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We have used both the acidic domains from actin-related protein (Arp) 2\/3 complex-binding proteins such as the Wiscott-Aldrich syndrome protein (N-WASP) or cortactin, and siRNA directing toward Arp2 to inhibit viral infection. HIV-1, simian immunodeficiency virus (SIV), and intracellular mature vaccinia virus (IMV) were sensitive to inhibition of the Arp2\/3 complex, whereas MLV, HSV-1, and adenovirus were not. Interestingly, pseudotyping HIV-1 with vesicular stomatitis virus G protein (VSV-G) overcame this inhibition. Constitutive inhibition of the Arp2\/3 complex in the T-cell line H9 also blocked replication of HIV-1. These data suggested the existence of an Arp2\/3 complex-dependent event during the early phase of the life cycles of both primate lentiviruses and IMV. Inhibiting the HIV-1's ability to activate Arp2\/3 complex could be a potential chemotherapeutic intervention for acquired immunodeficiency syndrome (AIDS).<\/jats:p>","DOI":"10.1091\/mbc.e04-04-0279","type":"journal-article","created":{"date-parts":[[2004,9,23]],"date-time":"2004-09-23T00:25:06Z","timestamp":1095899106000},"page":"5197-5207","source":"Crossref","is-referenced-by-count":93,"title":["Inhibiting the Arp2\/3 Complex Limits Infection of Both Intracellular Mature Vaccinia Virus and Primate Lentiviruses"],"prefix":"10.1091","volume":"15","author":[{"given":"Jun","family":"Komano","sequence":"first","affiliation":[{"name":"Laboratory of Virology and Pathogenesis, AIDS Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kosuke","family":"Miyauchi","sequence":"additional","affiliation":[{"name":"Laboratory of Virology and Pathogenesis, AIDS Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zene","family":"Matsuda","sequence":"additional","affiliation":[{"name":"Laboratory of Virology and Pathogenesis, AIDS Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoki","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Laboratory of Virology and Pathogenesis, AIDS Research Center, National Institute of Infectious Diseases, Tokyo 208-0011, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1076","reference":[{"key":"REF1","doi-asserted-by":"crossref","unstructured":"Aoki, Y., Aizaki, H., Shimoike, T., Tani, H., Ishii, K., Saito, I., Matsuura, Y., and Miyamura, T. (1998). A human liver cell line exhibits efficient translation of HCV RNAs produced by a recombinant adenovirus expressing T7 RNA polymerase.Virology250, 140\u2013150.","DOI":"10.1006\/viro.1998.9361"},{"key":"REF2","doi-asserted-by":"crossref","unstructured":"Bukrinskaya, A., Brichacek, B., Mann, A., and Stevenson, M. (1998). Establishment of a functional human immunodeficiency virus type 1 (HIV-1) reverse transcription complex involves the cytoskeleton.J. Exp. Med.188, 2113\u20132125.","DOI":"10.1084\/jem.188.11.2113"},{"key":"REF3","doi-asserted-by":"crossref","unstructured":"Cantarelli, V.V., Takahashi, A., Akeda, Y., Nagayama, K., and Honda, T. (2000). Interaction of enteropathogenic or enterohemorrhagicEscherichia coliwith HeLa cells results in translocation of cortactin to the bacterial adherence site.Infect. Immun.68, 382\u2013386.","DOI":"10.1128\/IAI.68.1.382-386.2000"},{"key":"REF4","doi-asserted-by":"crossref","unstructured":"Castellano, F., Le Clainche, C., Patin, D., Carlier, M.F., and Chavrier, P. (2001). A WASp-VASP complex regulates actin polymerization at the plasma membrane.EMBO J.20, 5603\u20135614.","DOI":"10.1093\/emboj\/20.20.5603"},{"key":"REF5","doi-asserted-by":"crossref","unstructured":"Cudmore, S., Reckmann, I., and Way, M. (1997). Viral manipulations of the actin cytoskeleton.Trends Microbiol.5, 142\u2013148.","DOI":"10.1016\/S0966-842X(97)01011-1"},{"key":"REF6","doi-asserted-by":"crossref","unstructured":"Dean, H.J., Terhune, S.S., Shieh, M.T., Susmarski, N., and Spear, P.G. (1994). Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.Virology199, 67\u201380.","DOI":"10.1006\/viro.1994.1098"},{"key":"REF7","doi-asserted-by":"crossref","unstructured":"Dehio, C., Prevost, M.C., and Sansonetti, P.J. (1995). Invasion of epithelial cells byShigella flexneriinduces tyrosine phosphorylation of cortactin by a pp60csrc-mediated signalling pathway.EMBO J.14, 2471\u20132482.","DOI":"10.1002\/j.1460-2075.1995.tb07244.x"},{"key":"REF8","doi-asserted-by":"crossref","unstructured":"Fawaz, F.S., van Ooij, C., Homola, E., Mutka, S.C., and Engel, J.N. (1997). Infection withChlamydia trachomatisalters the tyrosine phosphorylation and\/or localization of several host cell proteins including cortactin.Infect. Immun.65, 5301\u20135308.","DOI":"10.1128\/IAI.65.12.5301-5308.1997"},{"key":"REF9","doi-asserted-by":"crossref","unstructured":"Flanagan, L.A., Chou, J., Falet, H., Neujahr, R., Hartwig, J.H., and Stossel, T.P. (2001). Filamin A, the Arp2\/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells.J. Cell Biol.155, 511\u2013517.","DOI":"10.1083\/jcb.200105148"},{"key":"REF10","doi-asserted-by":"crossref","unstructured":"Frischknecht, F., Moreau, V., Rottger, S., Gonfloni, S., Reckmann, I., SupertiFurga, G., and Way, M. (1999). Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling.Nature401, 926\u2013929.","DOI":"10.1038\/44860"},{"key":"REF11","doi-asserted-by":"crossref","unstructured":"Fuerst, T.R., Niles, E.G., Studier, F.W., and Moss, B. (1986). Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase.Proc. Natl. Acad. Sci. USA83, 8122\u20138126.","DOI":"10.1073\/pnas.83.21.8122"},{"key":"REF12","doi-asserted-by":"crossref","unstructured":"Fuller, A.O., and Spear, P.G. (1987). Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface.Proc. Natl. Acad. Sci. USA84, 5454\u20135458.","DOI":"10.1073\/pnas.84.15.5454"},{"key":"REF13","doi-asserted-by":"crossref","unstructured":"Gournier, H., Goley, E.D., Niederstrasser, H., Trinh, T., and Welch, M.D. (2001). Reconstitution of human Arp2\/3 complex reveals critical roles of individual subunits in complex structure and activity.Mol. Cell8, 1041\u20131052.","DOI":"10.1016\/S1097-2765(01)00393-8"},{"key":"REF14","doi-asserted-by":"crossref","unstructured":"Gruenheid, S., and Finlay, B.B. (2003). Microbial pathogenesis and cytoskeletal function.Nature422, 775\u2013781.","DOI":"10.1038\/nature01603"},{"key":"REF15","doi-asserted-by":"crossref","unstructured":"Gundlach, B.R.et al.(1997). Construction, replication, and immunogenic properties of a simian immunodeficiency virus expressing interleukin-2.J. Virol.71, 2225\u20132232.","DOI":"10.1128\/JVI.71.3.2225-2232.1997"},{"key":"REF16","doi-asserted-by":"crossref","unstructured":"Harlander, R.S., Way, M., Ren, Q., Howe, D., Grieshaber, S.S., and Heinzen, R.A. (2003). Effects of ectopically expressed neuronal Wiskott-Aldrich syndrome protein domains onRickettsia rickettsiiactin-based motility.Infect. Immun.71, 1551\u20131556.","DOI":"10.1128\/IAI.71.3.1551-1556.2003"},{"key":"REF17","doi-asserted-by":"crossref","unstructured":"Higgs, H.N., Blanchoin, L., and Pollard, T.D. (1999). Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2\/3 complex on actin polymerization.Biochemistry38, 15212\u201315222.","DOI":"10.1021\/bi991843+"},{"key":"REF18","doi-asserted-by":"crossref","unstructured":"Higgs, H.N., and Pollard, T.D. (2001). Regulation of actin filament network formation through ARP2\/3 complex: activation by a diverse array of proteins.Annu. Rev. Biochem.70, 649\u2013676.","DOI":"10.1146\/annurev.biochem.70.1.649"},{"key":"REF19","doi-asserted-by":"crossref","unstructured":"Ichihashi, Y., and Oie, M. (1996). Neutralizing epitope on penetration protein of vaccinia virus.Virology220, 491\u2013494.","DOI":"10.1006\/viro.1996.0337"},{"key":"REF20","doi-asserted-by":"crossref","unstructured":"Iyengar, S., Hildreth, J.E., and Schwartz, D.H. (1998). Actin-dependent receptor colocalization required for human immunodeficiency virus entry into host cells.J. Virol.72, 5251\u20135255.","DOI":"10.1128\/JVI.72.6.5251-5255.1998"},{"key":"REF21","doi-asserted-by":"crossref","unstructured":"Kizhatil, K., and Albritton, L.M. (1997). Requirements for different components of the host cell cytoskeleton distinguish ecotropic murine leukemia virus entry via endocytosis from entry via surface fusion.J. Virol.71, 7145\u20137156.","DOI":"10.1128\/JVI.71.10.7145-7156.1997"},{"key":"REF22","doi-asserted-by":"crossref","unstructured":"Krause, M., Sechi, A.S., Konradt, M., Monner, D., Gertler, F.B., and Wehland, J. (2000). Fyn-binding protein (Fyb)\/SLP-76-associated protein (SLAP), Ena\/vasodilator-stimulated phosphoprotein (VASP) proteins and the Arp2\/3 complex link T cell receptor (TCR) signaling to the actin cytoskeleton.J. Cell Biol.149, 181\u2013194.","DOI":"10.1083\/jcb.149.1.181"},{"key":"REF23","doi-asserted-by":"crossref","unstructured":"Li, E., Stupack, D., Bokoch, G.M., and Nemerow, G.R. (1998). Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases.J. Virol.72, 8806\u20138812.","DOI":"10.1128\/JVI.72.11.8806-8812.1998"},{"key":"REF24","doi-asserted-by":"publisher","DOI":"10.1091\/mbc.11.7.2497"},{"key":"REF25","doi-asserted-by":"crossref","unstructured":"Machesky, L.M., and Insall, R.H. (1998). Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2\/3 complex.Curr. Biol.8, 1347\u20131356.","DOI":"10.1016\/S0960-9822(98)00015-3"},{"key":"REF26","doi-asserted-by":"crossref","unstructured":"Machesky, L.M., Mullins, R.D., Higgs, H.N., Kaiser, D.A., Blanchoin, L., May, R.C., Hall, M.E., and Pollard, T.D. (1999). Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2\/3 complex.Proc. Natl. Acad. Sci. 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(1990). The pH independence of mammalian retrovirus infection.J. Gen. Virol.71, 767\u2013773.","DOI":"10.1099\/0022-1317-71-4-767"},{"key":"REF31","doi-asserted-by":"crossref","unstructured":"McDonald, D., Vodicka, M.A., Lucero, G., Svitkina, T.M., Borisy, G.G., Emerman, M., and Hope, T.J. (2002). Visualization of the intracellular behavior of HIV in living cells.J. Cell Biol.159, 441\u2013452.","DOI":"10.1083\/jcb.200203150"},{"key":"REF32","doi-asserted-by":"crossref","unstructured":"McGee, K., Zettl, M., Way, M., and Fallman, M. (2001). A role for N-WASP in invasin-promoted internalisation.FEBS Lett.509, 59\u201365.","DOI":"10.1016\/S0014-5793(01)03139-8"},{"key":"REF33","doi-asserted-by":"crossref","unstructured":"Miki, H., Miura, K., and Takenawa, T. (1996). N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases.EMBO J.15, 5326\u20135335.","DOI":"10.1002\/j.1460-2075.1996.tb00917.x"},{"key":"REF34","doi-asserted-by":"crossref","unstructured":"Miki, H., and Takenawa, T. (1998). Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization.Biochem. Biophys. Res. Commun.243, 73\u201378.","DOI":"10.1006\/bbrc.1997.8064"},{"key":"REF35","doi-asserted-by":"crossref","unstructured":"Moreau, V., Frischknecht, F., Reckmann, I., Vincentelli, R., Rabut, G., Stewart, D., and Way, M. (2000). A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization.Nat. Cell Biol.2, 441\u2013448.","DOI":"10.1038\/35017080"},{"key":"REF36","doi-asserted-by":"crossref","unstructured":"Nussbaum, O., Broder, C.C., and Berger, E.A. (1994). Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation.J. Virol.68, 5411\u20135422.","DOI":"10.1128\/JVI.68.9.5411-5422.1994"},{"key":"REF37","doi-asserted-by":"crossref","unstructured":"Nussbaum, O., Roop, A., and Anderson, W.F. (1993). Sequences determining the pH dependence of viral entry are distinct from the host range-determining region of the murine ecotropic and amphotropic retrovirus envelope proteins.J. Virol.67, 7402\u20137405.","DOI":"10.1128\/JVI.67.12.7402-7405.1993"},{"key":"REF38","doi-asserted-by":"crossref","unstructured":"Panchal, S.C., Kaiser, D.A., Torres, E., Pollard, T.D., and Rosen, M.K. (2003). A conserved amphipathic helix in WASP\/Scar proteins is essential for activation of Arp2\/3 complex.Nat. Struct. Biol.10, 591\u2013598.","DOI":"10.1038\/nsb952"},{"key":"REF39","doi-asserted-by":"crossref","unstructured":"Pantaloni, D., Le Clainche, C., and Carlier, M.F. (2001). Mechanism of actinbased motility.Science292, 1502\u20131506.","DOI":"10.1126\/science.1059975"},{"key":"REF40","doi-asserted-by":"crossref","unstructured":"Ragheb, J.A., and Anderson, W.F. (1994). pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry.J. Virol.68, 3220\u20133231.","DOI":"10.1128\/JVI.68.5.3220-3231.1994"},{"key":"REF41","doi-asserted-by":"crossref","unstructured":"Rietdorf, J., Ploubidou, A., Reckmann, I., Holmstrom, A., Frischknecht, F., Zettl, M., Zimmermann, T., and Way, M. (2001). Kinesin-dependent movement on microtubules precedes actin-based motility of vaccinia virus.Nat. Cell Biol.3, 992\u20131000.","DOI":"10.1038\/ncb1101-992"},{"key":"REF42","doi-asserted-by":"crossref","unstructured":"Robinson, R.C., Turbedsky, K., Kaiser, D.A., Marchand, J.B., Higgs, H.N., Choe, S., and Pollard, T.D. (2001). Crystal structure of Arp2\/3 complex.Science294, 1679\u20131684.","DOI":"10.1126\/science.1066333"},{"key":"REF43","doi-asserted-by":"crossref","unstructured":"Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T., and Kirschner, M.W. (1999). The interaction between N-WASP and the Arp2\/3 complex links Cdc42-dependent signals to actin assembly.Cell97, 221\u2013231.","DOI":"10.1016\/S0092-8674(00)80732-1"},{"key":"REF44","doi-asserted-by":"crossref","unstructured":"Rosenthal, K.S., Perez, R., and Hodnichak, C. (1985). Inhibition of herpes simplex virus type 1 penetration by cytochalasins B and D.J. Gen. Virol.66, 1601\u20131605.","DOI":"10.1099\/0022-1317-66-7-1601"},{"key":"REF45","doi-asserted-by":"crossref","unstructured":"Rozelle, A.L.et al.(2000). Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft-enriched vesicles through WASP-Arp2\/3.Curr. Biol.10, 311\u2013320.","DOI":"10.1016\/S0960-9822(00)00384-5"},{"key":"REF46","doi-asserted-by":"crossref","unstructured":"Sakamoto, T., Ushijima, H., Okitsu, S., Suzuki, E., Sakai, K., Morikawa, S., and Muller, W.E. (2003). Establishment of an HIV cell-cell fusion assay by using two genetically modified HeLa cell lines and reporter gene.J. Virol. Methods114, 159\u2013166.","DOI":"10.1016\/j.jviromet.2003.08.016"},{"key":"REF47","doi-asserted-by":"crossref","unstructured":"Sakisaka, T.et al.(2001). Requirement of interaction of nectin-1alpha\/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1.J. Virol.75, 4734\u20134743.","DOI":"10.1128\/JVI.75.10.4734-4743.2001"},{"key":"REF48","doi-asserted-by":"crossref","unstructured":"Scaplehorn, N., Holmstrom, A., Moreau, V., Frischknecht, F., Reckmann, I., and Way, M. (2002). Grb2 and Nck act cooperatively to promote actin-based motility of vaccinia virus.Curr. Biol.12, 740\u2013745.","DOI":"10.1016\/S0960-9822(02)00812-6"},{"key":"REF49","doi-asserted-by":"crossref","unstructured":"Smith, G.L., Vanderplasschen, A., and Law, M. (2002). The formation and function of extracellular