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Journal articles on the topic 'Virus trafficking'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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1

Brandenburg, Boerries, and Xiaowei Zhuang. "Virus trafficking – learning from single-virus tracking." Nature Reviews Microbiology 5, no. 3 (March 2007): 197–208. http://dx.doi.org/10.1038/nrmicro1615.

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2

Spiropoulou, C. F., C. S. Goldsmith, T. R. Shoemaker, C. J. Peters, and R. W. Compans. "Sin nombre virus glycoprotein trafficking." Virology 308, no. 1 (March 2003): 48–63. http://dx.doi.org/10.1016/s0042-6822(02)00092-2.

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3

Wozniak, Ann L., Abby Long, Kellyann N. Jones-Jamtgaard, and Steven A. Weinman. "Hepatitis C virus promotes virion secretion through cleavage of the Rab7 adaptor protein RILP." Proceedings of the National Academy of Sciences 113, no. 44 (October 17, 2016): 12484–89. http://dx.doi.org/10.1073/pnas.1607277113.

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Hepatitis C virus (HCV) is an enveloped RNA virus that modifies intracellular trafficking processes. The mechanisms that HCV and other viruses use to modify these events are poorly understood. In this study, we observed that two different RNA viruses, HCV and Sendai, cause inhibition of ras-related protein Rab-7 (Rab7)-dependent endosome–lysosome fusion. In both cases, viral infection causes cleavage of the Rab7 adaptor protein RILP (Rab interacting lysosomal protein), which is responsible for linking Rab7 vesicles to dynein motor complexes. RILP cleavage results in the generation of a cleaved RILP fragment (cRILP) missing the N terminus of the molecule. Although RILP localizes in a perinuclear fashion, cRILP moves to the cell periphery. Both knockdown of RILP and expression of cRILP reproduced the HCV-induced trafficking defect, and restoring full-length RILP reversed the trafficking effects of virus. For the first 3 d after electroporation of HCV RNA, intracellular virus predominates over secreted virus, but the quantity of intracellular virus then rapidly declines as secreted virus dominates. The transition from the intracellular-predominant to the secretion-predominant phenotype corresponds to the time course of cRILP generation. Expressing cRILP directly prevents intracellular virus accumulation at early times without affecting net virus production. The ability of cRILP to promote virus secretion could be prevented by a kinesin inhibitor. HCV thus modifies cellular trafficking by cleaving RILP, which serves to redirect Rab7-containing vesicles to a kinesin-dependent trafficking mode promoting virion secretion. Cleavage of a Rab adaptor protein is thus a mechanism by which viruses modify trafficking patterns of infected cells.
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4

Jiang, Bingfu, and Eberhard Hildt. "Intracellular Trafficking of HBV Particles." Cells 9, no. 9 (September 2, 2020): 2023. http://dx.doi.org/10.3390/cells9092023.

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The human hepatitis B virus (HBV), that is causative for more than 240 million cases of chronic liver inflammation (hepatitis), is an enveloped virus with a partially double-stranded DNA genome. After virion uptake by receptor-mediated endocytosis, the viral nucleocapsid is transported towards the nuclear pore complex. In the nuclear basket, the nucleocapsid disassembles. The viral genome that is covalently linked to the viral polymerase, which harbors a bipartite NLS, is imported into the nucleus. Here, the partially double-stranded DNA genome is converted in a minichromosome-like structure, the covalently closed circular DNA (cccDNA). The DNA virus HBV replicates via a pregenomic RNA (pgRNA)-intermediate that is reverse transcribed into DNA. HBV-infected cells release apart from the infectious viral parrticle two forms of non-infectious subviral particles (spheres and filaments), which are assembled by the surface proteins but lack any capsid and nucleic acid. In addition, naked capsids are released by HBV replicating cells. Infectious viral particles and filaments are released via multivesicular bodies; spheres are secreted by the classic constitutive secretory pathway. The release of naked capsids is still not fully understood, autophagosomal processes are discussed. This review describes intracellular trafficking pathways involved in virus entry, morphogenesis and release of (sub)viral particles.
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5

Mouland, Andrew J., Hongbin Xu, Hongyi Cui, Winfried Krueger, Trent P. Munro, Melanie Prasol, Johanne Mercier, et al. "RNA Trafficking Signals in Human Immunodeficiency Virus Type 1." Molecular and Cellular Biology 21, no. 6 (March 15, 2001): 2133–43. http://dx.doi.org/10.1128/mcb.21.6.2133-2143.2001.

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ABSTRACT Intracellular trafficking of retroviral RNAs is a potential mechanism to target viral gene expression to specific regions of infected cells. Here we show that the human immunodeficiency virus type 1 (HIV-1) genome contains two sequences similar to the hnRNP A2 response element (A2RE), a cis-acting RNA trafficking sequence that binds to the trans-acting trafficking factor, hnRNP A2, and mediates a specific RNA trafficking pathway characterized extensively in oligodendrocytes. The two HIV-1 sequences, designated A2RE-1, within the major homology region of the gag gene, and A2RE-2, in a region of overlap between the vpr andtat genes, both bind to hnRNP A2 in vitro and are necessary and sufficient for RNA transport in oligodendrocytes in vivo. A single base change (A8G) in either sequence reduces hnRNP A2 binding and, in the case of A2RE-2, inhibits RNA transport. A2RE-mediated RNA transport is microtubule and hnRNP A2 dependent. Differentially labelledgag and vpr RNAs, containing A2RE-1 and A2RE-2, respectively, coassemble into the same RNA trafficking granules and are cotransported to the periphery of the cell. tat RNA, although it contains A2RE-2, is not transported as efficiently asvpr RNA. An A2RE/hnRNP A2-mediated trafficking pathway for HIV RNA is proposed, and the role of RNA trafficking in targeting HIV gene expression is discussed.
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6

Mankouri, Jamel, Cheryl Walter, Hazel Stewart, Matthew Bentham, Wei Sun Park, Won Do Heo, Mitsunori Fukuda, Stephen Griffin, and Mark Harris. "Release of Infectious Hepatitis C Virus from Huh7 Cells Occurs via atrans-Golgi Network-to-Endosome Pathway Independent of Very-Low-Density Lipoprotein Secretion." Journal of Virology 90, no. 16 (May 25, 2016): 7159–70. http://dx.doi.org/10.1128/jvi.00826-16.

