Erratum for Barouch-Bentov et al., “Hepatitis C Virus Proteins Interact with the Endosomal Sorting Complex Required for Transport (ESCRT) Machinery via Ubiquitination To Facilitate Viral Envelopment”

Barouch-Bentov, Rina; Neveu, Grégory; Xiao, Fei; Melanie, Beer; Bekerman, Elena; Schor, Stanford; Campbell, Joseph R.; Boonyaratanakornkit, Jim; Lindenbach, Brett D.; Lu, Albert; Jacob, Yves; Einav, Shirit

doi:10.1128/mbio.02234-17

Cited by 4 publications

(25 citation statements)

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“…This reasoning also applies to a recent study by Mankouri et al, in which they conclude that the inhibition of Rab GTPase did not affect VLDL secretion and therefore that VLDLs are not associated with HCV secretion (28). Some studies implicated noncanonical secretion in HCV egress involving the endosomal compartments, autophagosomes, endocytic machinery, and ESCRT proteins (35)(36)(37)49). The presence of complex glycans on virus-associated glycoproteins substantiates that HCV virions traverse through the Golgi apparatus (43).…”

Section: Discussionmentioning

confidence: 74%

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Hepatitis C Virus Lipoviroparticles Assemble in the Endoplasmic Reticulum (ER) and Bud off from the ER to the Golgi Compartment in COPII Vesicles

Syed

Khan

Yang

et al. 2017

J Virol

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Hepatitis C virus (HCV) exists as a lipoprotein-virus hybrid lipoviroparticle (LVP).In vitro studies have demonstrated the importance of apolipoproteins in HCV secretion and infectivity, leading to the notion that HCV coopts the secretion of very-low-density lipoprotein (VLDL) for its egress. However, the mechanisms involved in virus particle assembly and egress are still elusive. The biogenesis of VLDL particles occurs in the endoplasmic reticulum (ER), followed by subsequent lipidation in the ER and Golgi compartment. The secretion of mature VLDL particles occurs through the Golgi secretory pathway. HCV virions are believed to latch onto or fuse with the nascent VLDL particle in either the ER or the Golgi compartment, resulting in the generation of LVPs. In our attempt to unravel the collaboration between HCV and VLDL secretion, we studied HCV particles budding from the ER en route to the Golgi compartment in COPII vesicles. Biophysical characterization of COPII vesicles fractionated on an iodixanol gradient revealed that HCV RNA is enriched in the highly buoyant COPII vesicle fractions and cofractionates with apolipoprotein B (ApoB), ApoE, and the HCV core and envelope proteins. Electron microscopy of immunogoldlabeled microsections revealed that the HCV envelope and core proteins colocalize with apolipoproteins and HCV RNA in Sec31-coated COPII vesicles. Ultrastructural analysis also revealed the presence of HCV structural proteins, RNA, and apolipoproteins in the Golgi stacks. These findings support the hypothesis that HCV LVPs assemble in the ER and are transported to the Golgi compartment in COPII vesicles to embark on the Golgi secretory route.IMPORTANCE HCV assembly and release accompany the formation of LVPs that circulate in the sera of HCV patients and are also produced in an in vitro culture system. The pathway of HCV morphogenesis and secretion has not been fully understood. This study investigates the exact site where the association of HCV virions with host lipoproteins occurs. Using immunoprecipitation of COPII vesicles and immunogold electron microscopy (EM), we characterize the existence of LVPs that cofractionate with lipoproteins, viral proteins, RNA, and vesicular components. Our results show that this assembly occurs in the ER, and LVPs thus formed are carried through the Golgi network by vesicular transport. This work provides a unique insight into the HCV LVP assembly process within infected cells and offers opportunities for designing antiviral therapeutic cellular targets.

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Section: Discussionmentioning

confidence: 74%

“…␤-Actin was used as an internal protein loading control. envelopment, signifying the role of ESCRT proteins in the budding of HCV virions into the ER (49). The interaction of HCV envelope proteins with lipoproteins in the ER further hints at the likely morphogenesis of HCV LVPs in the ER (50).…”

Section: Discussionmentioning

confidence: 99%

Hepatitis C Virus Lipoviroparticles Assemble in the Endoplasmic Reticulum (ER) and Bud off from the ER to the Golgi Compartment in COPII Vesicles

