Submit
Search
Submit
Menu

  • Information

  • References

  • Contents

  • [1]M. Tsuchiya, S. R. Price, S. C. Tsai, J. Moss and M. Vaughan: Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. J Biol Chem 266(5), 2772-7 (1991)

  • [2]P. J. Peters, V. W. Hsu, C. E. Ooi, D. Finazzi, S. B. Teal, V. Oorschot, J. G. Donaldson and R. D. Klausner: Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J Cell Biol 128(6), 1003-17 (1995)

  • [3]W. E. Balch, R. A. Kahn and R. Schwaninger: ADP-ribosylation factor is required for vesicular trafficking between the endoplasmic reticulum and the cis-Golgi compartment. J Biol Chem 267(18), 13053-61 (1992)

  • [4]T. C. Taylor, R. A. Kahn and P. Melançon: Two distinct members of the ADP-ribosylation factor family of GTP-binding proteins regulate cell-free intra-Golgi transport. Cell 70(1), 69-79 (1992)

  • [5]P. Chardin, S. Paris, B. Antonny, S. Robineau, S. Béraud-Dufour, C. L. Jackson and M. Chabre: A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 384(6608), 481-4 (1996)

  • [6]A. Claude, B. P. Zhao, C. E. Kuziemsky, S. Dahan, S. J. Berger, J. P. Yan, A. D. Armold, E. M. Sullivan and P. Melançon: GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J Cell Biol 146(1), 71-84 (1999)

  • [7]A. Togawa, N. Morinaga, M. Ogasawara, J. Moss and M. Vaughan: Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. J Biol Chem 274(18), 12308-15 (1999)

  • [8]H. D. Jones, J. Moss and M. Vaughan: BIG1 and BIG2, brefeldin A-inhibited guanine nucleotide-exchange factors for ADP-ribosylation factors. Methods Enzymol 404, 174-84 (2005)

  • [9]S. Cockcroft, G. M. Thomas, A. Fensome, B. Geny, E. Cunningham, I. Gout, I. Hiles, N. F. Totty, O. Truong and J. J. Hsuan: Phospholipase D: a downstream effector of ARF in granulocytes. Science 263(5146), 523-6 (1994)

  • [10]H. A. Brown, S. Gutowski, C. R. Moomaw, C. Slaughter and P. C. Sternweis: ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 75(6), 1137-44 (1993)

  • [11]A. Honda, M. Nogami, T. Yokozeki, M. Yamazaki, H. Nakamura, H. Watanabe, K. Kawamoto, K. Nakayama, A. J. Morris, M. A. Frohman and Y. Kanaho: Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Cell 99(5), 521-32 (1999)

  • [12]J. R. Doedens and K. Kirkegaard: Inhibition of cellular protein secretion by poliovirus proteins 2B and 3A. EMBO J 14(5), 894-907 (1995)

  • [13]S. B. Deitz, D. A. Dodd, S. Cooper, P. Parham and K. Kirkegaard: MHC I-dependent antigen presentation is inhibited by poliovirus protein 3A. Proc Natl Acad Sci U S A 97(25), 13790-5 (2000)

  • [14]D. A. Dodd, T. H. Giddings and K. Kirkegaard: Poliovirus 3A protein limits interleukin-6 (IL-6), IL-8, and beta interferon secretion during viral infection. J Virol 75(17), 8158-65 (2001)

  • [15]N. Neznanov, A. Kondratova, K. M. Chumakov, B. Angres, B. Zhumabayeva, V. I. Agol and A. V. Gudkov: Poliovirus protein 3A inhibits tumor necrosis factor (TNF)-induced apoptosis by eliminating the TNF receptor from the cell surface. J Virol 75(21), 10409-20 (2001)

  • [16]J. R. Doedens, T. H. Giddings and K. Kirkegaard: Inhibition of endoplasmic reticulum-to-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J Virol 71(12), 9054-64 (1997)

  • [17]E. Wessels, D. Duijsings, R. A. Notebaart, W. J. Melchers and F. J. van Kuppeveld: A proline-rich region in the coxsackievirus 3A protein is required for the protein to inhibit endoplasmic reticulum-to-golgi transport. J Virol 79(8), 5163-73 (2005)

  • [18]O. Beske, M. Reichelt, M. P. Taylor, K. Kirkegaard and R. Andino: Poliovirus infection blocks ERGIC-to-Golgi trafficking and induces microtubule-dependent disruption of the Golgi complex. J Cell Sci 120(Pt 18), 3207-18 (2007)

  • [19]E. Wessels, D. Duijsings, T. K. Niu, S. Neumann, V. M. Oorschot, F. de Lange, K. H. Lanke, J. Klumperman, A. Henke, C. L. Jackson, W. J. Melchers and F. J. van Kuppeveld: A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1. Dev Cell 11(2), 191-201 (2006)

  • [20]E. Wessels, D. Duijsings, K. H. Lanke, S. H. van Dooren, C. L. Jackson, W. J. Melchers and F. J. van Kuppeveld: Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment. J Virol 80(23), 11852-60 (2006)

  • [21]G. A. Belov, Q. Feng, K. Nikovics, C. L. Jackson and E. Ehrenfeld: A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog 4(11), e1000216 (2008)

  • [22]S. S. Choe, D. A. Dodd and K. Kirkegaard: Inhibition of cellular protein secretion by picornaviral 3A proteins. Virology 337(1), 18-29 (2005)