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ABSTRACTThe release of infectious hepatitis C virus (HCV) particles from infected cells remains poorly characterized. We previously demonstrated that virus release is dependent on the endosomal sorting complex required for transport (ESCRT). Here, we show a critical role oftrans-Golgi network (TGN)-endosome trafficking during the assembly, but principally the secretion, of infectious virus. This was demonstrated by both small interfering RNA (siRNA)-mediated silencing of TGN-associated adaptor proteins and a panel of dominant negative (DN) Rab GTPases involved in TGN-endosome trafficking steps. Importantly, interfering with factors critical for HCV release did not have a concomitant effect on secretion of triglycerides, ApoB, or ApoE, indicating that particles are likely released from Huh7 cells via pathways distinct from that of very-low-density lipoprotein (VLDL). Finally, we show that HCV NS2 perturbs TGN architecture, redistributing TGN membranes to closely associate with HCV core protein residing on lipid droplets. These findings support the notion that HCV hijacks TGN-endosome trafficking to facilitate particle assembly and release. Moreover, although essential for assembly and infectivity, the trafficking of mature virions is seemingly independent of host lipoproteins.IMPORTANCEThe mechanisms by which infectious hepatitis C virus particles are assembled and released from the cell are poorly understood. We show that the virus subverts host cell trafficking pathways to effect the release of virus particles and disrupts the structure of the Golgi apparatus, a key cellular organelle involved in secretion. In addition, we demonstrate that the mechanisms used by the virus to exit the cell are distinct from those used by the cell to release lipoproteins, suggesting that the virus effects a unique modification to cellular trafficking pathways.
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7

Hsiao, Jye-Chian, Li-Wei Chu, Yung-Tsun Lo, Sue-Ping Lee, Tzu-Jung Chen, Cheng-Yen Huang, Yueh-Hsin Ping, and Wen Chang. "Intracellular Transport of Vaccinia Virus in HeLa Cells Requires WASH-VPEF/FAM21-Retromer Complexes and Recycling Molecules Rab11 and Rab22." Journal of Virology 89, no. 16 (June 3, 2015): 8365–82. http://dx.doi.org/10.1128/jvi.00209-15.

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ABSTRACTVaccinia virus, the prototype of theOrthopoxvirusgenus in the familyPoxviridae, infects a wide range of cell lines and animals. Vaccinia mature virus particles of the WR strain reportedly enter HeLa cells through fluid-phase endocytosis. However, the intracellular trafficking process of the vaccinia mature virus between cellular uptake and membrane fusion remains unknown. We used live imaging of single virus particles with a combination of various cellular vesicle markers, to track fluorescent vaccinia mature virus particle movement in cells. Furthermore, we performed functional interference assays to perturb distinct vesicle trafficking processes in order to delineate the specific route undertaken by vaccinia mature virus prior to membrane fusion and virus core uncoating in cells. Our results showed that vaccinia virus traffics to early endosomes, where recycling endosome markers Rab11 and Rab22 are recruited to participate in subsequent virus trafficking prior to virus core uncoating in the cytoplasm. Furthermore, we identified WASH-VPEF/FAM21-retromer complexes that mediate endosome fission and sorting of virus-containing vesicles prior to virus core uncoating in the cytoplasm.IMPORTANCEVaccinia mature virions of the WR strain enter HeLa cells through fluid phase endocytosis. We previously demonstrated that virus-containing vesicles are internalized into phosphatidylinositol 3-phosphate positive macropinosomes, which are then fused with Rab5-positive early endosomes. However, the subsequent process of sorting the virion-containing vesicles prior to membrane fusion remains unclear. We dissected the intracellular trafficking pathway of vaccinia mature virions in cells up to virus core uncoating in cytoplasm. We show that vaccinia mature virions first travel to early endosomes. Subsequent trafficking events require the important endosome-tethered protein VPEF/FAM21, which recruits WASH and retromer protein complexes to the endosome. There, the complex executes endosomal membrane fission and cargo sorting to the Rab11-positive and Rab22-positive recycling pathway, resulting in membrane fusion and virus core uncoating in the cytoplasm.
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8

Counihan, Natalie A., Stephen M. Rawlinson, and Brett D. Lindenbach. "Trafficking of Hepatitis C Virus Core Protein during Virus Particle Assembly." PLoS Pathogens 7, no. 10 (October 20, 2011): e1002302. http://dx.doi.org/10.1371/journal.ppat.1002302.

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9

Gilbert, Joanna M., Ilya G. Goldberg, and Thomas L. Benjamin. "Cell Penetration and Trafficking of Polyomavirus." Journal of Virology 77, no. 4 (February 15, 2003): 2615–22. http://dx.doi.org/10.1128/jvi.77.4.2615-2622.2003.

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ABSTRACT The murine polyomavirus (Py) enters mouse fibroblasts and kidney epithelial cells via an endocytic pathway that is caveola-independent (as well as clathrin-independent). In contrast, uptake of simian virus 40 into the same cells is dependent on caveola. Following the initial uptake of Py, both microtubules and microfilaments play roles in trafficking of the virus to the nucleus. Colcemid, which disrupts microtubules, inhibits the ability of Py to reach the nucleus and replicate. Paclitaxel, which stabilizes microtubules and prevents microtubule turnover, has no effect, indicating that intact but not dynamic microtubules are required for Py infectivity. Compounds that disrupt actin filaments enhance Py uptake while stabilization of actin filaments impedes Py infection. Virus particles are seen in association with actin in cells treated with microfilament-disrupting or filament-stabilizing agents at levels comparable to those in untreated cells, suggesting that a dynamic state of the microfilament system is important for Py infectivity.
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10

Miao, Congrong, Gertrud U. Radu, Hayat Caidi, Ralph A. Tripp, Larry J. Anderson, and Lia M. Haynes. "Treatment with respiratory syncytial virus G glycoprotein monoclonal antibody or F(ab′)2 components mediates reduced pulmonary inflammation in mice." Journal of General Virology 90, no. 5 (May 1, 2009): 1119–23. http://dx.doi.org/10.1099/vir.0.009308-0.

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Therapeutic treatment with a non-neutralizing monoclonal antibody (mAb) (131-2G) specific to respiratory syncytial virus (RSV) G glycoprotein mediates virus clearance and decreases leukocyte trafficking and interferon gamma (IFN-γ) production in the lungs of RSV-infected mice. Its F(ab′)2 component only mediates decreased leukocyte trafficking and IFN-γ production without reducing virus replication. Thus, this mAb has two independent actions that could facilitate treatment and/or prevention of RSV infection by reducing both virus replication and virus-induced pulmonary inflammation.
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11

Daniel, Gina R., Patricia J. Sollars, Gary E. Pickard, and Gregory A. Smith. "Pseudorabies Virus Fast Axonal Transport Occurs by a pUS9-Independent Mechanism." Journal of Virology 89, no. 15 (May 20, 2015): 8088–91. http://dx.doi.org/10.1128/jvi.00771-15.

