The Actin Cytoskeleton and Bacterial Infection PDF
Preview The Actin Cytoskeleton and Bacterial Infection
Current Topics in Microbiology and Immunology Hans Georg Mannherz Editor The Actin Cytoskeleton and Bacterial Infection Current Topics in Microbiology and Immunology Volume 399 Serieseditors RafiAhmed SchoolofMedicine,RollinsResearchCenter,EmoryUniversity,RoomG211,1510CliftonRoad,Atlanta,GA30322, USA KlausAktories MedizinischeFakultät,InstitutfürExperimentelleundKlinischePharmakologieundToxikologie,Abt.I, Albert-Ludwigs-UniversitätFreiburg,Albertstr.25,79104Freiburg,Germany ArturoCasadevall W.HarryFeinstoneDepartmentofMolecularMicrobiology&Immunology,JohnsHopkinsBloombergSchool ofPublicHealth,615N.WolfeStreet,RoomE5132,Baltimore,MD21205USA RichardW.Compans DepartmentofMicrobiologyandImmunology,EmoryUniversity,1518CliftonRoad,CNR5005,Atlanta,GA30322, USA JorgeE.Galan BoyerCtr.forMolecularMedicine,SchoolofMedicine,YaleUniversity,295CongressAvenue,room343, NewHaven,CT06536-0812,USA AdolfoGarcía-Sastre IcahnSchoolofMedicineatMountSinai,DepartmentofMicrobiology,1468MadisonAve.,Box1124,NewYork NY10029,USA TasukuHonjo FacultyofMedicine,DepartmentofMedicalChemistry,KyotoUniversity,Sakyo-ku,Yoshida,Kyoto606-8501,Japan YoshihiroKawaoka InfluenzaResearchInstitute,UniversityofWisconsin-Madison,575ScienceDrive,Madison,WI53711,USA BernardMalissen Centred’ImmunologiedeMarseille-Luminy,ParcScientifiquedeLuminy,Case906,13288,MarseilleCedex9,France MichaelB.A.Oldstone DepartmentofImmunologyandMicrobialScience,TheScrippsResearchInstitute,10550NorthTorreyPinesRoad,La Jolla,CA92037,USA KlausPalme InstituteofBiologyII/MolecularPlantPhysiology,Albert-Ludwigs-UniversitätFreiburg, 79104Freiburg,Germany RinoRappuoli GSKVaccines,ViaFiorentina1,Siena,53100,Italy PeterK.Vogt DepartmentofMolecularandExperimentalMedicine,TheScrippsResearchInstitute,BCC-239, 10550NorthTorreyPinesRoadLaJolla,CA92037USA HonoraryEditor HilaryKoprowski(deceased) FormerlyatBiotechnologyFoundation,Inc.,Ardmore,PA,USA More information about this series at http://www.springer.com/series/82 Hans Georg Mannherz Editor The Actin Cytoskeleton and Bacterial Infection Responsible Series Editor: Klaus Aktories 123 Editor Hans GeorgMannherz Institut für Anatomie, Abteilung für AnatomieundMolekulare Embryologie Ruhr-Universität Bochum Bochum Germany ISSN 0070-217X ISSN 2196-9965 (electronic) CurrentTopics inMicrobiology andImmunology ISBN978-3-319-50046-1 ISBN978-3-319-50047-8 (eBook) DOI 10.1007/978-3-319-50047-8 LibraryofCongressControlNumber:2016960308 ©SpringerInternationalPublishingAG2017 Thisworkissubjecttocopyright.AllrightsarereservedbythePublisher,whetherthewholeorpart of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission orinformationstorageandretrieval,electronicadaptation,computersoftware,orbysimilarordissimilar methodologynowknownorhereafterdeveloped. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publicationdoesnotimply,evenintheabsenceofaspecificstatement,thatsuchnamesareexemptfrom therelevantprotectivelawsandregulationsandthereforefreeforgeneraluse. The publisher, the authors and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authorsortheeditorsgiveawarranty,expressorimplied,withrespecttothematerialcontainedhereinor for any errors or omissions that may have been made. The publisher remains neutral with regard to jurisdictionalclaimsinpublishedmapsandinstitutionalaffiliations. Printedonacid-freepaper ThisSpringerimprintispublishedbySpringerNature TheregisteredcompanyisSpringerInternationalPublishingAG Theregisteredcompanyaddressis:Gewerbestrasse11,6330Cham,Switzerland Preface Three types of cytoplasmic filaments form the cellular cytoskeleton. These fila- ments often extent from the cell nucleus to the plasma membrane. They stabilise cell shape and provide tensile strength. Different classes of proteins form the dif- ferent types offilaments: A large number of tissue specific proteins (the interme- diate filament