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Susanne Bailer
Max von Pettenkofer-Institute, Ludwig-Maximilians-University Munich, 80539 Munich, Germany

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Journal article
Published: 05 August 2021 in Viruses
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Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at the inner nuclear membrane, which is critical for this process. The nuclear import of both proteins ensues separately from each other: pUL31 is actively imported through the central pore channel, while pUL34 is transported along the peripheral pore membrane. With this study, we identified a functional bipartite NLS between residues 178 and 194 of pUL34. pUL34 lacking its NLS is mislocalized to the TGN but retargeted to the ER upon insertion of the authentic NLS or a mimic NLS, independent of the insertion site. If co-expressed with pUL31, either of the pUL34-NLS variants is efficiently, although not completely, targeted to the nuclear rim where co-localization with pUL31 and membrane budding seem to occur, comparable to the wild-type. The viral mutant HSV1(17+)Lox-UL34-NLS mt is modestly attenuated but viable and associated with localization of pUL34-NLS mt to both the nuclear periphery and cytoplasm. We propose that targeting of pUL34 to the INM is facilitated by, but not dependent on, the presence of an NLS, thereby supporting NEC formation and viral replication.

ACS Style

Christina Funk; Débora Marques Da Silveira E Santos; Melanie Ott; Verena Raschbichler; Susanne Bailer. The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex. Viruses 2021, 13, 1544 .

AMA Style

Christina Funk, Débora Marques Da Silveira E Santos, Melanie Ott, Verena Raschbichler, Susanne Bailer. The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex. Viruses. 2021; 13 (8):1544.

Chicago/Turabian Style

Christina Funk; Débora Marques Da Silveira E Santos; Melanie Ott; Verena Raschbichler; Susanne Bailer. 2021. "The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex." Viruses 13, no. 8: 1544.

Journal article
Published: 11 March 2020 in Viruses
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Nuclear egress is a regulated process shared by α-, β- and γ-herpesviruses. The core nuclear egress complex (NEC) is composed of the membrane-anchored protein homologs of human cytomegalovirus (HCMV) pUL50, murine cytomegalovirus (MCMV) pM50, Epstein–Barr virus (EBV) BFRF1 or varicella zoster virus (VZV) Orf24, which interact with the autologous NEC partners pUL53, pM53, BFLF2 or Orf27, respectively. Their recruitment of additional proteins leads to the assembly of a multicomponent NEC, coordinately regulating viral nucleocytoplasmic capsid egress. Here, the functionality of VZV, HCMV, MCMV and EBV core NECs was investigated by coimmunoprecipitation and confocal imaging analyses. Furthermore, a recombinant MCMV, harboring a replacement of ORF M50 by UL50, was analyzed both in vitro and in vivo. In essence, core NEC interactions were strictly limited to autologous NEC pairs and only included one measurable nonautologous interaction between the homologs of HCMV and MCMV. A comparative analysis of MCMV-WT versus MCMV-UL50-infected murine fibroblasts revealed almost identical phenotypes on the levels of protein and genomic replication kinetics. In infected BALB/c mice, virus spread to lung and other organs was found comparable between these viruses, thus stating functional complementarity. In conclusion, our study underlines that herpesviral core NEC proteins are functionally conserved regarding complementarity of core NEC interactions, which were found either virus-specific or restricted within subfamilies.

ACS Style

Sigrun Häge; Eric Sonntag; Eva Maria Borst; Pierre Tannig; Lisa Seyler; Tobias Bäuerle; Susanne M. Bailer; Chung-Pei Lee; Regina Müller; Christina Wangen; Jens Milbradt; Manfred Marschall. Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses. Viruses 2020, 12, 303 .

AMA Style

Sigrun Häge, Eric Sonntag, Eva Maria Borst, Pierre Tannig, Lisa Seyler, Tobias Bäuerle, Susanne M. Bailer, Chung-Pei Lee, Regina Müller, Christina Wangen, Jens Milbradt, Manfred Marschall. Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses. Viruses. 2020; 12 (3):303.

Chicago/Turabian Style

Sigrun Häge; Eric Sonntag; Eva Maria Borst; Pierre Tannig; Lisa Seyler; Tobias Bäuerle; Susanne M. Bailer; Chung-Pei Lee; Regina Müller; Christina Wangen; Jens Milbradt; Manfred Marschall. 2020. "Patterns of Autologous and Nonautologous Interactions between Core Nuclear Egress Complex (NEC) Proteins of α-, β- and γ-Herpesviruses." Viruses 12, no. 3: 303.