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Reactivation from latency results in transmission of neurotropic herpesviruses from the nervous system to body surfaces, referred to as anterograde axonal trafficking. The virus-encoded protein pUS9 promotes axonal dissemination by sorting virus particles into axons, but whether it is also an effector of fast axonal transport within axons is unknown. To determine the role of pUS9 in anterograde trafficking, we analyzed the axonal transport of pseudorabies virus in the presence and absence of pUS9.
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12

Stidwill, Robert P., and Urs F. Greber. "Intracellular Virus Trafficking Reveals Physiological Characteristics of the Cytoskeleton." Physiology 15, no. 2 (April 2000): 67–71. http://dx.doi.org/10.1152/physiologyonline.2000.15.2.67.

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Virus particles that infect eukaryotic cells can take advantage of the cytoskeleton and associated motors to translocate through the cytoplasm. Depending on the virus, motor proteins are recruited or, alternatively, cytoskeletal elements are induced to polymerize onto viral structures. Here we review recent advances toward understanding the roles of the cytoskeleton in virus trafficking.
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13

Ramos-Nascimento, Ana, Bárbara Kellen, Filipe Ferreira, Marta Alenquer, Sílvia Vale-Costa, Graça Raposo, Cédric Delevoye, and Maria João Amorim. "KIF13A mediates trafficking of influenza A virus ribonucleoproteins." Journal of Cell Science 130, no. 23 (October 23, 2017): 4038–50. http://dx.doi.org/10.1242/jcs.210807.

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14

Mues, Mascha B., Natalia Cheshenko, Duncan W. Wilson, Leslie Gunther-Cummins, and Betsy C. Herold. "Dynasore Disrupts Trafficking of Herpes Simplex Virus Proteins." Journal of Virology 89, no. 13 (April 15, 2015): 6673–84. http://dx.doi.org/10.1128/jvi.00636-15.

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ABSTRACTDynasore, a small-molecule inhibitor of the GTPase activity of dynamin, inhibits the entry of several viruses, including herpes simplex virus (HSV), but its impact on other steps in the viral life cycle has not been delineated. The current study was designed to test the hypothesis that dynamin is required for viral protein trafficking and thus has pleiotropic inhibitory effects on HSV infection. Dynasore inhibited HSV-1 and HSV-2 infection of human epithelial and neuronal cells, including primary genital tract cells and human fetal neurons and astrocytes. Similar results were obtained when cells were transfected with a plasmid expressing dominant negative dynamin. Kinetic studies demonstrated that dynasore reduced the number of viral capsids reaching the nuclear pore if added at the time of viral entry and that, when added as late as 8 h postentry, dynasore blocked the transport of newly synthesized viral proteins from the nucleus to the cytosol. Proximity ligation assays demonstrated that treatment with dynasore prevented the colocalization of VP5 and dynamin. This resulted in a reduction in the number of viral capsids isolated from sucrose gradients. Fewer capsids were observed by electron microscopy in dynasore-treated cells than in control-treated cells. There were also reductions in infectious progeny released into culture supernatants and in cell-to-cell spread. Together, these findings suggest that targeting dynamin-HSV interactions may provide a new strategy for HSV treatment and prevention.IMPORTANCEHSV infections remain a global health problem associated with significant morbidity, particularly in neonates and immunocompromised hosts, highlighting the need for novel approaches to treatment and prevention. The current studies indicate that dynamin plays a role in multiple steps in the viral life cycle and provides a new target for antiviral therapy. Dynasore, a small-molecule inhibitor of dynamin, has pleiotropic effects on HSV-1 and HSV-2 infection and impedes viral entry, trafficking of viral proteins, and capsid formation.
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15

Dugan, A. S., S. Eash, and W. J. Atwood. "Update on BK virus entry and intracellular trafficking." Transplant Infectious Disease 8, no. 2 (June 2006): 62–67. http://dx.doi.org/10.1111/j.1399-3062.2006.00153.x.

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16

Whittaker, G., M. Bui, and A. Helenius. "Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons." Journal of virology 70, no. 5 (1996): 2743–56. http://dx.doi.org/10.1128/jvi.70.5.2743-2756.1996.

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17

Balasubramaniam, Muthukumar, and Eric O. Freed. "New Insights into HIV Assembly and Trafficking." Physiology 26, no. 4 (August 2011): 236–51. http://dx.doi.org/10.1152/physiol.00051.2010.

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Assembly and release of human immunodeficiency virus type 1 (HIV-1) particles is mediated by the viral Gag polyprotein precursor. Gag is synthesized in the cytosol and rapidly translocates to membrane to orchestrate particle production. The cell biology of HIV-1 Gag trafficking is currently one of the least understood aspects of HIV-1 replication. In this review, we highlight the current understanding of the cellular machinery involved in Gag trafficking and virus assembly.
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Sieczkarski, Sara B., H. Alex Brown, and Gary R. Whittaker. "Role of Protein Kinase C βII in Influenza Virus Entry via Late Endosomes." Journal of Virology 77, no. 1 (January 1, 2003): 460–69. http://dx.doi.org/10.1128/jvi.77.1.460-469.2003.

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ABSTRACT Many viruses take advantage of receptor-mediated endocytosis in order to enter target cells. We have utilized influenza virus and Semliki Forest virus (SFV) to define a role for protein kinase C βII (PKCβII) in endocytic trafficking. We show that specific PKC inhibitors prevent influenza virus infection, suggesting a role for classical isoforms of PKC. We also examined virus entry in cells overexpressing dominant-negative forms of PKCα and -β. Cells expressing a phosphorylation-deficient form of PKCβII (T500V), but not an equivalent mutant form of PKCα, inhibited successful influenza virus entry—with the virus accumulating in late endosomes. SFV, however, believed to enter cells from the early endosome, was unaffected by PKCβII T500V expression. We also examined the trafficking of two cellular ligands, transferrin and epidermal growth factor (EGF). PKCβII T500V expression specifically blocked EGF receptor trafficking and degradation, without affecting transferrin receptor recycling. As with influenza virus, in PKCβII kinase-dead cells, EGF receptor was trapped in a late endosome compartment. Our findings suggest that PKCβII is an important regulator of a late endosomal sorting event needed for influenza virus entry and infection.
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Whittaker, Gary R. "Intracellular trafficking of influenza virus: clinical implications for molecular medicine." Expert Reviews in Molecular Medicine 3, no. 5 (February 8, 2001): 1–13. http://dx.doi.org/10.1017/s1462399401002447.