  • [23]J. Wang, J. Du and Q. Jin: Class I ADP-ribosylation factors are involved in enterovirus 71 replication. PLoS One 9(6), e99768 (2014)

  • [24]K. Moffat, G. Howell, C. Knox, G. J. Belsham, P. Monaghan, M. D. Ryan and T. Wileman: Effects of foot-and-mouth disease virus nonstructural proteins on the structure and function of the early secretory pathway: 2BC but not 3A blocks endoplasmic reticulum-to-Golgi transport. J Virol 79(7), 4382-95 (2005)

  • [25]K. Moffat, C. Knox, G. Howell, S. J. Clark, H. Yang, G. J. Belsham, M. Ryan and T. Wileman: Inhibition of the secretory pathway by foot-and-mouth disease virus 2BC protein is reproduced by coexpression of 2B with 2C, and the site of inhibition is determined by the subcellular location of 2C. J Virol 81(3), 1129-39 (2007)

  • [26]G. A. Belov, C. Habbersett, D. Franco and E. Ehrenfeld: Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication. J Virol 81(17), 9259-67 (2007)

  • [27]K. V. Konan, T. H. Giddings, M. Ikeda, K. Li, S. M. Lemon and K. Kirkegaard: Nonstructural protein precursor NS4A/B from hepatitis C virus alters function and ultrastructure of host secretory apparatus. J Virol 77(14), 7843-55 (2003)

  • [28]M. Matto, E. H. Sklan, N. David, N. Melamed-Book, J. E. Casanova, J. S. Glenn and B. Aroeti: Role for ADP ribosylation factor 1 in the regulation of hepatitis C virus replication. J Virol 85(2), 946-56 (2011)

  • [29]L. Goueslain, K. Alsaleh, P. Horellou, P. Roingeard, V. Descamps, G. Duverlie, Y. Ciczora, C. Wychowski, J. Dubuisson and Y. Rouillé: Identification of GBF1 as a cellular factor required for hepatitis C virus RNA replication. J Virol 84(2), 773-87 (2010)

  • [30]A. W. Tai, Y. Benita, L. F. Peng, S. S. Kim, N. Sakamoto, R. J. Xavier and R. T. Chung: A functional genomic screen identifies cellular cofactors of hepatitis C virus replication. Cell Host Microbe 5(3), 298-307 (2009)

  • [31]D. Egger, B. Wölk, R. Gosert, L. Bianchi, H. E. Blum, D. Moradpour and K. Bienz: Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J Virol 76(12), 5974-84 (2002)

  • [32]H. Li, X. Yang, G. Yang, Z. Hong, L. Zhou, P. Yin, Y. Xiao, L. Chen, R. T. Chung and L. Zhang: Hepatitis C virus NS5A hijacks ARFGAP1 to maintain a phosphatidylinositol 4-phosphate-enriched microenvironment. J Virol 88(11), 5956-66 (2014)

  • [33]C. Wang, C. L. Timmons, Q. Shao, B. L. Kinlock, T. M. Turner, A. Iwamoto, H. Zhang, H. Liu and B. Liu: GB virus type C E2 protein inhibits human immunodeficiency virus type 1 Gag assembly by downregulating human ADP-ribosylation factor 1. Oncotarget 6(41), 43293-309 (2015)

  • [34]N. Bhattarai and J. T. Stapleton: GB virus C: the good boy virus? Trends Microbiol 20(3), 124-30 (2012)

  • [35]M. M. Samsa, J. A. Mondotte, N. G. Iglesias, I. Assunção-Miranda, G. Barbosa-Lima, A. T. Da Poian, P. T. Bozza and A. V. Gamarnik: Dengue virus capsid protein usurps lipid droplets for viral particle formation. PLoS Pathog 5(10), e1000632 (2009)

  • [36]N. G. Iglesias, J. A. Mondotte, L. A. Byk, F. A. De Maio, M. M. Samsa, C. Alvarez and A. V. Gamarnik: Dengue Virus Uses a Non-Canonical Function of the Host GBF1-Arf-COPI System for Capsid Protein Accumulation on Lipid Droplets. Traffic 16(9), 962-77 (2015)

  • [37]K. G. Soni, G. A. Mardones, R. Sougrat, E. Smirnova, C. L. Jackson and J. S. Bonifacino: Coatomer-dependent protein delivery to lipid droplets. J Cell Sci 122(Pt 11), 1834-41 (2009)

  • [38]F. N. Katz and H. F. Lodish: Transmembrane biogenesis of the vesicular stomatitis virus glycoprotein. J Cell Biol 80(2), 416-26 (1979)

  • [39]D. Panda, A. Das, P. X. Dinh, S. Subramaniam, D. Nayak, N. J. Barrows, J. L. Pearson, J. Thompson, D. L. Kelly, I. Ladunga and A. K. Pattnaik: RNAi screening reveals requirement for host cell secretory pathway in infection by diverse families of negative-strand RNA viruses. Proc Natl Acad Sci U S A 108(47), 19036-41 (2011)

  • [40]J. F. Roeth, M. Williams, M. R. Kasper, T. M. Filzen and K. L. Collins: HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail. J Cell Biol 167(5), 903-13 (2004)