enveloped vaccina virus.J. Gen. Virol.83,2915\u20132931.","DOI":"10.1099\/0022-1317-83-12-2915"},{"key":"REF50","doi-asserted-by":"crossref","unstructured":"Stein, B.S., Gowda, S.D., Lifson, J.D., Penhallow, R.C., Bensch, K.G., and Engleman, E.G. (1987). pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane.Cell49, 659\u2013668.","DOI":"10.1016\/0092-8674(87)90542-3"},{"key":"REF51","doi-asserted-by":"crossref","unstructured":"Takase-Yoden, S., and Watanabe, R. (1999). Contribution of virus-receptor interaction to distinct viral proliferation of neuropathogenic and nonneuropathogenic murine leukemia viruses in rat glial cells.J. Virol.73, 4461\u20134464.","DOI":"10.1128\/JVI.73.5.4461-4464.1999"},{"key":"REF52","doi-asserted-by":"crossref","unstructured":"Takenawa, T., and Miki, H. (2001). WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement.J. Cell Sci.114, 1801\u20131809.","DOI":"10.1242\/jcs.114.10.1801"},{"key":"REF53","doi-asserted-by":"crossref","unstructured":"Uruno, T., Liu, J., Zhang, P., Fan, Y., Egile, C., Li, R., Mueller, S.C., and Zhan, X. (2001). Activation of Arp2\/3 complex-mediated actin polymerization by cortactin.Nat. Cell Biol.3, 259\u2013266.","DOI":"10.1038\/35060051"},{"key":"REF54","doi-asserted-by":"crossref","unstructured":"Vanderplasschen, A., Hollinshead, M., and Smith, G.L. (1998). Intracellular and extracellular vaccinia virions enter cells by different mechanisms.J. Gen. Virol.79, 877\u2013887.","DOI":"10.1099\/0022-1317-79-4-877"},{"key":"REF55","doi-asserted-by":"crossref","unstructured":"Wang, K., Huang, S., Kapoor-Munshi, A., and Nemerow, G. (1998). Adenovirus internalization and infection require dynamin.J. Virol.72, 3455\u20133458.","DOI":"10.1128\/JVI.72.4.3455-3458.1998"},{"key":"REF56","doi-asserted-by":"crossref","unstructured":"Weaver, A.M., Karginov, A.V., Kinley, A.W., Weed, S.A., Li, Y., Parsons, J.T., and Cooper, J.A. (2001). Cortactin promotes and stabilizes Arp2\/3-induced actin filament network formation.Curr. 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Cortactin: coupling membrane dynamics to cortical actin assembly.Oncogene20, 6418\u20136434.","DOI":"10.1038\/sj.onc.1204783"},{"key":"REF60","doi-asserted-by":"crossref","unstructured":"Welch, M.D., Rosenblatt, J., Skoble, J., Portnoy, D.A., and Mitchison, T.J. (1998). Interaction of human Arp2\/3 complex and theListeria monocytogenesActA protein in actin filament nucleation.Science281, 105\u2013108.","DOI":"10.1126\/science.281.5373.105"},{"key":"REF61","doi-asserted-by":"crossref","unstructured":"Wittels, M., and Spear, P.G. (1991). Penetration of cells by herpes simplex virus does not require a low pH-dependent endocytic pathway.Virus Res.18, 271\u2013290.","DOI":"10.1016\/0168-1702(91)90024-P"},{"key":"REF62","doi-asserted-by":"crossref","unstructured":"Zalevsky, J., Grigorova, I., and Mullins, R.D. (2001). Activation of the Arp2\/3 complex by theListeriaacta protein. Acta binds two actin monomers and three subunits of the Arp2\/3 complex.J. Biol. Chem.276, 3468\u20133475.","DOI":"10.1074\/jbc.M006407200"},{"key":"REF63","doi-asserted-by":"crossref","unstructured":"Zhang, J.et al.(1999). Antigen receptor-induced activation and cytoskeletal rearrangement are impaired in Wiskott-Aldrich syndrome protein-deficient lymphocytes.J. Exp. Med.190, 1329\u20131342.","DOI":"10.1084\/jem.190.9.1329"},{"key":"REF64","doi-asserted-by":"crossref","unstructured":"Zhang, J., Shi, F., Badour, K., Deng, Y., McGavin, M.K., and Siminovitch, K.A. (2002). WASp verprolin homology, cofilin homology, and acidic region domain-mediated actin polymerization is required for T cell development.Proc. Natl. Acad. Sci. 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