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The trafficking and processing steps that occur in cells that are infected with influenza virus play a crucial role in the outcome of infection. These steps are targets for new and future anti-viral drugs, and can affect the relative virulence of the virus and its ability to cause disease. The virus first binds to its host cell via specific sialic acid residues, which can control the species tropism of the virus. The internalisation of the virus, into the nucleus of the cell, is dependent on a low pH, and this process is therapeutically targeted by the drug amantadine. Following replication, the newly formed viral genomes leave the nucleus and assemble into infectious particles at the plasma membrane. The targeting and processing of the various viral components at this late stage of the infectious cycle can have a major effect on the ability of the virus to spread and cause disease in its host. Finally, the release of viruses is dependent on the enzyme neuraminidase (NA), and this function has recently been targeted by the NA inhibitors, a new generation of drugs against influenza virus.
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20

Celma, Cristina C. P., and Polly Roy. "A Viral Nonstructural Protein Regulates Bluetongue Virus Trafficking and Release." Journal of Virology 83, no. 13 (April 15, 2009): 6806–16. http://dx.doi.org/10.1128/jvi.00263-09.

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ABSTRACT Bluetongue virus (BTV), a nonenveloped insect-borne virus, is released from infected cells by multiple pathways. Unlike other nonenveloped viruses, in addition to cell lysis the newly synthesized virus particles also appear to use a unique “budding” process. The nonstructural protein NS3, the only membrane protein encoded by BTV in infected cells, has been implicated in this process, since it appears to interact not only with the outermost viral capsid protein VP2 but also with a component of the cellular ESCRT pathway. However, to date it had not been possible to obtain direct evidence for the involvement of NS3 in BTV morphogenesis due to the lack of a genetic system that would allow introducing the targeted mutation in NS3 gene. In this study, we have used the recently developed T7 transcript-based reverse genetics system for BTV to introduce mutations in the sequence of NS3 into the viral genome and have investigated the effect of these mutations in the context of a replicating virus. While certain NS3 mutations exhibited drastic effects on newly synthesized virus release, others had less pronounced effects. In particular, mutations of two residues in the Tsg101 binding motif, the putative L domain of NS3, altered normal virus egress patterns and left nascent particles tethered to the cellular membrane, apparently arrested in the process of budding. In cells infected with a mutant virus that was incapable of an NS3-VP2 interaction, no budding particles were visualized. These data suggest that NS3 may act like the membrane protein of enveloped viruses and is responsible for intracellular trafficking and budding of virus particles. NS3 is thus a bridge between the maturing virion particles and cellular proteins during virus egress.
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Siddiqa, Abida, Justyna Broniarczyk, and Lawrence Banks. "Papillomaviruses and Endocytic Trafficking." International Journal of Molecular Sciences 19, no. 9 (September 4, 2018): 2619. http://dx.doi.org/10.3390/ijms19092619.

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Endocytic trafficking plays a major role in transport of incoming human papillomavirus (HPVs) from plasma membrane to the trans Golgi network (TGN) and ultimately into the nucleus. During this infectious entry, several cellular sorting factors are recruited by the viral capsid protein L2, which plays a critical role in ensuring successful transport of the L2/viral DNA complex to the nucleus. Later in the infection cycle, two viral oncoproteins, E5 and E6, have also been shown to modulate different aspects of endocytic transport pathways. In this review, we highlight how HPV makes use of and perturbs normal endocytic transport pathways, firstly to achieve infectious virus entry, secondly to produce productive infection and the completion of the viral life cycle and, finally, on rare occasions, to bring about the development of malignancy.
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22

Whitman, Shannon D., Everett Clinton Smith, and Rebecca Ellis Dutch. "Differential Rates of Protein Folding and Cellular Trafficking for the Hendra Virus F and G Proteins: Implications for F-G Complex Formation." Journal of Virology 83, no. 17 (June 24, 2009): 8998–9001. http://dx.doi.org/10.1128/jvi.00414-09.

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ABSTRACT Hendra virus F protein-promoted membrane fusion requires the presence of the viral attachment protein, G. However, events leading to the association of these glycoproteins remain unclear. Results presented here demonstrate that Hendra virus G undergoes slower secretory pathway trafficking than is observed for Hendra virus F. This slowed trafficking is not dependent on the G protein cytoplasmic tail, the presence of the G receptor ephrin B2, or interaction with other viral proteins. Instead, Hendra virus G was found to undergo intrinsically slow oligomerization within the endoplasmic reticulum. These results suggest that the critical F-G interactions occur only after the initial steps of synthesis and cellular transport.
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Chu, J. J. H., and M. L. Ng. "Infectious Entry of West Nile Virus Occurs through a Clathrin-Mediated Endocytic Pathway." Journal of Virology 78, no. 19 (October 1, 2004): 10543–55. http://dx.doi.org/10.1128/jvi.78.19.10543-10555.2004.

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ABSTRACT The pathway of West Nile flavivirus early internalization events was mapped in detail in this study. Overexpression of dominant-negative mutants of Eps15 strongly inhibits West Nile virus (WNV) internalization, and pharmacological drugs that blocks clathrin also caused a marked reduction in virus entry but not caveola-dependent endocytosis inhibitory agent, filipin. Using immunocryoelectron microscopy, WNV particles were seen within clathrin-coated pits after 2 min postinfection. Double-labeling immunofluorescence assays and immunoelectron microscopy performed with anti-WNV envelope or capsid proteins and cellular markers (EEA1 and LAMP1) revealed the trafficking pathway of internalized virus particles from early endosomes to lysosomes and finally the uncoating of the virus particles. Disruption of host cell cytoskeleton (actin filaments and microtubules) with cytochalasin D and nocodazole showed significant reduction in virus infectivity. Actin filaments are shown to be essential during the initial penetration of the virus across the plasma membrane, whereas microtubules are involved in the trafficking of internalized virus from early endosomes to lysosomes for uncoating. Cells treated with lysosomotropic agents were largely resistant to infection, indicating that a low-pH-dependent step is required for WNV infection. In situ hybridization of DNA probes specific for viral RNA demonstrated the trafficking of uncoated viral RNA genomes to the endoplasmic reticulum.
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Isogai, M., Y. Saitou, N. Takahashi, T. Itabashi, M. Terada, H. Satoh, and N. Yoshikawa. "The 50-kDa Protein of Apple chlorotic leaf spot virus Interferes with Intracellular and Intercellular Targeting and Tubule-Inducing Activity of the 39-kDa Protein of Grapevine berry inner necrosis virus." Molecular Plant-Microbe Interactions® 16, no. 3 (March 2003): 188–95. http://dx.doi.org/10.1094/mpmi.2003.16.3.188.

