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      How HIV Takes Advantage of the Cytoskeleton in Entry and Replication

      review-article
      Author(s): , *
      Publication date (Electronic):
      Journal: Viruses
      Publisher: Molecular Diversity Preservation International (MDPI)
      Keywords: HIV, actin cytoskeleton, entry, Nef, cofilin

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          Abstract

          The host cell cytoskeleton plays a key role in the life cycle of viral pathogens whose propagation depends on mandatory intracellular steps. Accordingly, also the human immunodeficiency virus type 1 (HIV-1) has evolved strategies to exploit and modulate in particular the actin cytoskeleton for its purposes. This review will recapitulate recent findings on how HIV-1 hijacks the cytoskeleton to facilitate entry into, transport within and egress from host cells as well as to commandeer communication of infected with uninfected bystander cells.

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          Actin, a central player in cell shape and movement.

          Thomas Pollard, John Cooper (2009)
          The protein actin forms filaments that provide cells with mechanical support and driving forces for movement. Actin contributes to biological processes such as sensing environmental forces, internalizing membrane vesicles, moving over surfaces, and dividing the cell in two. These cellular activities are complex; they depend on interactions of actin monomers and filaments with numerous other proteins. Here, we present a summary of the key questions in the field and suggest how those questions might be answered. Understanding actin-based biological phenomena will depend on identifying the participating molecules and defining their molecular mechanisms. Comparisons of quantitative measurements of reactions in live cells with computer simulations of mathematical models will also help generate meaningful insights.
          Article 0 comments Cited 607 times – based on 0 reviews     Review now
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            Cellular motility driven by assembly and disassembly of actin filaments.

            Thomas Pollard, Gary Borisy (2003)
            Motile cells extend a leading edge by assembling a branched network of actin filaments that produces physical force as the polymers grow beneath the plasma membrane. A core set of proteins including actin, Arp2/3 complex, profilin, capping protein, and ADF/cofilin can reconstitute the process in vitro, and mathematical models of the constituent reactions predict the rate of motion. Signaling pathways converging on WASp/Scar proteins regulate the activity of Arp2/3 complex, which mediates the initiation of new filaments as branches on preexisting filaments. After a brief spurt of growth, capping protein terminates the elongation of the filaments. After filaments have aged by hydrolysis of their bound ATP and dissociation of the gamma phosphate, ADF/cofilin proteins promote debranching and depolymerization. Profilin catalyzes the exchange of ADP for ATP, refilling the pool of ATP-actin monomers bound to profilin, ready for elongation.
            Article 0 comments Cited 572 times – based on 0 reviews     Review now
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              HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes.

              Kosuke Miyauchi, Yuri Kim, Olga S. Latinovic … (2009)
              Enveloped viruses that rely on a low pH-dependent step for entry initiate infection by fusing with acidic endosomes, whereas the entry sites for pH-independent viruses, such as HIV-1, have not been defined. These viruses have long been assumed to fuse directly with the plasma membrane. Here we used population-based measurements of the viral content delivery into the cytosol and time-resolved imaging of single viruses to demonstrate that complete HIV-1 fusion occurred in endosomes. In contrast, viral fusion with the plasma membrane did not progress beyond the lipid mixing step. HIV-1 underwent receptor-mediated internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. We also show that, strikingly, endosomal fusion is sensitive to a dynamin inhibitor, dynasore. These findings imply that HIV-1 infects cells via endocytosis and envelope glycoprotein- and dynamin-dependent fusion with intracellular compartments.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Viruses
                Title: Viruses
                Publisher: Molecular Diversity Preservation International (MDPI)
                ISSN (Electronic): 1999-4915
                Publication date (Electronic): 28 March 2011
                Publication date Collection: April 2011
                Volume: 3
                Issue: 4
                Pages: 293-311
                Affiliations
                Department of Infectious Diseases, Virology, University Hospital Heidelberg, Im Neuenheimer Feld 324, D-69120 Heidelberg, Germany; E-Mail: bettina.stolp@ 123456med.uni-heidelberg.de
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: oliver.fackler@ 123456med.uni-heidelberg.de ; Tel.: +49-6221-56-1322; Fax: +49-6221-56-5003.
                Article
                Publisher ID: viruses-03-00293
                DOI: 10.3390/v3040293
                PMC ID: 3185699
                PubMed ID: 21994733
                SO-VID: 39d80bd5-c7f7-4797-9e3f-ec2d6b97e976
                Copyright © © 2011 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 2 February 2011
                Date revision received : 11 March 2011
                Date accepted : 19 March 2011
                Categories
                Subject: Review

                ScienceOpen disciplines: Microbiology & Virology
                Keywords: hiv,entry,actin cytoskeleton,nef,cofilin
                Data availability:
                ScienceOpen disciplines: Microbiology & Virology
                Keywords: hiv, entry, actin cytoskeleton, nef, cofilin

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