Protein-lipid interactions critical to replication of the influenza A virus

被引:39
作者
Chlanda, Petr [1 ]
Zimmerberg, Joshua [1 ]
机构
[1] Eunice Kennedy Shriver Natl Inst Child Hlth & Hum, Sect Integrat Biophys, NIH, Bethesda, MD 20892 USA
关键词
influenza virus; lipid microdomains; membrane fission; membrane fusion; virus budding; virus entry; HEMAGGLUTININ FUSION PEPTIDE; MEMBRANE-FUSION; M2; PROTEIN; MATRIX PROTEIN; CHOLESTEROL-BINDING; CYTOPLASMIC TAIL; PLASMA-MEMBRANE; M1; LOW PH; CRYOELECTRON TOMOGRAPHY;
D O I
10.1002/1873-3468.12118
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Influenza A virus (IAV) assembles on the plasma membrane where viral proteins localize to form a bud encompassing the viral genome, which ultimately pinches off to give rise to newly formed infectious virions. Upon entry, the virus faces the opposite task-fusion with the endosomal membrane and disassembly to deliver the viral genome to the cytoplasm. There are at least four influenza proteins-hemagglutinin (HA), neuraminidase (NA), matrix 1 protein (M1), and the M2 ion channel-that are known to directly interact with the cellular membrane and modify membrane curvature in order to both assemble and disassemble membrane-enveloped virions. Here, we summarize and discuss current knowledge of the interactions of lipids and membrane proteins involved in the IAV replication cycle.
引用
收藏
页码:1940 / 1954
页数:15
相关论文
共 103 条
[1]
Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein [J].
Ali, A ;
Avalos, RT ;
Ponimaskin, E ;
Nayak, DP .
JOURNAL OF VIROLOGY, 2000, 74 (18) :8709-8719
[2]
Influenza A virus uses the aggresome processing machinery for host cell entry [J].
Banerjee, Indranil ;
Miyake, Yasuyuki ;
Nobs, Samuel Philip ;
Schneider, Christoph ;
Horvath, Peter ;
Kopf, Manfred ;
Matthias, Patrick ;
Helenius, Ari ;
Yamauchi, Yohei .
SCIENCE, 2014, 346 (6208) :473-477
[3]
pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane Fusion [J].
Batishchev, O. V. ;
Shilova, L. A. ;
Kachala, M. V. ;
Tashkin, V. Y. ;
Sokolov, V. S. ;
Fedorova, N. V. ;
Baratova, L. A. ;
Knyazev, D. G. ;
Zimmerberg, J. ;
Chizmadzhev, Y. A. .
JOURNAL OF VIROLOGY, 2016, 90 (01) :575-585
[4]
Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin [J].
Biswas, Subrata ;
Yin, Shu-Rong ;
Blank, Paul S. ;
Zimmerberg, Joshua .
JOURNAL OF GENERAL PHYSIOLOGY, 2008, 131 (05) :503-513
[5]
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
[6]
Intrinsically disordered proteins drive membrane curvature [J].
Busch, David J. ;
Houser, Justin R. ;
Hayden, Carl C. ;
Sherman, Michael B. ;
Lafer, Eileen M. ;
Stachowiak, Jeanne C. .
NATURE COMMUNICATIONS, 2015, 6
[7]
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
[8]
Direct Visualization of the Action of Triton X-100 on Giant Vesicles of Erythrocyte Membrane Lipids [J].
Casadei, Bruna R. ;
Domingues, Cleyton C. ;
de Paula, Eneida ;
Riske, Karin A. .
BIOPHYSICAL JOURNAL, 2014, 106 (11) :2417-2425
[9]
The Influenza Virus M2 Protein Cytoplasmic Tail Interacts with the M1 Protein and Influences Virus Assembly at the Site of Virus Budding [J].
Chen, Benjamin J. ;
Leser, George P. ;
Jackson, David ;
Lamb, Robert A. .
JOURNAL OF VIROLOGY, 2008, 82 (20) :10059-10070
[10]
Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles [J].
Chen, Benjamin J. ;
Leser, George P. ;
Morita, Eiji ;
Lamb, Robert A. .
JOURNAL OF VIROLOGY, 2007, 81 (13) :7111-7123