  • [41]Q. T. Shen, X. Ren, R. Zhang, I. H. Lee and J. H. Hurley: HIV-1 Nef hijacks clathrin coats by stabilizing AP-1:Arf1 polygons. Science 350(6259), aac5137 (2015)

  • [42]R. Chaudhuri, O. W. Lindwasser, W. J. Smith, J. H. Hurley and J. S. Bonifacino: Downregulation of CD4 by human immunodeficiency virus type 1 Nef is dependent on clathrin and involves direct interaction of Nef with the AP2 clathrin adaptor. J Virol 81(8), 3877-90 (2007)

  • [43]S. Yamayoshi, G. Neumann and Y. Kawaoka: Role of the GTPase Rab1b in ebolavirus particle formation. J Virol 84(9), 4816-20 (2010)

  • [44]E. Sun, J. He and X. Zhuang: Dissecting the role of COPI complexes in influenza virus infection. J Virol 87(5), 2673-85 (2013)

  • [45]S. Kliche, W. Nagel, E. Kremmer, C. Atzler, A. Ege, T. Knorr, U. Koszinowski, W. Kolanus and J. Haas: Signaling by human herpesvirus 8 kaposin A through direct membrane recruitment of cytohesin-1. Mol Cell 7(4), 833-43 (2001)

  • [46]S. Dales, H. J. Eggers, i. Tamm and G. E. Palade: electron microscopic study of the formation of poliovirus. Virology 26, 379-89 (1965)

  • [47]D. Stuart and J. Fogh: Micromorphology of Fl cells infected with polio and coxsackie viruses. Virology 13(2), 177-& (1961)

  • [48]M. W. Cho, N. Teterina, D. Egger, K. Bienz and E. Ehrenfeld: Membrane rearrangement and vesicle induction by recombinant poliovirus 2C and 2BC in human cells. Virology 202(1), 129-45 (1994)

  • [49]I. V. Sandoval and L. Carrasco: Poliovirus infection and expression of the poliovirus protein 2B provoke the disassembly of the Golgi complex, the organelle target for the antipoliovirus drug Ro-090179. J Virol 71(6), 4679-93 (1997)

  • [50]G. A. Belov, V. Nair, B. T. Hansen, F. H. Hoyt, E. R. Fischer and E. Ehrenfeld: Complex dynamic development of poliovirus membranous replication complexes. J Virol 86(1), 302-12 (2012)

  • [51]E. C. Freundt, L. Yu, C. S. Goldsmith, S. Welsh, A. Cheng, B. Yount, W. Liu, M. B. Frieman, U. J. Buchholz, G. R. Screaton, J. Lippincott-Schwartz, S. R. Zaki, X. N. Xu, R. S. Baric, K. Subbarao and M. J. Lenardo: The open reading frame 3a protein of severe acute respiratory syndrome-associated coronavirus promotes membrane rearrangement and cell death. J Virol 84(2), 1097-109 (2010)

  • [52]K. Knoops, M. Kikkert, S. H. Worm, J. C. Zevenhoven-Dobbe, Y. van der Meer, A. J. Koster, A. M. Mommaas and E. J. Snijder: SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol 6(9), e226 (2008)

  • [53]E. J. Snijder, Y. van der Meer, J. Zevenhoven-Dobbe, J. J. Onderwater, J. van der Meulen, H. K. Koerten and A. M. Mommaas: Ultrastructure and origin of membrane vesicles associated with the severe acute respiratory syndrome coronavirus replication complex. J Virol 80(12), 5927-40 (2006)

  • [54]M. H. Verheije, M. Raaben, M. Mari, E. G. Te Lintelo, F. Reggiori, F. J. van Kuppeveld, P. J. Rottier and C. A. de Haan: Mouse hepatitis coronavirus RNA replication depends on GBF1-mediated ARF1 activation. PLoS Pathog 4(6), e1000088 (2008)

  • [55]C. Barlowe, L. Orci, T. Yeung, M. Hosobuchi, S. Hamamoto, N. Salama, M. F. Rexach, M. Ravazzola, M. Amherdt and R. Schekman: COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 77(6), 895-907 (1994)

  • [56]K. Matsuoka, L. Orci, M. Amherdt, S. Y. Bednarek, S. Hamamoto, R. Schekman and T. Yeung: COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 93(2), 263-75 (1998)

  • [57]C. Barlowe and R. Schekman: SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365(6444), 347-9 (1993)

  • [58]X. Bi, R. A. Corpina and J. Goldberg: Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature 419(6904), 271-7 (2002)

  • [59]E. Miller, B. Antonny, S. Hamamoto and R. Schekman: Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 21(22), 6105-13 (2002)

  • [60]E. A. Miller, T. H. Beilharz, P. N. Malkus, M. C. Lee, S. Hamamoto, L. Orci and R. Schekman: Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114(4), 497-509 (2003)

  • [61]X. Bi, J. D. Mancias and J. Goldberg: Insights into COPII coat nucleation from the structure of Sec23.Sar1 complexed with the active fragment of Sec31. Dev Cell 13(5), 635-45 (2007)

  • [62]S. Fath, J. D. Mancias, X. Bi and J. Goldberg: Structure and organization of coat proteins in the COPII cage. Cell 129(7), 1325-36 (2007)

  • [63]N. Bhattacharya, J. O Donnell and S. M. Stagg: The structure of the Sec13/31 COPII cage bound to Sec23. J Mol Biol 420(4-5), 324-34 (2012)