proteins) form the intermediate filaments, proteins of the tubulin familybuildthemicrotubules,andtheactinsthemicrofilaments,whichorganizethe actincytoskeleton.Thecytoskeletalfilamentsdifferinstructureandfunctions.The intermediate filaments have mainly shape stabilising functions. In addition to cell shape stabilising functions the microtubules provide the routes for the intracellular transport of vesicles and form the spindle apparatus during cell division, the actin cytoskeleton participates in a number of motile processes like cell locomotion and more specialized processes as endo- and exocytosis, vesicular transport, and cytokinesis. The supramolecular structure of the cytoskeleton is subjected to con- stant reorganization according to the cellular activities. In the past the different filament types have been regarded as separate functional entities, recent data, however,stronglyindicatestructural andfunctionallinkages(as alsodemonstrated by the contribution by Schwan and Aktories). Actin is the most abundant protein in many eukaryotic cells. In mammals six tissue-specificisoforms assembletotheactin containing microfilaments, whichare often organized into bundles or higher ordered networks. The highly dynamic behaviouroftheactincytoskeletonisregulatedbyalargenumberofactinbinding proteins (ABP). The ABPs can be grouped into different functional classes, which regulate the assembly or disassembly of actin filaments and are often targets of signalling pathways. Bacteriahaveevolvedalargearsenaloftoxinsandeffectors,someofwhichare injected into host cells by type-3 secretion mechanisms to avoid phagocytosis by professional macrophages (see contribution by Aepfelbacher & Wolters). Alternatively,bacterialtoxinsorvirulencefactorsinducespecialplasmamembrane extensions of non-professional phagocytotic cells, which embrace bacteria leading totheiruptakeintohostcellswiththeaimtosecuretheirsurvivalbygainingaccess tonutrientsforproliferation,toachievetransportwithinthecytoplasmorfromcell v vi Preface to cell and finally their release into the environment for further dissemination (see contribution by Stradal & Costa). The actin cytoskeleton is essential for all these processes. Therefore it is not surprising that actin is a preferred target of many bacterial toxins and effector proteins also due to its highly conserved primary and ternary structure and its intracellular abundance. With the 11 contributions this volume tries to introduce this fast progressing field of research without pretending completeness. Bacteria have evolved a vast number of tricks to secure their survival and proliferation. Therefore only a few bacteria and their toxins and effectors will be introduced with the intention to indicatecommonmodesofaction.Thestructure,propertiesanddynamicbehaviour of actin cytoskeleton itself and the different classes of actin-binding proteins (ABP) will introduced with constant reference to bacterial toxins and effectors, which interfere their functions by modifying their normal behaviour (Kühn & Mannherz). Bacterial toxins or effectors affect either the actin cytoskeleton by modifying actindirectlyorsubvertingcertainABPsorsignallingpathwaysleadingtotheactin cytoskeleton by modifying small GTP-binding proteins terminating at regulatory ABPs (see contributions by Aepfelbacher & Wolters, Lemichez, and Stradal & Costa). Often a bacterium has developed toxins aiming on both mechanisms to influence the actin cytoskeleton like for instance Photorhabdus luminescens (con- tributionbyLangetal.),Clostridia(Schwan&Aktories),Yersinia(contributionby Aepfelbacher & Wolters). A number of bacterial toxins modify actin directly by ADP-ribosylation or cross-linking. These modifications subvert the normal functioning of the actin cytoskeletonandtherebysecure bacterialsurvivalbyinhibitingphagocytosis.This area willbe covered by four contributions, which extend from theircellular effects to structural studies