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To understand why transgenic Nicotiana occidentalis plants expressing a functional movement protein (MP) of Apple chlorotic leaf spot virus (ACLSV) show specific resistance to Grapevine berry inner necrosis virus (GINV), the MPs of ACLSV (50KP) and GINV (39KP) were fused to green, yellow, or cyan fluorescent proteins (GFP, YFP, or CFP). These fusion proteins were transiently expressed in leaf cells of both transgenic (50KP) and nontransgenic (NT) plants, and the intracellular and intercellular trafficking and tubule-inducing activity of these proteins were compared. The results indicate that in epidermal cells and protoplasts from 50KP plant leaves, the trafficking and tubule-inducing activities of GINV-39KP were specifically blocked while those of ACLSV-50KP and Apple stem grooving virus MP (36KP) were not affected. Additionally, when 39KP-YFP and 50KP-CFP were coexpressed in the leaf epidermis of NT plants, the fluorescence of both proteins was confined to single cells, indicating that 50KP-CFP interferes with the cell-to-cell trafficking of 39KP-YFP and vice versa. Mutational analyses of 50KP showed that the deletion mutants that retained the activities described above still blocked cell-to-cell trafficking of 39KP, but the dysfunctional 50KP mutants could no longer impede cell-to-cell movement of 39KP. Transgenic plants expressing the functional 50KP deletion mutants showed specific resistance against GINV. In contrast, transgenic plants expressing the dysfunctional 50KP mutants did not show any resistance to the virus. From these results, we conclude that the specific resistance of 50KP plants to GINV is due to the ability of the 50KP to block intracellular and intercellular trafficking of GINV 39KP.
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Hutt-Fletcher, Lindsey. "Epstein-Barr Virus: Cell Trafficking Is Crucial for Persistence." Microbe Magazine 9, no. 6 (June 1, 2014): 245–49. http://dx.doi.org/10.1128/microbe.9.245.1.

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26

Chu, J. J. H., and M. L. Ng. "Trafficking mechanism of west Nile (Sarafend) virus structural proteins." Journal of Medical Virology 67, no. 1 (March 13, 2002): 127–36. http://dx.doi.org/10.1002/jmv.2201.

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27

Elton, Debra, Maria Joao Amorim, Liz Medcalf, and Paul Digard. "‘Genome gating’; polarized intranuclear trafficking of influenza virus RNPs." Biology Letters 1, no. 2 (April 22, 2005): 113–17. http://dx.doi.org/10.1098/rsbl.2004.0253.

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28

Holcman, D. "Modeling DNA and Virus Trafficking in the Cell Cytoplasm." Journal of Statistical Physics 127, no. 3 (February 13, 2007): 471–94. http://dx.doi.org/10.1007/s10955-007-9282-4.

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Gottschalk, Elinor Y., and Patricio I. Meneses. "A Dual Role for the Nonreceptor Tyrosine Kinase Pyk2 during the Intracellular Trafficking of Human Papillomavirus 16." Journal of Virology 89, no. 17 (June 24, 2015): 9103–14. http://dx.doi.org/10.1128/jvi.01183-15.

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ABSTRACTThe infectious process of human papillomaviruses (HPVs) has been studied considerably, and many cellular components required for viral entry and trafficking continue to be revealed. In this study, we investigated the role of the nonreceptor tyrosine kinase Pyk2 during HPV16 pseudovirion infection of human keratinocytes. We found that Pyk2 is necessary for infection and appears to be involved in the intracellular trafficking of the virus. Small interfering RNA-mediated reduction of Pyk2 resulted in a significant decrease in infection but did not prevent viral entry at the plasma membrane. Pyk2 depletion resulted in altered endolysosomal trafficking of HPV16 and accelerated unfolding of the viral capsid. Furthermore, we observed retention of the HPV16 pseudogenome in thetrans-Golgi network (TGN) in Pyk2-depleted cells, suggesting that the kinase could be required for the viral DNA to exit the TGN. While Pyk2 has previously been shown to function during the entry of enveloped viruses at the plasma membrane, the kinase has not yet been implicated in the intracellular trafficking of a nonenveloped virus such as HPV. Additionally, these data enrich the current literature on Pyk2's function in human keratinocytes.IMPORTANCEIn this study, we investigated the role of the nonreceptor tyrosine kinase Pyk2 during human papillomavirus (HPV) infection of human skin cells. Infections with high-risk types of HPV such as HPV16 are the leading cause of cervical cancer and a major cause of genital and oropharyngeal cancer. As a nonenveloped virus, HPV enters cells by interacting with cellular receptors and established cellular trafficking routes to ensure that the viral DNA reaches the nucleus for productive infection. This study identified Pyk2 as a cellular component required for the intracellular trafficking of HPV16 during infection. Understanding the infectious pathways of HPVs is critical for developing additional preventive therapies. Furthermore, this study advances our knowledge of intracellular trafficking processes in keratinocytes.
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Harrison, Angela R., Shawn Todd, Megan Dearnley, Cassandra T. David, Diane Green, Stephen M. Rawlinson, Gough G. Au, Glenn A. Marsh, and Gregory W. Moseley. "Antagonism of STAT3 signalling by Ebola virus." PLOS Pathogens 17, no. 6 (June 24, 2021): e1009636. http://dx.doi.org/10.1371/journal.ppat.1009636.

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Many viruses target signal transducers and activators of transcription (STAT) 1 and 2 to antagonise antiviral interferon signalling, but targeting of signalling by other STATs/cytokines, including STAT3/interleukin 6 that regulate processes important to Ebola virus (EBOV) haemorrhagic fever, is poorly defined. We report that EBOV potently inhibits STAT3 responses to interleukin-6 family cytokines, and that this is mediated by the interferon-antagonist VP24. Mechanistic analysis indicates that VP24 effects a unique strategy combining distinct karyopherin-dependent and karyopherin-independent mechanisms to antagonise STAT3-STAT1 heterodimers and STAT3 homodimers, respectively. This appears to reflect distinct mechanisms of nuclear trafficking of the STAT3 complexes, revealed for the first time by our analysis of VP24 function. These findings are consistent with major roles for global inhibition of STAT3 signalling in EBOV infection, and provide new insights into the molecular mechanisms of STAT3 nuclear trafficking, significant to pathogen-host interactions, cell physiology and pathologies such as cancer.
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Canto, Tomas, and Peter Palukaitis. "Replicase-Mediated Resistance to Cucumber Mosaic Virus Does Not Inhibit Localization and/or Trafficking of the Viral Movement Protein." Molecular Plant-Microbe Interactions® 12, no. 8 (August 1999): 743–47. http://dx.doi.org/10.1094/mpmi.1999.12.8.743.

