/12/16L1 are required for proper particle assembly and/or stability. In support, the capsid protein was found to interact with Atg5 and colocalize with Atg5/12/16L1, implicating that autophagy pathway functions are involved in capsid biogenesis. However, a complete and functional autophagy pathway is dispensable for capsid release, as judged by knockdown analysis of Atg8/LC3 family members and pharmaceutical ablation of canonical autophagy. Experiments aimed at analysing the capsid release-stimulating activity of the Alix protein provide further evidence for a link between capsid formation and autophagy.
MeSH term(s)	Autophagy-Related Protein 12 ; Autophagy-Related Protein 5 ; Autophagy-Related Proteins ; Capsid/metabolism ; Carrier Proteins/metabolism ; Cell Line ; Gene Expression ; Gene Knockdown Techniques ; Hepatitis B virus/physiology ; Hepatocytes/virology ; Host-Pathogen Interactions ; Humans ; Microtubule-Associated Proteins/metabolism ; Protein Interaction Mapping ; Small Ubiquitin-Related Modifier Proteins/metabolism ; Virus Assembly ; Virus Release ; rab GTP-Binding Proteins/metabolism
Chemical Substances	ATG12 protein, human ; ATG16L1 protein, human ; ATG5 protein, human ; Autophagy-Related Protein 12 ; Autophagy-Related Protein 5 ; Autophagy-Related Proteins ; Carrier Proteins ; Microtubule-Associated Proteins ; Small Ubiquitin-Related Modifier Proteins ; RAB33B protein, human (EC 3.6.1.-) ; rab GTP-Binding Proteins (EC 3.6.5.2)
Keywords	covid19
Language	English
Publishing date	2015-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/cmi.12398
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Article: Hepatitis B Virus Exploits ERGIC-53 in Conjunction with COPII to Exit Cells

Zeyen, Lisa / Döring, Tatjana / Prange, Reinhild

Abstract	Several decades after its discovery, the hepatitis B virus (HBV) still displays one of the most successful pathogens in human populations worldwide. The identification and characterization of interactions between cellular and pathogenic components are essential for the development of antiviral treatments. Due to its small-sized genome, HBV highly depends on cellular functions to produce and export progeny particles. Deploying biochemical-silencing methods and molecular interaction studies in HBV-expressing liver cells, we herein identified the cellular ERGIC-53, a high-mannose-specific lectin, and distinct components of the endoplasmic reticulum (ER) export machinery COPII as crucial factors of viral trafficking and egress. Whereas the COPII subunits Sec24A, Sec23B and Sar1 are needed for both viral and subviral HBV particle exit, ERGIC-53 appears as an exclusive element of viral particle propagation, therefore interacting with the N146-glycan of the HBV envelope in a productive manner. Cell-imaging studies pointed to ER-derived, subcellular compartments where HBV assembly initiates. Moreover, our findings provide evidence that HBV exploits the functions of ERGIC-53 and Sec24A after the envelopment of nucleocapsids at these compartments in conjunction with endosomal sorting complexes required for transport (ESCRT) components. These data reveal novel insights into HBV assembly and trafficking, illustrating therapeutic prospects for intervening with the viral life cycle.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #718168
Database	COVID19

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