illuminating their selectivity. How phagocytosis is normally able to eliminate bacterial invasion is detailed for the uptake of Borrelia by mac- rophages in one contribution (Naj & Linder). ADP-ribosyltransferases also modify small GTP-binding proteins of the Rho-family resulting in dramatic effects in their signalling capacity to the actin cytoskeleton(onespecialcontributionandpartofanumberofothercontributions). Alternatively, extracellular gastrointestinal pathogens manipulate the signalling pathways leading to the actin cytoskeleton by secreting virulence factors that modify the GTPase cycle of host Rho-GTPases thus securing their survival (This topic will be covered with two contributions (by Lemichez and Stradal & Costa). Some intracellular bacteria hijack the actin cytoskeleton to their own needs by presenting on one pole bacterial proteins that lead to the assembly of a comet-like F-actin tail able by rapid actin subunit treadmilling to propel the pathogen within the cytoplasm of the host cell and for further dissemination from cell to cell (see contribution by Pillich et al.). In many instances the analysis of the action of bacterial toxins and virulence factors provided important clues to the function of endogenous ABPs or even helped to identify ABPs, which were binding partners of certain bacterial effector proteins like the Arp2/3 complex as partner of ActA of Listeria. Future studies on Preface vii bacterial toxins will certainly uncover new insights into their functions and also unravelnewaspectsoftheinherentregulatorymechanismoftheactincytoskeleton, which might also lead to the development of new antibiotic drugs. As a further outlookinthisperspectivethisvolumeincludesadescriptionofthebacterialactins, which are different in primary but similar ternary structure to their eukaryotic counterparts, and their interactors (contribution by Gayathri). Bochum, Germany Hans Georg Mannherz Contents Actin: Structure, Function, Dynamics, and Interactions with Bacterial Toxins ... .... ..... .... .... .... .... .... ..... .... 1 Sonja Kühn and Hans Georg Mannherz Formation of Nanotube-Like Protrusions, Regulation of Septin Organization and Re-guidance of Vesicle Traffic by Depolymerization of the Actin Cytoskeleton Induced by Binary Bacterial Protein Toxins. .... .... .... .... .... ..... .... 35 Carsten Schwan and Klaus Aktories Photorhabdus luminescens Toxins TccC3 and TccC5 Affect the Interaction of Actin with Actin-Binding Proteins Essential for Treadmilling ... .... .... ..... .... .... .... .... .... ..... .... 53 Alexander E. Lang, Sonja Kühn and Hans Georg Mannherz Comparative Studies of Actin- and Rho-Specific ADP-Ribosylating Toxins: Insight from Structural Biology. .... .... .... .... ..... .... 69 Hideaki Tsuge, Toshiharu Tsurumura, Akiyuki Toda, Haruka Murata, Waraphan Toniti and Toru Yoshida Pathogenic Mechanisms of Actin Cross-Linking Toxins: Peeling Away the Layers... .... .... ..... .... .... .... .... .... ..... .... 87 Elena Kudryashova, David B. Heisler and Dmitri S. Kudryashov ActA of Listeria monocytogenes and Its Manifold Activities as an Important Listerial Virulence Factor... .... .... .... ..... .... 113 Helena Pillich, Madhu Puri and Trinad Chakraborty Actin-Dependent Regulation of Borrelia burgdorferi Phagocytosis by Macrophages ... .... .... ..... .... .... .... .... .... ..... .... 133 Xenia Naj and Stefan Linder New Aspects on Bacterial Effectors Targeting Rho GTPases. ..... .... 155 Emmanuel Lemichez ix x Contents Type III Secreted Virulence Factors Manipulating Signaling to Actin Dynamics.. .... .... ..... .... .... .... .... .... ..... .... 175 Theresia E.B. Stradal and Sonia C.P. Costa Acting on Actin: Rac and Rho Played by Yersinia. .... .... ..... .... 201 Martin Aepfelbacher and Manuel Wolters Bacterial Actins and Their Interactors .. .... .... .... .... ..... .... 221 Pananghat Gayathri
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