  • [64]S. M. Stagg, C. Gürkan, D. M. Fowler, P. LaPointe, T. R. Foss, C. S. Potter, B. Carragher and W. E. Balch: Structure of the Sec13/31 COPII coat cage. Nature 439(7073), 234-8 (2006)

  • [65]A. Bielli, C. J. Haney, G. Gabreski, S. C. Watkins, S. I. Bannykh and M. Aridor: Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J Cell Biol 171(6), 919-24 (2005)

  • [66]B. Antonny, D. Madden, S. Hamamoto, L. Orci and R. Schekman: Dynamics of the COPII coat with GTP and stable analogues. Nat Cell Biol 3(6), 531-7 (2001)

  • [67]L. F. Kung, S. Pagant, E. Futai, J. G. D’Arcangelo, R. Buchanan, J. C. Dittmar, R. J. Reid, R. Rothstein, S. Hamamoto, E. L. Snapp, R. Schekman and E. A. Miller: Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat. EMBO J 31(4), 1014-27 (2012)

  • [68]R. C. Rust, L. Landmann, R. Gosert, B. L. Tang, W. Hong, H. P. Hauri, D. Egger and K. Bienz: Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J Virol 75(20), 9808-18 (2001)

  • [69]T. Yorimitsu and K. Sato: Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites. Mol Biol Cell 23(15), 2930-42 (2012)

  • [70]M. Trahey, H. S. Oh, C. E. Cameron and J. C. Hay: Poliovirus infection transiently increases COPII vesicle budding. J Virol 86(18), 9675-82 (2012)

  • [71]R. Midgley, K. Moffat, S. Berryman, P. Hawes, J. Simpson, D. Fullen, D. J. Stephens, A. Burman and T. Jackson: A role for endoplasmic reticulum exit sites in foot-and-mouth disease virus infection. J Gen Virol 94(Pt 12), 2636-46 (2013)

  • [72]T. M. Sharp, S. Guix, K. Katayama, S. E. Crawford and M. K. Estes: Inhibition of cellular protein secretion by norwalk virus nonstructural protein p22 requires a mimic of an endoplasmic reticulum export signal. PLoS One 5(10), e13130 (2010)

  • [73]T. M. Sharp, S. E. Crawford, N. J. Ajami, F. H. Neill, R. L. Atmar, K. Katayama, B. Utama and M. K. Estes: Secretory pathway antagonism by calicivirus homologues of Norwalk virus nonstructural protein p22 is restricted to noroviruses. Virol J 9, 181 (2012)

  • [74]M. Schwartz, J. Chen, M. Janda, M. Sullivan, J. den Boon and P. Ahlquist: A positive-strand RNA virus replication complex parallels form and function of retrovirus capsids. Mol Cell 9(3), 505-14 (2002)

  • [75]B. L. Gancarz, L. Hao, Q. He, M. A. Newton and P. Ahlquist: Systematic identification of novel, essential host genes affecting bromovirus RNA replication. PLoS One 6(8), e23988 (2011)

  • [76]D. B. Kushner, B. D. Lindenbach, V. Z. Grdzelishvili, A. O. Noueiry, S. M. Paul and P. Ahlquist: Systematic, genome-wide identification of host genes affecting replication of a positive-strand RNA virus. Proc Natl Acad Sci U S A 100(26), 15764-9 (2003)

  • [77]A. Diaz, J. Zhang, A. Ollwerther, X. Wang and P. Ahlquist: Host ESCRT proteins are required for bromovirus RNA replication compartment assembly and function. PLoS Pathog 11(3), e1004742 (2015)

  • [78]A. Diaz, X. Wang and P. Ahlquist: Membrane-shaping host reticulon proteins play crucial roles in viral RNA replication compartment formation and function. Proc Natl Acad Sci U S A 107(37), 16291-6 (2010)

  • [79]C. Suarez, G. Andres, A. Kolovou, S. Hoppe, M. L. Salas, P. Walther and J. Krijnse Locker: African swine fever virus assembles a single membrane derived from rupture of the endoplasmic reticulum. Cell Microbiol 17(11), 1683-98 (2015)

  • [80]J. M. Rodríguez, R. García-Escudero, M. L. Salas and G. Andrés: African swine fever virus structural protein p54 is essential for the recruitment of envelope precursors to assembly sites. J Virol 78(8), 4299-1313 (2004)

  • [81]M. Windsor, P. Hawes, P. Monaghan, E. Snapp, M. L. Salas, J. M. Rodríguez and T. Wileman: Mechanism of collapse of endoplasmic reticulum cisternae during African swine fever virus infection. Traffic 13(1), 30-42 (2012)

  • [82]C. L. Netherton, M. C. McCrossan, M. Denyer, S. Ponnambalam, J. Armstrong, H. H. Takamatsu and T. E. Wileman: African swine fever virus causes microtubule-dependent dispersal of the trans-golgi network and slows delivery of membrane protein to the plasma membrane. J Virol 80(22), 11385-92 (2006)

  • [83]M. McCrossan, M. Windsor, S. Ponnambalam, J. Armstrong and T. Wileman: The trans Golgi network is lost from cells infected with African swine fever virus. J Virol 75(23), 11755-65 (2001)

  • [84]D. Pérez-Núñez, E. García-Urdiales, M. Martínez-Bonet, M. L. Nogal, S. Barroso, Y. Revilla and R. Madrid: CD2v Interacts with Adaptor Protein AP-1 during African Swine Fever Infection. PLoS One 10(4), e0123714 (2015)

