Viral membrane fusion

被引:550
作者
Harrison, Stephen C. [1 ,2 ]
机构
[1] Harvard Univ, Sch Med, Boston Childrens Hosp, 3 Blackfan Circle, Boston, MA 02115 USA
[2] Howard Hughes Med Inst, Boston, MA 02115 USA
关键词
Virus entry; Fusion mechanism; Fusion protein; SEMLIKI-FOREST-VIRUS; HIV-1 ENVELOPE TRIMER; NIEMANN-PICK C1; CRYSTAL-STRUCTURE; INFLUENZA HEMAGGLUTININ; DENGUE VIRUS; CRYOELECTRON MICROSCOPY; GLYCOPROTEIN TRIMERS; PREFUSION FORM; CORE STRUCTURE;
D O I
10.1016/j.virol.2015.03.043
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics. (C) 2015 The Author. Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
引用
收藏
页码:498 / 507
页数:10
相关论文
共 101 条
[1]   Characterization of Monomeric Intermediates during VSV Glycoprotein Structural Transition [J].
Albertini, Aurelie A. ;
Merigoux, Cecile ;
Libersou, Sonia ;
Madiona, Karine ;
Bressanelli, Stephane ;
Roche, Stephane ;
Lepault, Jean ;
Melki, Ronald ;
Vachette, Patrice ;
Gaudin, Yves .
PLOS PATHOGENS, 2012, 8 (02)
[2]   The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition [J].
Armstrong, RT ;
Kushnir, AS ;
White, JM .
JOURNAL OF CELL BIOLOGY, 2000, 151 (02) :425-437
[3]   Class III viral membrane fusion proteins [J].
Backovic, Marija ;
Jardetzky, Theodore S. .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2009, 19 (02) :189-196
[4]   Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy [J].
Bartesaghi, Alberto ;
Merk, Alan ;
Borgnia, Mario J. ;
Milne, Jacqueline L. S. ;
Subramaniam, Sriram .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2013, 20 (12) :1352-1357
[5]   Cryo-Electron Tomography of Rubella Virus [J].
Battisti, Anthony J. ;
Yoder, Joshua D. ;
Plevka, Pavel ;
Winkler, Dennis C. ;
Prasad, Vidya Mangala ;
Kuhn, Richard J. ;
Frey, Teryl K. ;
Steven, Alasdair C. ;
Rossmann, Michael G. .
JOURNAL OF VIROLOGY, 2012, 86 (20) :11078-11085
[6]   TRIMERIC SUBDOMAIN OF THE SIMIAN IMMUNODEFICIENCY VIRUS GLYCOPROTEIN [J].
BLACKLOW, SC ;
LU, M ;
KIM, P .
BIOCHEMISTRY, 1995, 34 (46) :14955-14962
[7]   Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering [J].
Bose, Sayantan ;
Zokarkar, Aarohi ;
Welch, Brett D. ;
Leser, George P. ;
Jardetzky, Theodore S. ;
Lamb, Robert A. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (39) :E2625-E2634
[8]   A Stabilized Headless Measles Virus Attachment Protein Stalk Efficiently Triggers Membrane Fusion [J].
Brindley, Melinda A. ;
Suter, Rolf ;
Schestak, Isabel ;
Kiss, Gabriella ;
Wright, Elizabeth R. ;
Plemper, Richard K. .
JOURNAL OF VIROLOGY, 2013, 87 (21) :11693-11703
[9]   STRUCTURE OF INFLUENZA HEMAGGLUTININ AT THE PH OF MEMBRANE-FUSION [J].
BULLOUGH, PA ;
HUGHSON, FM ;
SKEHEL, JJ ;
WILEY, DC .
NATURE, 1994, 371 (6492) :37-43
[10]   Structural organization of a filamentous influenza A virus [J].
Calder, Lesley J. ;
Wasilewski, Sebastian ;
Berriman, John A. ;
Rosenthal, Peter B. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (23) :10685-10690