Syed

Khan

Yang

et al. 2017

J Virol

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“…In search of ubiquitin signaling proteins that mediate NS2 ubiquitination, we screened for interactions between a library of the ubiquitin proteasome system (UPS) proteins and NS2 via HT-GPCA (Biquand et al, 2017). This protein-fragment complementation assay (PCA) format relies on reversible reconstitution of a luciferase activity from split Gaussia luciferase reporters (GLuc1 and GLuc2) and provides a high-fidelity means to measure weak and transient interactions, such as those between ESCRT and cargo (K d in the mM range; Barouch-Bentov et al, 2016;Cassonnet et al, 2011;Hirano et al, 2006;Neveu et al, 2012;Raiborg et al, 2002). Moreover, it allows detection of interactions involving membrane proteins, such as NS2, in mammalian cells and within appropriate subcellular compartments (Barouch-Bentov et al, 2016;Xiao et al, 2018).…”

Section: Profiling Ubiquitin Signaling Interactors Of Ns2 Via a Proteomic Screenmentioning

confidence: 99%

“…This protein-fragment complementation assay (PCA) format relies on reversible reconstitution of a luciferase activity from split Gaussia luciferase reporters (GLuc1 and GLuc2) and provides a high-fidelity means to measure weak and transient interactions, such as those between ESCRT and cargo (K d in the mM range; Barouch-Bentov et al, 2016;Cassonnet et al, 2011;Hirano et al, 2006;Neveu et al, 2012;Raiborg et al, 2002). Moreover, it allows detection of interactions involving membrane proteins, such as NS2, in mammalian cells and within appropriate subcellular compartments (Barouch-Bentov et al, 2016;Xiao et al, 2018). The library used for this screen was recently assembled to screen for interactions with the PB2 polymerase protein of five influenza A virus strains and the E6 and E7 oncoproteins of human papilloma virus (Biquand et al, 2017;Poirson et al, 2017).…”

Section: Profiling Ubiquitin Signaling Interactors Of Ns2 Via a Proteomic Screenmentioning

confidence: 99%

“…Enveloped RNA viruses commonly recruit TSG101, Nedd4like E3 ubiquitin ligases, or Alix to enter the ESCRT network via late domains and bud from the plasma membrane (Votteler and Sundquist, 2013). In contrast, we reported that HRS (hepatocyte growth factor-regulated tyrosine kinase substrate) serves as the entry point for HCV, a virus lacking defined late domains, into the ESCRT pathway and has a role in HCV envelopment (Barouch-Bentov et al, 2016). Moreover, we demonstrated that K63 polyubiquitination of lysine residues within HCV NS2 mediates HRS binding and HCV assembly, thereby compensating for the absence of late domains (Barouch- .…”

Section: Introductionmentioning

confidence: 99%

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MARCH8 Ubiquitinates the Hepatitis C Virus Nonstructural 2 Protein and Mediates Viral Envelopment

et al. 2019

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Tegument Assembly, Secondary Envelopment and Exocytosis

Hogue

2022

Current Issues in Molecular Biology

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Alphaherpesvirus tegument assembly, secondary envelopment, and exocytosis processes are understood in broad strokes, but many of the individual steps in this pathway, and their molecular and cell biological details, remain unclear. Viral tegument and membrane proteins form an extensive and robust protein interaction network, such that essentially any structural protein can be deleted, yet particles are still assembled, enveloped, and released from infected cells.We conceptually divide the tegument proteins into three groups: conserved inner and outer teguments that participate in nucleocapsid and membrane contacts, respectively; and "middle" tegument proteins, consisting of some of the most abundant tegument proteins that serve as central hubs in the protein interaction network, yet which are unique to the alphaherpesviruses. We then discuss secondary envelopment, reviewing the tegument-membrane contacts and cellular factors that drive this process. We place this viral process in the context of cell biological processes, including the endocytic pathway, ESCRT machinery, autophagy, secretory pathway, intracellular transport, and exocytosis mechanisms. Finally, we speculate about potential relationships between caister.com/cimb 551 Curr. Issues Mol. Biol. Vol. 42 Curr. Issues Mol.

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Erratum for Barouch-Bentov et al., “Hepatitis C Virus Proteins Interact with the Endosomal Sorting Complex Required for Transport (ESCRT) Machinery via Ubiquitination To Facilitate Viral Envelopment”

Cited by 4 publications

References 0 publications

Hepatitis C Virus Lipoviroparticles Assemble in the Endoplasmic Reticulum (ER) and Bud off from the ER to the Golgi Compartment in COPII Vesicles

Hepatitis C Virus Lipoviroparticles Assemble in the Endoplasmic Reticulum (ER) and Bud off from the ER to the Golgi Compartment in COPII Vesicles

MARCH8 Ubiquitinates the Hepatitis C Virus Nonstructural 2 Protein and Mediates Viral Envelopment

Tegument Assembly, Secondary Envelopment and Exocytosis

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