  • [85]J. M. Mackenzie, M. K. Jones and E. G. Westaway: Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells. J Virol 73(11), 9555-67 (1999)

  • [86]P. W. Chu and E. G. Westaway: Molecular and ultrastructural analysis of heavy membrane fractions associated with the replication of Kunjin virus RNA. Arch Virol 125(1-4), 177-91 (1992)

  • [87]E. G. Westaway, J. M. Mackenzie, M. T. Kenney, M. K. Jones and A. A. Khromykh: Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures. J Virol 71(9), 6650-61 (1997)

  • [88]J. M. Mackenzie and E. G. Westaway: Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J Virol 75(22), 10787-99 (2001)

  • [89]J. Roosendaal, E. G. Westaway, A. Khromykh and J. M. Mackenzie: Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80(9), 4623-32 (2006)

  • [90]P. H. Kaufusi, J. F. Kelley, R. Yanagihara and V. R. Nerurkar: Induction of endoplasmic reticulum-derived replication-competent membrane structures by West Nile virus non-structural protein 4B. PLoS One 9(1), e84040 (2014)

  • [91]S. Welsch, S. Miller, I. Romero-Brey, A. Merz, C. K. Bleck, P. Walther, S. D. Fuller, C. Antony, J. Krijnse-Locker and R. Bartenschlager: Composition and three-dimensional architecture of the dengue virus replication and assembly sites. Cell Host Microbe 5(4), 365-75 (2009)

  • [92]S. Miller, S. Kastner, J. Krijnse-Locker, S. Bühler and R. Bartenschlager: The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J Biol Chem 282(12), 8873-82 (2007)

  • [93]D. Magliano, J. A. Marshall, D. S. Bowden, N. Vardaxis, J. Meanger and J. Y. Lee: Rubella virus replication complexes are virus-modified lysosomes. Virology 240(1), 57-63 (1998)

  • [94]J. Fontana, W. P. Tzeng, G. Calderita, A. Fraile-Ramos, T. K. Frey and C. Risco: Novel replication complex architecture in rubella replicon-transfected cells. Cell Microbiol 9(4), 875-90 (2007)

  • [95]J. Fontana, C. López-Iglesias, W. P. Tzeng, T. K. Frey, J. J. Fernández and C. Risco: Three-dimensional structure of Rubella virus factories. Virology 405(2), 579-91 (2010)

  • [96]P. M. Grimley, I. K. Berezesky and R. M. Friedman: Cytoplasmic structures associated with an arbovirus infection: loci of viral ribonucleic acid synthesis. J Virol 2(11), 1326-38 (1968)

  • [97]A. Salonen, L. Vasiljeva, A. Merits, J. Magden, E. Jokitalo and L. Kääriäinen: Properly folded nonstructural polyprotein directs the semliki forest virus replication complex to the endosomal compartment. J Virol 77(3), 1691-702 (2003)

  • [98]P. Kujala, A. Ikäheimonen, N. Ehsani, H. Vihinen, P. Auvinen and L. Kääriäinen: Biogenesis of the Semliki Forest virus RNA replication complex. J Virol 75(8), 3873-84 (2001)

  • [99]E. I. Frolova, R. Gorchakov, L. Pereboeva, S. Atasheva and I. Frolov: Functional Sindbis virus replicative complexes are formed at the plasma membrane. J Virol 84(22), 11679-95 (2010)

  • [100]P. Spuul, G. Balistreri, L. Kääriäinen and T. Ahola: Phosphatidylinositol 3-kinase-, actin-, and microtubule-dependent transport of Semliki Forest Virus replication complexes from the plasma membrane to modified lysosomes. J Virol 84(15), 7543-57 (2010)

  • [101]L. R. Delgui, J. F. Rodríguez and M. I. Colombo: The endosomal pathway and the Golgi complex are involved in the infectious bursal disease virus life cycle. J Virol 87(16), 8993-9007 (2013)

  • [102]M. Galloux, S. Libersou, N. Morellet, S. Bouaziz, B. Da Costa, M. Ouldali, J. Lepault and B. Delmas: Infectious bursal disease virus, a non-enveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes. J Biol Chem 282(28), 20774-84 (2007)

  • [103]N. Tolonen, L. Doglio, S. Schleich and J. Krijnse Locker: Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei. Mol Biol Cell 12(7), 2031-46 (2001)

  • [104]S. Dales and E. H. Mosbach: Vaccinia as a model for membrane biogenesis. Virology 35(4), 564-83 (1968)

  • [105]P. S. Satheshkumar, A. Weisberg and B. Moss: Vaccinia virus H7 protein contributes to the formation of crescent membrane precursors of immature virions. J Virol 83(17), 8439-50 (2009)

  • [106]X. Meng, X. Wu, B. Yan, J. Deng and Y. Xiang: Analysis of the role of vaccinia virus H7 in virion membrane biogenesis with an H7-deletion mutant. J Virol 87(14), 8247-53 (2013)

  • [107]W. Resch, A. S. Weisberg and B. Moss: Vaccinia virus nonstructural protein encoded by the A11R gene is required for formation of the virion membrane. J Virol 79(11), 6598-609 (2005)