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Replicase-mediated resistance to cucumber mosaic virus (CMV) affects CMV replication and restricts CMV movement. Confocal laser scanning microscopic analysis of resistant plants inoculated with either CMV or potato virus X, expressing the CMV movement protein (MP) fused to the green fluorescent protein (GFP), showed that the CMV MP was not inhibited from either plasmodesmal association or trafficking in the CMV-resistant plants. CMV expressing free GFP was able to move to adjacent cells, demonstrating that replicase-mediated resistance did not directly block the trafficking of CMV RNA.
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Cheerathodi, Mujeeb, Dingani Nkosi, Allaura S. Cone, Sara B. York, and David G. Meckes. "Epstein-Barr Virus LMP1 Modulates the CD63 Interactome." Viruses 13, no. 4 (April 15, 2021): 675. http://dx.doi.org/10.3390/v13040675.

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Tetraspanin CD63 is a cluster of cell surface proteins with four transmembrane domains; it is associated with tetraspanin-enriched microdomains and typically localizes to late endosomes and lysosomes. CD63 plays an important role in the cellular trafficking of different proteins, EV cargo sorting, and vesicle formation. We have previously shown that CD63 is important in LMP1 trafficking to EVs, and this also affects LMP1-mediated intracellular signaling including MAPK/ERK, NF-κB, and mTOR activation. Using the BioID method combined with mass spectrometry, we sought to define the broad CD63 interactome and how LMP1 modulates this network of interacting proteins. We identified a total of 1600 total proteins as a network of proximal interacting proteins to CD63. Biological process enrichment analysis revealed significant involvement in signal transduction, cell communication, protein metabolism, and transportation. The CD63-only interactome was enriched in Rab GTPases, SNARE proteins, and sorting nexins, while adding LMP1 into the interactome increased the presence of signaling and ribosomal proteins. Our results showed that LMP1 alters the CD63 interactome, shifting the network of protein enrichment from protein localization and vesicle-mediated transportation to metabolic processes and translation. We also show that LMP1 interacts with mTOR, Nedd4 L, and PP2A, indicating the formation of a multiprotein complex with CD63, thereby potentially regulating LMP1-dependent mTOR signaling. Collectively, the comprehensive analysis of CD63 proximal interacting proteins provides insights into the network of partners required for endocytic trafficking and extracellular vesicle cargo sorting, formation, and secretion.
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Kropff, Barbara, Yvonne Koedel, William Britt, and Michael Mach. "Optimal Replication of Human Cytomegalovirus Correlates with Endocytosis of Glycoprotein gpUL132." Journal of Virology 84, no. 14 (May 5, 2010): 7039–52. http://dx.doi.org/10.1128/jvi.01644-09.

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ABSTRACT Envelopment of a herpesvirus particle is a complex process of which much is still to be learned. We previously identified the glycoprotein gpUL132 of human cytomegalovirus (HCMV) as an envelope component of the virion. In its carboxy-terminal portion, gpUL132 contains at least four motifs for sorting of transmembrane proteins to endosomes; among them are one dileucine-based signal and three tyrosine-based signals of the YXXØ and NPXY (where X stands for any amino acid, and Ø stands for any bulky hydrophobic amino acid) types. To investigate the role of each of these trafficking signals in intracellular localization and viral replication, we constructed a panel of expression plasmids and recombinant viruses in which the signals were rendered nonfunctional by mutagenesis. In transfected cells wild-type gpUL132 was mainly associated with the trans-Golgi network. Consecutive mutation of the trafficking signals resulted in increasing fractions of the protein localized at the cell surface, with gpUL132 mutated in all four trafficking motifs predominantly associated with the plasma membrane. Concomitant with increased surface expression, endocytosis of mutant gpUL132 was reduced, with a gpUL132 expressing all four motifs in mutated form being almost completely impaired in endocytosis. The replication of recombinant viruses harboring mutations in single trafficking motifs was comparable to replication of wild-type virus. In contrast, viruses containing mutations in three or four of the trafficking signals showed pronounced deficits in replication with a reduction of approximately 100-fold. Moreover, recombinant viruses expressing gpUL132 with three or four trafficking motifs mutated failed to incorporate the mutant protein into the virus particle. These results demonstrate a role of endocytosis of an HCMV envelope glycoprotein for incorporation into the virion and optimal virus replication.
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Han, Q., C. Chang, L. Li, C. Klenk, J. Cheng, Y. Chen, N. Xia, et al. "Sumoylation of Influenza A Virus Nucleoprotein Is Essential for Intracellular Trafficking and Virus Growth." Journal of Virology 88, no. 16 (June 11, 2014): 9379–90. http://dx.doi.org/10.1128/jvi.00509-14.

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Joo, Kye-Il, Yun Fang, Yarong Liu, Liang Xiao, Zhen Gu, April Tai, Chi-Lin Lee, Yi Tang, and Pin Wang. "Enhanced Real-Time Monitoring of Adeno-Associated Virus Trafficking by Virus–Quantum Dot Conjugates." ACS Nano 5, no. 5 (April 13, 2011): 3523–35. http://dx.doi.org/10.1021/nn102651p.

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Ren, Changchun, April F. White, and Selvarangan Ponnazhagan. "Notch1 Augments Intracellular Trafficking of Adeno-Associated Virus Type 2." Journal of Virology 81, no. 4 (December 6, 2006): 2069–73. http://dx.doi.org/10.1128/jvi.01811-06.

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ABSTRACT We report here the significance of the Notch1 receptor in intracellular trafficking of recombinant adeno-associated virus type 2 (rAAV2). RNA profiling of human prostate cancer cell lines with various degrees of AAV transduction indicated a correlation of the amount of Notch1 with rAAV transgene expression. A definitive role of Notch1 in enhancing AAV transduction was confirmed by developing clonal derivatives of DU145 cells overexpressing either full-length or intracellular Notch1. To discern stages of AAV2 transduction influenced by Notch1, competitive binding with soluble heparin and Notch1 antibody, intracellular trafficking using Cy3-labeled rAAV2, and blocking assays for proteasome and dynamin pathways were performed. Results indicated that in the absence or low-level expression of Notch1, only binding of virus was found on the cell surface and internalization was impaired. However, increased Notch1 expression in these cells allowed efficient perinuclear accumulation of labeled capsids. Nuclear transport of the vector was evident by transgene expression and real-time PCR analyses. Dynamin levels were not found to be different among these cell lines, but blocking dynamin function abrogated AAV2 transduction in DU145 clones overexpressing full-length Notch1 but not in clones overexpressing intracellular Notch1. These studies provide evidence for the role of activated Notch1 in intracellular trafficking of AAV2, which may have implications in the optimal use of AAV2 in human gene therapy.
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Krzyzaniak, Magdalena, Michael Mach, and William J. Britt. "The Cytoplasmic Tail of Glycoprotein M (gpUL100) Expresses Trafficking Signals Required for Human Cytomegalovirus Assembly and Replication." Journal of Virology 81, no. 19 (July 11, 2007): 10316–28. http://dx.doi.org/10.1128/jvi.00375-07.