Original article
Published: 07 December 2018 in Traffic
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Morphogenesis of herpesviral virions is initiated in the nucleus but completed in the cytoplasm. Mature virions contain more than 25 tegument proteins many of which perform both nuclear and cytoplasmic functions suggesting they shuttle between these compartments. While nuclear import of herpesviral proteins was shown to be crucial for viral propagation, active nuclear export and its functional impact are still poorly understood. To systematically analyse nuclear export of tegument proteins present in virions of Herpes simplex virus type 1 (HSV1) and Epstein Barr virus (EBV), the Nuclear EXport Trapped by RAPamycin assay (NEX‐TRAP) was applied. Nine of the 22 investigated HSV1 tegument proteins including pUL4, pUL7, pUL11, pUL13, pUL21, pUL37d11, pUL47, pUL48, and pUS2 as well as two out of six EBV orthologs harbor nuclear export activity. A functional leucine‐rich nuclear export sequence (NES) recognized by the export factor CRM1/Xpo1 was identified in six of them. The comparison between experimental and bioinformatic data indicates that experimental validation of predicted NESes is required. Mutational analysis of the pUL48/VP16 NES revealed its importance for herpesviral propagation. Together our data suggest that nuclear export is an important feature of the herpesviral life cycle required to coordinate nuclear and cytoplasmic processes. This article is protected by copyright. All rights reserved.

ACS Style

Christina Funk; Verena Raschbichler; Diana Lieber; Jens Wetschky; Eileen K. Arnold; Jacqueline Leimser; Michael Biggel; Caroline C. Friedel; Zsolt Ruzsics; Susanne M. Bailer. Comprehensive analysis of nuclear export of herpes simplex virus type 1 tegument proteins and their Epstein‐Barr virus orthologs. Traffic 2018, 20, 152 -167.

AMA Style

Christina Funk, Verena Raschbichler, Diana Lieber, Jens Wetschky, Eileen K. Arnold, Jacqueline Leimser, Michael Biggel, Caroline C. Friedel, Zsolt Ruzsics, Susanne M. Bailer. Comprehensive analysis of nuclear export of herpes simplex virus type 1 tegument proteins and their Epstein‐Barr virus orthologs. Traffic. 2018; 20 (2):152-167.

Chicago/Turabian Style

Christina Funk; Verena Raschbichler; Diana Lieber; Jens Wetschky; Eileen K. Arnold; Jacqueline Leimser; Michael Biggel; Caroline C. Friedel; Zsolt Ruzsics; Susanne M. Bailer. 2018. "Comprehensive analysis of nuclear export of herpes simplex virus type 1 tegument proteins and their Epstein‐Barr virus orthologs." Traffic 20, no. 2: 152-167.

Review
Published: 25 November 2017 in Cells
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Herpesviral capsid assembly is initiated in the nucleoplasm of the infected cell. Size constraints require that newly formed viral nucleocapsids leave the nucleus by an evolutionarily conserved vescular transport mechanism called nuclear egress. Mature capsids released from the nucleoplasm are engaged in a membrane-mediated budding process, composed of primary envelopment at the inner nuclear membrane and de-envelopment at the outer nuclear membrane. Once in the cytoplasm, the capsids receive their secondary envelope for maturation into infectious virions. Two viral proteins conserved throughout the herpesvirus family, the integral membrane protein pUL34 and the phosphoprotein pUL31, form the nuclear egress complex required for capsid transport from the infected nucleus to the cytoplasm. Formation of the nuclear egress complex results in budding of membrane vesicles revealing its function as minimal virus-encoded membrane budding and scission machinery. The recent structural analysis unraveled details of the heterodimeric nuclear egress complex and the hexagonal coat it forms at the inside of budding vesicles to drive primary envelopment. With this review, I would like to present the capsid-escort-model where pUL31 associates with capsids in nucleoplasmic replication compartments for escort to sites of primary envelopment thereby coupling capsid maturation and nuclear egress.

ACS Style

Susanne M. Bailer. Venture from the Interior—Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane. Cells 2017, 6, 46 .

AMA Style

Susanne M. Bailer. Venture from the Interior—Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane. Cells. 2017; 6 (4):46.

Chicago/Turabian Style

Susanne M. Bailer. 2017. "Venture from the Interior—Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane." Cells 6, no. 4: 46.

