Viral exploitation of actin: force-generation and scaffolding functions in viral infection
- 295 Downloads
As a fundamental component of the host cellular cytoskeleton, actin is routinely engaged by infecting viruses. Furthermore, viruses from diverse groups, and infecting diverse hosts, have convergently evolved an array of mechanisms for manipulating the actin cytoskeleton for efficacious infection. An ongoing chorus of research now indicates that the actin cytoskeleton is critical for viral replication at many stages of the viral life cycle, including binding, entry, nuclear localization, genomic transcription and reverse transcription, assembly, and egress/dissemination. Specifically, viruses subvert the force-generating and macromolecular scaffolding properties of the actin cytoskeleton to propel viral surfing, internalization, and migration within the cell. Additionally, viruses utilize the actin cytoskeleton to support and organize assembly sites, and eject budding virions for cell-to-cell transmission. It is the purpose of this review to provide an overview of current research, focusing on the various mechanisms and themes of virus-mediated actin modulation described therein.
Keywordsviral infection actin cytoskeleton cofilin LIMK Arp2/3 GTPase
Unable to display preview. Download preview PDF.
- Barrero-Villar M, Cabrero J R, Gordón-Alonso M, Barroso-González J, Alvarez-Losada S, Muñoz-Fernández M A, Sánchez-Madrid F, Valenzuela-Fernández A. 2009. Moesin is required for HIV-1-induced CD4-CXCR4 interaction, F-actin redistribution, membrane fusion and viral infection in lymphocytes. J Cell Sci, 122: 103–113.PubMedCrossRefGoogle Scholar
- Cameron P U, Saleh S, Sallmann G, Solomon A, Wightman F, Evans V A, Boucher G, Haddad E K, Sekaly R-P, Harman A N, Anderson J L, Jones K L, Mak J, Cunningham A L, Jaworowski A, Lewin S R. 2010. Establishment of HIV-1 latency in resting CD4+ T cells depends on chemokine-induced changes in the actin cytoskeleton. Proc Natl Acad Sci U S A, 107: 16934–16939.PubMedCentralPubMedCrossRefGoogle Scholar
- Hiller G, Jungwirth C, Weber K. 1981. Fluorescence microscopical analysis of the life cycle of vaccinia virus in chick embryo fibroblasts. Virus-cytoskeleton interactions. Exp Cell Res, 132: 81–87.Google Scholar
- Kimura T, Hashimoto I, Yamamoto A, Nishikawa M, Fujisawa J I. 2000. Rev-dependent association of the intron-containing HIV-1 gag mRNA with the nuclear actin bundles and the inhibition of its nucleocytoplasmic transport by latrunculin-B. Genes Cells Devoted Mol Cell Mech, 5: 289–307.CrossRefGoogle Scholar
- Sowinski S, Jolly C, Berninghausen O, Purbhoo M A, Chauveau A, Köhler K, Oddos S, Eissmann P, Brodsky F M, Hopkins C, Onfelt B, Sattentau Q, Davis D M. 2008. Membrane nanotubes physically connect T cells over long distances presenting a novel route for HIV-1 transmission. Nat Cell Biol, 10: 211–219.PubMedCrossRefGoogle Scholar
- Vasiliver-Shamis G, Tuen M, Wu T W, Starr T, Cameron T O, Thomson R, Kaur G, Liu J, Visciano M L, Li H, Kumar R, Ansari R, Han D P, Cho M W, Dustin M L, Hioe C E. 2008. Human immunodeficiency virus type 1 envelope gp120 induces a stop signal and virological synapse formation in noninfected CD4+ T cells. J Virol, 82: 9445–9457.PubMedCentralPubMedCrossRefGoogle Scholar
- Wakimoto H, Shimodo M, Satoh Y, Kitagawa Y, Takeuchi K, Gotoh B, Itoh M. 2013. F-Actin Modulates Measles Virus Cell-Cell Fusion and Assembly by Altering the Interaction between the Matrix Protein and the Cytoplasmic Tail of Hemagglutinin. J Virol, 87: 1974–1984.PubMedCentralPubMedCrossRefGoogle Scholar
- Wen X, Ding L, Wang J-J, Qi M, Hammonds J, Chu H, Chen X, Hunter E, Spearman P. 2014. ROCK1 and LIM Kinase Modulate Retrovirus Particle Release and Cell-Cell Transmission Events. J Virol,; DOI: 10.1128/JVI.00023-14.Google Scholar
- Yoder A, Yu D, Dong L, Iyer S R, Xu X, Kelly J, Liu J, Wang W, Vorster P J, Agulto L, Stephany D A, Cooper J N, Marsh J W, Wu Y. 2008. HIV envelope-CXCR4 signaling activates cofilin to overcome cortical actin restriction in resting CD4 T cells. Cell, 134: 782–792.PubMedCentralPubMedCrossRefGoogle Scholar