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ABSTRACT The virion envelope of human cytomegalovirus (HCMV) is complex and consists of an incompletely defined number of glycoproteins. The gM/gN protein complex is the most abundant protein component of the envelope. Studies have indicated that deletion of the viral gene encoding either gM or gN is a lethal mutation. Analysis of the amino acid sequence of gM disclosed a C-terminal acidic cluster of amino acids and a tyrosine-containing trafficking motif, both of which are well-described trafficking/sorting signals in the cellular secretory pathway. To investigate the roles of these signals in the trafficking of the gM/gN complex during virus assembly, we made a series of gM (UL100 open reading frame) mutants in the AD169 strain of HCMV. Mutant viruses that lacked the entire C-terminal cytoplasmic tail of gM were not viable, suggesting that the cytoplasmic tail of gM is essential for virus replication. In addition, the gM mutant protein lacking the cytoplasmic domain exhibited decreased protein stability. Mutant viruses with a deletion of the acidic cluster or alanine substitutions in tyrosine-based motifs were viable but exhibited a replication-impaired phenotype suggestive of a defect in virion assembly. Analysis of these mutant gMs using static immunofluorescence and fluorescence recovery after photobleaching demonstrated delayed kinetics of intracellular localization of the gM/gN protein to the virus assembly compartment compared to the wild-type protein. These data suggest an important role of the glycoprotein gM during virus assembly, particularly in the dynamics of gM trafficking during viral-particle assembly.
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Heidegger, Simon, David Anz, Nicolas Stephan, Bernadette Bohn, Tina Herbst, Wolfgang Peter Fendler, Nina Suhartha, et al. "Virus-associated activation of innate immunity induces rapid disruption of Peyer’s patches in mice." Blood 122, no. 15 (October 10, 2013): 2591–99. http://dx.doi.org/10.1182/blood-2013-01-479311.

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Key Points Systemic virus infection leads to rapid disruption of the Peyer’s patches but not of peripheral lymph nodes. Virus-associated innate immune activation and type I IFN release blocks trafficking of B cells to Peyer’s patches.
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39

Berka, Ursula, Martin Hamann, and Dirk Lindemann. "Early Events in Foamy Virus—Host Interaction and Intracellular Trafficking." Viruses 5, no. 4 (April 8, 2013): 1055–74. http://dx.doi.org/10.3390/v5041055.

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40

Fernandes, Fiona, Kang Chen, Lorna S. Ehrlich, Jing Jin, Min H. Chen, Gisselle N. Medina, Marc Symons, et al. "Phosphoinositides Direct Equine Infectious Anemia Virus Gag Trafficking and Release." Traffic 12, no. 4 (February 1, 2011): 438–51. http://dx.doi.org/10.1111/j.1600-0854.2010.01153.x.

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41

Portilho, Débora M., Roger Persson, and Nathalie Arhel. "Role of non-motile microtubule-associated proteins in virus trafficking." Biomolecular Concepts 7, no. 5-6 (December 1, 2016): 283–92. http://dx.doi.org/10.1515/bmc-2016-0018.

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AbstractViruses are entirely dependent on their ability to infect a host cell in order to replicate. To reach their site of replication as rapidly and efficiently as possible following cell entry, many have evolved elaborate mechanisms to hijack the cellular transport machinery to propel themselves across the cytoplasm. Long-range movements have been shown to involve motor proteins along microtubules (MTs) and direct interactions between viral proteins and dynein and/or kinesin motors have been well described. Although less well-characterized, it is also becoming increasingly clear that non-motile microtubule-associated proteins (MAPs), including structural MAPs of the MAP1 and MAP2 families, and microtubule plus-end tracking proteins (+TIPs), can also promote viral trafficking in infected cells, by mediating interaction of viruses with filaments and/or motor proteins, and modulating filament stability. Here we review our current knowledge on non-motile MAPs, their role in the regulation of cytoskeletal dynamics and in viral trafficking during the early steps of infection.
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42

Lagache, Thibault, and David Holcman. "Effective Motion of a Virus Trafficking Inside a Biological Cell." SIAM Journal on Applied Mathematics 68, no. 4 (January 2008): 1146–67. http://dx.doi.org/10.1137/060672820.

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43

Chambers, Raychel, and Toru Takimoto. "Trafficking of Sendai Virus Nucleocapsids Is Mediated by Intracellular Vesicles." PLoS ONE 5, no. 6 (June 7, 2010): e10994. http://dx.doi.org/10.1371/journal.pone.0010994.

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44

Paßvogel, Lars, Barbara G. Klupp, Harald Granzow, Walter Fuchs, and Thomas C. Mettenleiter. "Functional Characterization of Nuclear Trafficking Signals in Pseudorabies Virus pUL31." Journal of Virology 89, no. 4 (December 10, 2014): 2002–12. http://dx.doi.org/10.1128/jvi.03143-14.