Review
Published: 20 June 2017 in Virus Genes
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Herpesviruses are enveloped DNA viruses that infect vertebrate cells. Their high potential cloning capacity and the lifelong persistence of their genomes in various host cells make them attractive platforms for vector-based therapy. In this review, we would like to highlight recent advances of three major areas of herpesvirus vector development and application: (i) oncolytic therapy, (ii) recombinant vaccines, and (iii) large capacity gene transfer vehicles.

ACS Style

Susanne M. Bailer; Christina Funk; André Riedl; Zsolt Ruzsics. Herpesviral vectors and their application in oncolytic therapy, vaccination, and gene transfer. Virus Genes 2017, 53, 741 -748.

AMA Style

Susanne M. Bailer, Christina Funk, André Riedl, Zsolt Ruzsics. Herpesviral vectors and their application in oncolytic therapy, vaccination, and gene transfer. Virus Genes. 2017; 53 (5):741-748.

Chicago/Turabian Style

Susanne M. Bailer; Christina Funk; André Riedl; Zsolt Ruzsics. 2017. "Herpesviral vectors and their application in oncolytic therapy, vaccination, and gene transfer." Virus Genes 53, no. 5: 741-748.

Journal article
Published: 20 October 2016 in Virology Journal
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Herpes simplex virus type 1 (HSV1), a member of the alphaherpesvirinae, can cause recurrent facial lesions and encephalitis. Two membrane envelopment processes, one at the inner nuclear membrane and a second at cytoplasmic membranes are crucial for a productive viral infection. Depending on the subfamily, herpesviruses encode more than 11 different transmembrane proteins including members of the tail-anchored protein family. HSV1 encodes three tail-anchored proteins pUL34, pUL56 and pUS9 characterized by a single hydrophobic region positioned at their C-terminal end that needs to be released from the ribosome prior to posttranslational membrane insertion. Asna1/TRC40 is an ATPase that targets tail-anchored proteins to the endoplasmic reticulum in a receptor-dependent manner. Cell biological data point to a critical and general role of Asna1/TRC40 in tail-anchored protein biogenesis. With this study, we aimed to determine the importance of the tail-anchored insertion machinery for HSV1 infection. To determine protein-protein interactions, the yeast-two hybrid system was applied. Asna1/TRC40 was depleted using RNA interference. Transient transfection and virus infection experiments followed by indirect immunofluorescence analysis were applied to analyse the localization of viral proteins as well as the impact of Asna1/TRC40 depletion on virus infection. All HSV1 tail-anchored proteins specifically bound to Asna1/TRC40 but independently localized to their target membranes. While non-essential for cell viability, Asna1/TRC40 is required for efficient HSV1 replication. We show that early events of the replication cycle like virion entry and overall viral gene expression were unaffected by depletion of Asna1/TRC40. Furthermore, equal amounts of infectious virions were formed and remained cell-associated. This indicated that both nuclear egress of capsids that requires the essential tail-anchored protein pUL34, and secondary envelopment to form infectious virions were successfully completed. Despite large part of the virus life cycle proceeding normally, viral propagation was more than 10 fold reduced. We show that depletion of Asna1/TRC40 specifically affected a step late in infection during release of infectious virions to the extracellular milieu. Asna1/TRC40 is required at a late step of herpesviral infection for efficient release of mature virions to the extracellular milieu. This study reveals novel tools to decipher exocytosis of newly formed virions as well as hitherto unknown cellular targets for antiviral therapy.

ACS Style

Melanie Ott; Débora Marques; Christina Funk; Susanne M. Bailer. Asna1/TRC40 that mediates membrane insertion of tail-anchored proteins is required for efficient release of Herpes simplex virus 1 virions. Virology Journal 2016, 13, 175 .

AMA Style

Melanie Ott, Débora Marques, Christina Funk, Susanne M. Bailer. Asna1/TRC40 that mediates membrane insertion of tail-anchored proteins is required for efficient release of Herpes simplex virus 1 virions. Virology Journal. 2016; 13 (1):175.

Chicago/Turabian Style

Melanie Ott; Débora Marques; Christina Funk; Susanne M. Bailer. 2016. "Asna1/TRC40 that mediates membrane insertion of tail-anchored proteins is required for efficient release of Herpes simplex virus 1 virions." Virology Journal 13, no. 1: 175.