  • [108]X. Meng, A. Embry, L. Rose, B. Yan, C. Xu and Y. Xiang: Vaccinia virus A6 is essential for virion membrane biogenesis and localization of virion membrane proteins to sites of virion assembly. J Virol 86(10), 5603-13 (2012)

  • [109]L. Maruri-Avidal, A. S. Weisberg and B. Moss: Direct formation of vaccinia virus membranes from the endoplasmic reticulum in the absence of the newly characterized L2-interacting protein A30.5. J Virol 87(22), 12313-26 (2013)

  • [110]L. Maruri-Avidal, A. Domi, A. S. Weisberg and B. Moss: Participation of vaccinia virus l2 protein in the formation of crescent membranes and immature virions. J Virol 85(6), 2504-11 (2011)

  • [111]P. Chlanda, M. A. Carbajal, M. Cyrklaff, G. Griffiths and J. Krijnse-Locker: Membrane rupture generates single open membrane sheets during vaccinia virus assembly. Cell Host Microbe 6(1), 81-90 (2009)

  • [112]B. Sodeik, G. Griffiths, M. Ericsson, B. Moss and R. W. Doms: Assembly of vaccinia virus: effects of rifampin on the intracellular distribution of viral protein p65. J Virol 68(2), 1103-14 (1994)

  • [113]P. Traktman, K. Liu, J. DeMasi, R. Rollins, S. Jesty and B. Unger: Elucidating the essential role of the A14 phosphoprotein in vaccinia virus morphogenesis: construction and characterization of a tetracycline-inducible recombinant. J Virol 74(8), 3682-95 (2000)

  • [114]B. Unger, J. Mercer, K. A. Boyle and P. Traktman: Biogenesis of the vaccinia virus membrane: genetic and ultrastructural analysis of the contributions of the A14 and A17 proteins. J Virol 87(2), 1083-97 (2013)

  • [115]J. R. Rodríguez, C. Risco, J. L. Carrascosa, M. Esteban and D. Rodríguez: Vaccinia virus 15-kilodalton (A14L) protein is essential for assembly and attachment of viral crescents to virosomes. J Virol 72(2), 1287-96 (1998)

  • [116]D. Rodríguez, M. Esteban and J. R. Rodríguez: Vaccinia virus A17L gene product is essential for an early step in virion morphogenesis. J Virol 69(8), 4640-8 (1995)

  • [117]D. Rodríguez, C. Risco, J. R. Rodríguez, J. L. Carrascosa and M. Esteban: Inducible expression of the vaccinia virus A17L gene provides a synchronized system to monitor sorting of viral proteins during morphogenesis. J Virol 70(11), 7641-53 (1996)

  • [118]E. J. Wolffe, D. M. Moore, P. J. Peters and B. Moss: Vaccinia virus A17L open reading frame encodes an essential component of nascent viral membranes that is required to initiate morphogenesis. J Virol 70(5), 2797-808 (1996)

  • [119]H. Bisht, A. S. Weisberg, P. Szajner and B. Moss: Assembly and disassembly of the capsid-like external scaffold of immature virions during vaccinia virus morphogenesis. J Virol 83(18), 9140-50 (2009)

  • [120]T. Betakova, E. J. Wolffe and B. Moss: Regulation of vaccinia virus morphogenesis: phosphorylation of the A14L and A17L membrane proteins and C-terminal truncation of the A17L protein are dependent on the F10L kinase. J Virol 73(5), 3534-43 (1999)

  • [121]P. Traktman, A. Caligiuri, S. A. Jesty, K. Liu and U. Sankar: Temperature-sensitive mutants with lesions in the vaccinia virus F10 kinase undergo arrest at the earliest stage of virion morphogenesis. J Virol 69(10), 6581-7 (1995)

  • [122]B. Moss: Poxvirus membrane biogenesis. Virology 479-480, 619-26 (2015)

  • [123]B. Sodeik, R. W. Doms, M. Ericsson, G. Hiller, C. E. Machamer, W. van ’t Hof, G. van Meer, B. Moss and G. Griffiths: Assembly of vaccinia virus: role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks. J Cell Biol 121(3), 521-41 (1993)

  • [124]C. Risco, J. R. Rodríguez, C. López-Iglesias, J. L. Carrascosa, M. Esteban and D. Rodríguez: Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly. J Virol 76(4), 1839-55 (2002)

  • [125]M. Husain and B. Moss: Evidence against an essential role of COPII-mediated cargo transport to the endoplasmic reticulum-Golgi intermediate compartment in the formation of the primary membrane of vaccinia virus. J Virol 77(21), 11754-66 (2003)

  • [126]L. Maruri-Avidal, A. S. Weisberg, H. Bisht and B. Moss: Analysis of viral membranes formed in cells infected by a vaccinia virus L2-deletion mutant suggests their origin from the endoplasmic reticulum. J Virol 87(3), 1861-71 (2013)

  • [127]L. Maruri-Avidal, A. S. Weisberg and B. Moss: Vaccinia virus L2 protein associates with the endoplasmic reticulum near the growing edge of crescent precursors of immature virions and stabilizes a subset of viral membrane proteins. J Virol 85(23), 12431-41 (2011)

  • [128]K. J. Erlandson, H. Bisht, A. S. Weisberg, S. I. Hyun, B. T. Hansen, E. R. Fischer, J. E. Hinshaw and B. Moss: Poxviruses Encode a Reticulon-Like Protein that Promotes Membrane Curvature. Cell Rep (2016)