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ABSTRACTThe herpesviral nuclear egress complex (NEC), consisting of pUL31 and pUL34 homologs, mediates efficient translocation of newly synthesized capsids from the nucleus to the cytosol. The tail-anchored membrane protein pUL34 is autonomously targeted to the nuclear envelope, while pUL31 is recruited to the inner nuclear membrane (INM) by interaction with pUL34. A nuclear localization signal (NLS) in several pUL31 homologs suggests importin-mediated translocation of the protein. Here we demonstrate that deletion or mutation of the NLS in pseudorabies virus (PrV) pUL31 resulted in exclusively cytosolic localization, indicating active nuclear export. Deletion or mutation of a predicted nuclear export signal (NES) in mutant constructs lacking a functional NLS resulted in diffuse nuclear and cytosolic localization, indicating that both signals are functional. pUL31 molecules lacking the complete NLS or NES were not recruited to the INM by pUL34, while site-specifically mutated proteins formed the NEC and partially complemented the defect of the UL31 deletion mutant. Our data demonstrate that the N terminus of pUL31, encompassing the NLS, is required for efficient nuclear targeting but not for pUL34 interaction, while the C terminus, containing the NES but not necessarily the NES itself, is required for complex formation and efficient budding of viral capsids at the INM. Moreover, pUL31-ΔNLS displayed a dominant negative effect on wild-type PrV replication, probably by diverting pUL34 to cytoplasmic membranes.IMPORTANCEThe molecular details of nuclear egress of herpesvirus capsids are still enigmatic. Although the key players, homologs of herpes simplex virus pUL34 and pUL31, which interact and form the heterodimeric nuclear egress complex, are well known, the molecular basis of this interaction and the successive budding, vesicle formation, and scission from the INM, as well as capsid release into the cytoplasm, remain largely obscure. Here we show that classical cellular targeting signals for nuclear import and export are important for proper localization and function of the NEC, thus regulating herpesvirus nuclear egress.
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Teofili, Luciana, Maria G. Iachininoto, Sara Capodimonti, Claudio Ucciferri, Eugenia R. Nuzzolo, Maurizio Martini, Lorenza Torti, et al. "Endothelial progenitor cell trafficking in human immunodeficiency virus-infected persons." AIDS 24, no. 16 (October 2010): 2443–50. http://dx.doi.org/10.1097/qad.0b013e32833ef79d.

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46

Lee, Grace E., John W. Murray, Allan W. Wolkoff, and Duncan W. Wilson. "Reconstitution of Herpes Simplex Virus Microtubule-Dependent Trafficking In Vitro." Journal of Virology 80, no. 9 (May 1, 2006): 4264–75. http://dx.doi.org/10.1128/jvi.80.9.4264-4275.2006.

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ABSTRACT Microtubule-mediated anterograde transport of herpes simplex virus (HSV) from the neuronal cell body to the axon terminal is crucial for the spread and transmission of the virus. It is therefore of central importance to identify the cellular and viral factors responsible for this trafficking event. In previous studies, we isolated HSV-containing cytoplasmic organelles from infected cells and showed that they represent the first and only destination for HSV capsids after they emerge from the nucleus. In the present study, we tested whether these cytoplasmic compartments were capable of microtubule-dependent traffic. Organelles containing green fluorescent protein-labeled HSV capsids were isolated and found to be able to bind rhodamine-labeled microtubules polymerized in vitro. Following the addition of ATP, the HSV-associated organelles trafficked along the microtubules, as visualized by time lapse microscopy in an imaging microchamber. The velocity and processivity of trafficking resembled those seen for neurotropic herpesvirus traffic in living axons. The use of motor-specific inhibitors indicated that traffic was predominantly kinesin mediated, consistent with the reconstitution of anterograde traffic. Immunocytochemical studies revealed that the majority of HSV-containing organelles attached to the microtubules contained the trans-Golgi network marker TGN46. This simple, minimal reconstitution of microtubule-mediated anterograde traffic should facilitate and complement molecular analysis of HSV egress in vivo.
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47

Acosta, Eliana G., Viviana Castilla, and Elsa B. Damonte. "Differential Requirements in Endocytic Trafficking for Penetration of Dengue Virus." PLoS ONE 7, no. 9 (September 7, 2012): e44835. http://dx.doi.org/10.1371/journal.pone.0044835.

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48

Patient, Romuald, Christophe Hourioux, Pierre-Yves Sizaret, Sylvie Trassard, Camille Sureau, and Philippe Roingeard. "Hepatitis B Virus Subviral Envelope Particle Morphogenesis and Intracellular Trafficking." Journal of Virology 81, no. 8 (January 31, 2007): 3842–51. http://dx.doi.org/10.1128/jvi.02741-06.

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ABSTRACT Hepatitis B virus (HBV) is unusual in that its surface proteins (small [S], medium, and large [L]) are not only incorporated into the virion envelope but they also bud into empty subviral particles in great excess over virions. The morphogenesis of these subviral envelope particles remains unclear, but the S protein is essential and sufficient for budding. We show here that, in contrast to the presumed model, the HBV subviral particle formed by the S protein self-assembles into branched filaments in the lumen of the endoplasmic reticulum (ER). These long filaments are then folded and bridged for packing into crystal-like structures, which are then transported by ER-derived vesicles to the ER-Golgi intermediate compartment (ERGIC). Within the ERGIC, they are unpacked and relaxed, and their size and shape probably limits further progression through the secretory pathway. Such progression requires their conversion into spherical particles, which occurred spontaneously during the purification of these filaments by affinity chromatography. Small branched filaments are also formed by the L protein in the ER lumen, but these filaments are not packed into transport vesicles. They are transported less efficiently to the ERGIC, potentially accounting for the retention of the L protein within cells. These findings shed light on an important step in the HBV infectious cycle, as the intracellular accumulation of HBV subviral filaments may be directly linked to viral pathogenesis.
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Wang, Zhi-Gang, Shu-Lin Liu, and Dai-Wen Pang. "Quantum Dots: A Promising Fluorescent Label for Probing Virus Trafficking." Accounts of Chemical Research 54, no. 14 (June 28, 2021): 2991–3002. http://dx.doi.org/10.1021/acs.accounts.1c00276.

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50

Harrison, Angela R., Cassandra T. David, Stephen M. Rawlinson, and Gregory W. Moseley. "The Ebola Virus Interferon Antagonist VP24 Undergoes Active Nucleocytoplasmic Trafficking." Viruses 13, no. 8 (August 19, 2021): 1650. http://dx.doi.org/10.3390/v13081650.

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Viral interferon (IFN) antagonist proteins mediate evasion of IFN-mediated innate immunity and are often multifunctional, with distinct roles in viral replication. The Ebola virus IFN antagonist VP24 mediates nucleocapsid assembly, and inhibits IFN-activated signaling by preventing nuclear import of STAT1 via competitive binding to nuclear import receptors (karyopherins). Proteins of many viruses, including viruses with cytoplasmic replication cycles, interact with nuclear trafficking machinery to undergo nucleocytoplasmic transport, with key roles in pathogenesis; however, despite established karyopherin interaction, potential nuclear trafficking of VP24 has not been investigated. We find that inhibition of nuclear export pathways or overexpression of VP24-binding karyopherin results in nuclear localization of VP24. Molecular mapping indicates that cytoplasmic localization of VP24 depends on a CRM1-dependent nuclear export sequence at the VP24 C-terminus. Nuclear export is not required for STAT1 antagonism, consistent with competitive karyopherin binding being the principal antagonistic mechanism, while export mediates return of nuclear VP24 to the cytoplasm where replication/nucleocapsid assembly occurs.
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