Journal article
Published: 17 March 2016 in Viruses
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The herpes simplex virus type 1 (HSV-1) glycoprotein N (gN/UL49.5) is a type I transmembrane protein conserved throughout the herpesvirus family. gN is a resident of the endoplasmic reticulum that in the presence of gM is translocated to the trans Golgi network. gM and gN are covalently linked by a single disulphide bond formed between cysteine 46 of gN and cysteine 59 of gM. Exit of gN from the endoplasmic reticulum requires the N-terminal core of gM composed of eight transmembrane domains but is independent of the C-terminal extension of gM. Co-transport of gN and gM to the trans Golgi network also occurs upon replacement of conserved cysteines in gM and gN, suggesting that their physical interaction is mediated by covalent and non-covalent forces. Deletion of gN/UL49.5 using bacterial artificial chromosome (BAC) mutagenesis generated mutant viruses with wild-type growth behaviour, while full deletion of gM/UL10 resulted in an attenuated phenotype. Deletion of gN/UL49.5 in conjunction with various gM/UL10 mutants reduced average plaque sizes to the same extent as either single gM/UL10 mutant, indicating that gN is nonessential for the function performed by gM. We propose that gN functions in gM-dependent as well as gM-independent processes during which it is complemented by other viral factors.

ACS Style

Hannah Striebinger; Christina Funk; Verena Raschbichler; Susanne M. Bailer. Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M. Viruses 2016, 8, 83 .

AMA Style

Hannah Striebinger, Christina Funk, Verena Raschbichler, Susanne M. Bailer. Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M. Viruses. 2016; 8 (3):83.

Chicago/Turabian Style

Hannah Striebinger; Christina Funk; Verena Raschbichler; Susanne M. Bailer. 2016. "Subcellular Trafficking and Functional Relationship of the HSV-1 Glycoproteins N and M." Viruses 8, no. 3: 83.

Research article
Published: 17 June 2015 in PLOS Pathogens
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Progeny capsids of herpesviruses leave the nucleus by budding through the nuclear envelope. Two viral proteins, the membrane protein pUL34 and the nucleo-phosphoprotein pUL31 form the nuclear egress complex that is required for capsid egress out of the nucleus. All pUL31 orthologs are composed of a diverse N-terminal domain with 1 to 3 basic patches and a conserved C-terminal domain. To decipher the functions of the N-terminal domain, we have generated several Herpes simplex virus mutants and show here that the N-terminal domain of pUL31 is essential with basic patches being critical for viral propagation. pUL31 and pUL34 entered the nucleus independently of each other via separate routes and the N-terminal domain of pUL31 was required to prevent their premature interaction in the cytoplasm. Unexpectedly, a classical bipartite nuclear localization signal embedded in this domain was not required for nuclear import of pUL31. In the nucleus, pUL31 associated with the nuclear envelope and newly formed capsids. Viral mutants lacking the N-terminal domain or with its basic patches neutralized still associated with nucleocapsids but were unable to translocate them to the nuclear envelope. Replacing the authentic basic patches with a novel artificial one resulted in HSV1(17+)Lox-UL31-hbpmp1mp2, that was viable but delayed in nuclear egress and compromised in viral production. Thus, while the C-terminal domain of pUL31 is sufficient for the interaction with nucleocapsids, the N-terminal domain was essential for capsid translocation to sites of nuclear egress and a coordinated interaction with pUL34. Our data indicate an orchestrated sequence of events with pUL31 binding to nucleocapsids and escorting them to the inner nuclear envelope. We propose a common mechanism for herpesviral nuclear egress: pUL31 is required for intranuclear translocation of nucleocapsids and subsequent interaction with pUL34 thereby coupling capsid maturation with primary envelopment. Herpesviral capsid assembly is initiated in the host nucleus. Due to size constraints, newly formed nucleocapsids are unable to leave the nucleus through the nuclear pore complex. Instead herpesviruses apply an evolutionarily conserved mechanism for nuclear export of capsids called nuclear egress. This process is initiated by docking of capsids at the inner nuclear membrane, budding of enveloped capsids into the perinuclear space followed by de-envelopment and release of capsids to the cytoplasm where further maturation occurs. Two viral proteins conserved throughout the herpesvirus family, the membrane protein pUL34 and the phosphoprotein pUL31 form the nuclear egress complex that is critical for primary envelopment. We show here that pUL31 and pUL34 enter the nucleus independently of each other. pUL31 is targeted to the nucleoplasm where it binds to nucleocapsids via the conserved C-terminal domain, while its N-terminal domain is important for capsid translocation to the nuclear envelope and for a coordinated interaction with pUL34. Our data suggest a mechanism that is apparently conserved among all herpesviruses with pUL31 escorting nucleocapsids to the nuclear envelope in order to couple capsid maturation with primary envelopment.