  • [129]C. M. Heath, M. Windsor and T. Wileman: Aggresomes resemble sites specialized for virus assembly. J Cell Biol 153(3), 449-55 (2001)

  • [130]J. A. Johnston, M. E. Illing and R. R. Kopito: Cytoplasmic dynein/dynactin mediates the assembly of aggresomes. Cell Motil Cytoskeleton 53(1), 26-38 (2002)

  • [131]J. A. Johnston, C. L. Ward and R. R. Kopito: Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143(7), 1883-98 (1998)

  • [132]S. Stefanovic, M. Windsor, K. I. Nagata, M. Inagaki and T. Wileman: Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II. J Virol 79(18), 11766-75 (2005)

  • [133]C. Haolong, N. Du, T. Hongchao, Y. Yang, Z. Wei, Z. Hua, Z. Wenliang, S. Lei and T. Po: Enterovirus 71 VP1 activates calmodulin-dependent protein kinase II and results in the rearrangement of vimentin in human astrocyte cells. PLoS One 8(9), e73900 (2013)

  • [134]S. Das, A. Vasanji and P. E. Pellett: Three-dimensional structure of the human cytomegalovirus cytoplasmic virion assembly complex includes a reoriented secretory apparatus. J Virol 81(21), 11861-9 (2007)

  • [135]S. Das and P. E. Pellett: Spatial relationships between markers for secretory and endosomal machinery in human cytomegalovirus-infected cells versus those in uninfected cells. J Virol 85(12), 5864-79 (2011)

  • [136]V. Sanchez, K. D. Greis, E. Sztul and W. J. Britt: Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: characterization of a potential site of virus assembly. J Virol 74(2), 975-86 (2000)

  • [137]N. J. Buchkovich, T. G. Maguire and J. C. Alwine: Role of the endoplasmic reticulum chaperone BiP, SUN domain proteins, and dynein in altering nuclear morphology during human cytomegalovirus infection. J Virol 84(14), 7005-17 (2010)

  • [138]S. Das, D. A. Ortiz, S. J. Gurczynski, F. Khan and P. E. Pellett: Identification of human cytomegalovirus genes important for biogenesis of the cytoplasmic virion assembly complex. J Virol 88(16), 9086-99 (2014)

  • [139]N. J. Buchkovich, T. G. Maguire, A. W. Paton, J. C. Paton and J. C. Alwine: The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment. J Virol 83(22), 11421-8 (2009)

  • [140]S. V. Indran, M. E. Ballestas and W. J. Britt: Bicaudal D1-dependent trafficking of human cytomegalovirus tegument protein pp150 in virus-infected cells. J Virol 84(7), 3162-77 (2010)

  • [141]M. A. Krzyzaniak, M. Mach and W. J. Britt: HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein FIP4. Traffic 10(10), 1439-57 (2009)

  • [142]L. M. Hook, F. Grey, R. Grabski, R. Tirabassi, T. Doyle, M. Hancock, I. Landais, S. Jeng, S. McWeeney, W. Britt and J. A. Nelson: Cytomegalovirus miRNAs target secretory pathway genes to facilitate formation of the virion assembly compartment and reduce cytokine secretion. Cell Host Microbe 15(3), 363-73 (2014)

  • [143]P. Lučin, H. Mahmutefendić, G. Blagojević Zagorac and M. Ilić Tomaš: Cytomegalovirus immune evasion by perturbation of endosomal trafficking. Cell Mol Immunol 12(2), 154-69 (2015)

  • [144]A. Halenius, C. Gerke and H. Hengel: Classical and non-classical MHC I molecule manipulation by human cytomegalovirus: so many targets—but how many arrows in the quiver? Cell Mol Immunol 12(2), 139-53 (2015)

  • [145]T. R. Jones, E. J. Wiertz, L. Sun, K. N. Fish, J. A. Nelson and H. L. Ploegh: Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains. Proc Natl Acad Sci U S A 93(21), 11327-33 (1996)

  • [146]K. Ahn, A. Angulo, P. Ghazal, P. A. Peterson, Y. Yang and K. Früh: Human cytomegalovirus inhibits antigen presentation by a sequential multistep process. Proc Natl Acad Sci U S A 93(20), 10990-5 (1996)

  • [147]W. Smith, P. Tomasec, R. Aicheler, A. Loewendorf, I. Nemčovičová, E. C. Wang, R. J. Stanton, M. Macauley, P. Norris, L. Willen, E. Ruckova, A. Nomoto, P. Schneider, G. Hahn, D. M. Zajonc, C. F. Ware, G. W. Wilkinson and C. A. Benedict: Human cytomegalovirus glycoprotein UL141 targets the TRAIL death receptors to thwart host innate antiviral defenses. Cell Host Microbe 13(3), 324-35 (2013)

  • [148]P. Tomasec, E. C. Wang, A. J. Davison, B. Vojtesek, M. Armstrong, C. Griffin, B. P. McSharry, R. J. Morris, S. Llewellyn-Lacey, C. Rickards, A. Nomoto, C. Sinzger and G. W. Wilkinson: Downregulation of natural killer cell-activating ligand CD155 by human cytomegalovirus UL141. Nat Immunol 6(2), 181-8 (2005)