ACS Style

Christina Funk; Melanie Ott; Verena Raschbichler; Claus-Henning Nagel; Anne Binz; Beate Sodeik; Rudolf Bauerfeind; Susanne M. Bailer. The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain. PLOS Pathogens 2015, 11, e1004957 .

AMA Style

Christina Funk, Melanie Ott, Verena Raschbichler, Claus-Henning Nagel, Anne Binz, Beate Sodeik, Rudolf Bauerfeind, Susanne M. Bailer. The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain. PLOS Pathogens. 2015; 11 (6):e1004957.

Chicago/Turabian Style

Christina Funk; Melanie Ott; Verena Raschbichler; Claus-Henning Nagel; Anne Binz; Beate Sodeik; Rudolf Bauerfeind; Susanne M. Bailer. 2015. "The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal Domain." PLOS Pathogens 11, no. 6: e1004957.

Book chapter
Published: 20 July 2013 in Methods in Molecular Biology
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Quantification of infectious virus is crucial to many experimental approaches in virological research. A broadly used and facile technique is the so-called "plaque assay" which provides precise information on the absolute quantity of infectivity in a given volume. Due to advances in the understanding of viral gene expression, transactivator-promoter pairs have been identified which can be used in transgenic cell lines as reporters of viral infection. Even though such "cellular reporter assay" systems are mostly restricted to relative quantification, they are attractive tools which can complement or replace the conventional plaque assay. Cellular reporter assays become especially interesting in state-of-the-art high-throughput screening approaches, as for instance RNAi and compound library screens, since they are often compatible with small-scale and automated experimentation. In this chapter, a regular plaque assay as well as a cellular reporter assay employing a luciferase reporter gene are described. As an example, HSV-1 infectivity is assessed with both methods yielding complementary information. Advantages and disadvantages of the two techniques and possible applications are discussed.

ACS Style

Diana Lieber; Susanne M. Bailer. Determination of HSV-1 Infectivity by Plaque Assay and a Luciferase Reporter Cell Line. Methods in Molecular Biology 2013, 1064, 171 -181.

AMA Style

Diana Lieber, Susanne M. Bailer. Determination of HSV-1 Infectivity by Plaque Assay and a Luciferase Reporter Cell Line. Methods in Molecular Biology. 2013; 1064 ():171-181.

Chicago/Turabian Style

Diana Lieber; Susanne M. Bailer. 2013. "Determination of HSV-1 Infectivity by Plaque Assay and a Luciferase Reporter Cell Line." Methods in Molecular Biology 1064, no. : 171-181.

Journal article
Published: 30 September 2010 in FEBS Letters
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The heterogeneous nuclear ribonucleoprotein (hnRNP) K is an evolutionarily conserved protein with roles in signal transduction and gene expression. An impact of hnRNP K on the life cycle of a broad range of viral pathogens was reported while functional data for herpesviruses were lacking. In this study we show that hnRNP K is important for Herpes simplex virus 1 egress. In absence of hnRNP K, viral entry, gene expression, viral DNA replication, and maturation of nuclear particles appear normal whereas release of infectious virions to the extracellular space was significantly affected. Our results indicate that hnRNP K has an impact on a late step of herpesviral propagation making it a potential antiviral target

ACS Style

Tina Schmidt; Hannah Striebinger; Jürgen Haas; Susanne M. Bailer. The heterogeneous nuclear ribonucleoprotein K is important for Herpes simplex virus-1 propagation. FEBS Letters 2010, 584, 4361 -4365.

AMA Style

Tina Schmidt, Hannah Striebinger, Jürgen Haas, Susanne M. Bailer. The heterogeneous nuclear ribonucleoprotein K is important for Herpes simplex virus-1 propagation. FEBS Letters. 2010; 584 (20):4361-4365.

Chicago/Turabian Style

Tina Schmidt; Hannah Striebinger; Jürgen Haas; Susanne M. Bailer. 2010. "The heterogeneous nuclear ribonucleoprotein K is important for Herpes simplex virus-1 propagation." FEBS Letters 584, no. 20: 4361-4365.