  • [149]N. J. Bennett, O. Ashiru, F. J. Morgan, Y. Pang, G. Okecha, R. A. Eagle, J. Trowsdale, J. G. Sissons and M. R. Wills: Intracellular sequestration of the NKG2D ligand ULBP3 by human cytomegalovirus. J Immunol 185(2), 1093-102 (2010)

  • [150]O. Ashiru, N. J. Bennett, L. H. Boyle, M. Thomas, J. Trowsdale and M. R. Wills: NKG2D ligand MICA is retained in the cis-Golgi apparatus by human cytomegalovirus protein UL142. J Virol 83(23), 12345-54 (2009)

  • [151]J. Wu, N. J. Chalupny, T. J. Manley, S. R. Riddell, D. Cosman and T. Spies: Intracellular retention of the MHC class I-related chain B ligand of NKG2D by the human cytomegalovirus UL16 glycoprotein. J Immunol 170(8), 4196-200 (2003)

  • [152]M. H. Furman, N. Dey, D. Tortorella and H. L. Ploegh: The human cytomegalovirus US10 gene product delays trafficking of major histocompatibility complex class I molecules. J Virol 76(22), 11753-6 (2002)

  • [153]J. Trgovcich, C. Cebulla, P. Zimmerman and D. D. Sedmak: Human cytomegalovirus protein pp71 disrupts major histocompatibility complex class I cell surface expression. J Virol 80(2), 951-63 (2006)

  • [154]S. A. Welte, C. Sinzger, S. Z. Lutz, H. Singh-Jasuja, K. L. Sampaio, U. Eknigk, H. G. Rammensee and A. Steinle: Selective intracellular retention of virally induced NKG2D ligands by the human cytomegalovirus UL16 glycoprotein. Eur J Immunol 33(1), 194-203 (2003)

  • [155]C. A. Fielding, R. Aicheler, R. J. Stanton, E. C. Wang, S. Han, S. Seirafian, J. Davies, B. P. McSharry, M. P. Weekes, P. R. Antrobus, V. Prod’homme, F. P. Blanchet, D. Sugrue, S. Cuff, D. Roberts, A. J. Davison, P. J. Lehner, G. W. Wilkinson and P. Tomasec: Two novel human cytomegalovirus NK cell evasion functions target MICA for lysosomal degradation. PLoS Pathog 10(5), e1004058 (2014)

  • [156]T. R. Jones and L. Sun: Human cytomegalovirus US2 destabilizes major histocompatibility complex class I heavy chains. J Virol 71(4), 2970-9 (1997)

  • [157]B. E. Gewurz, E. W. Wang, D. Tortorella, D. J. Schust and H. L. Ploegh: Human cytomegalovirus US2 endoplasmic reticulum-lumenal domain dictates association with major histocompatibility complex class I in a locus-specific manner. J Virol 75(11), 5197-204 (2001 )

  • [158]K. Oresic and D. Tortorella: Endoplasmic reticulum chaperones participate in human cytomegalovirus US2-mediated degradation of class I major histocompatibility complex molecules. J Gen Virol 89(Pt 5), 1122-30 (2008)

  • [159]T. R. Jones, L. K. Hanson, L. Sun, J. S. Slater, R. M. Stenberg and A. E. Campbell: Multiple independent loci within the human cytomegalovirus unique short region down-regulate expression of major histocompatibility complex class I heavy chains. J Virol 69(8), 4830-41 (1995)

  • [160]C. E. Shamu, D. Flierman, H. L. Ploegh, T. A. Rapoport and V. Chau: Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 12(8), 2546-55 (2001)

  • [161]E. J. Wiertz, T. R. Jones, L. Sun, M. Bogyo, H. J. Geuze and H. L. Ploegh: The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84(5), 769-79 (1996)

  • [162]B. Park, E. Spooner, B. L. Houser, J. L. Strominger and H. L. Ploegh: The HCMV membrane glycoprotein US10 selectively targets HLA-G for degradation. J Exp Med 207(9), 2033-41 (2010)

  • [163]I. Jelcic, J. Reichel, C. Schlude, E. Treutler, C. Sinzger and A. Steinle: The polymorphic HCMV glycoprotein UL20 is targeted for lysosomal degradation by multiple cytoplasmic dileucine motifs. Traffic 12(10), 1444-56 (2011)

Article Metrics

  • Information

  • Download

  • Contents

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

1 Mar 2017Review
Rerouting the traffic from a virus perspective
Linda Cruz 1, Nicholas J. Buchkovich 1,*
Affiliation
Article Info

1 Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania, USA

Abstract

Viruses are important human and animal pathogens causing disease that affect global health and the economy. One outcome of many virus infections is the regulation of cellular trafficking machinery. Viral proteins recruit and interact with cellular trafficking proteins to divert the normal trafficking of key proteins or to induce the formation of novel membrane structures in the host cell. These alterations often increase replication efficiency by mislocalizing immune regulators or restriction factors ot by creating platforms for replication and assembly of new virus particles. Our knowledge of how viruses interact with the cellular trafficking machinery is still limited and furthering this understanding will be important for the future development of prophylactic and therapeutic treatments. This review provides a glimpse of the types of interplay between viral and cellular factors that result in a disruption of cellular trafficking or modifications to cellular membranes.

Keywords

  • Virus
  • Trafficking
  • Membrane
  • Arf1
  • Organelle Morphology
  • Transport
  • Assembly Compartments
  • Review

References