Viroporins

被引:310
作者
Gonzalez, ME
Carrasco, L
机构
[1] Inst Salud Carlos III, Unidad Expres Viral, Ctr Nacl Microbiol, Madrid 28220, Spain
[2] Univ Autonoma Madrid, Ctr Biol Mol Severo Ochoa, Fac Ciencias, E-28049 Madrid, Spain
关键词
animal virus; membrane permeability; membrane pore; channel ion; virus budding;
D O I
10.1016/S0014-5793(03)00780-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Viroporins are a group of proteins that participate in several viral functions, including the promotion of release of viral particles from cells. These proteins also affect cellular functions, including the cell vesicle system, glycoprotein trafficking and membrane permeability. Viroporins are not essential for the replication of viruses, but their presence enhances virus growth. Comprising some 60-120 amin(C)o acids, viroporins have a hydrophobic transmembrane domain that interacts with and expands the lipid bilayer. Some viroporins also contain other motifs, such as basic amino acid residues or a domain rich in aromatic amino acids that confers on the protein the ability to interact with the interfacial lipid bilayer. Viroporin oligomerization gives rise to hydrophilic pores at the membranes of virus-infected cells. As the list of known viroporins steadily grows, recent research efforts focus on deciphering the actions of the viroporins poliovirus 2B, alphavirus 6K, HIV-1 Vpu and influenza virus M2. All these proteins can enhance the passage of ions and small molecules through membranes depending on their concentration gradient. Future work will lengthen the list of viroporins and will provide a deeper understanding of their mechanisms of action. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:28 / 34
页数:7
相关论文
共 99 条
[1]   Viroporin-mediated membrane permeabilization - Pore formation by nonstructural poliovirus 2B protein [J].
Agirre, A ;
Barco, A ;
Carrasco, L ;
Nieva, JL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (43) :40434-40441
[2]   Membrane permeabilization by poliovirus proteins 2B and 2BC [J].
Aldabe, R ;
Barco, A ;
Carrasco, L .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (38) :23134-23137
[3]   Genetic analysis of the cell-to-cell movement of beet yellows closterovirus [J].
Alzhanova, DV ;
Hagiwara, Y ;
Peremyslov, VV ;
Dolja, VV .
VIROLOGY, 2000, 268 (01) :192-200
[4]   MEMBRANE PERMEABILIZATION BY DIFFERENT REGIONS OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 TRANSMEMBRANE GLYCOPROTEIN GP41 [J].
ARROYO, J ;
BOCETA, M ;
GONZALEZ, ME ;
MICHEL, M ;
CARRASCO, L .
JOURNAL OF VIROLOGY, 1995, 69 (07) :4095-4102
[5]   Identification of regions of poliovirus 2BC protein that are involved in cytotoxicity [J].
Barco, A ;
Carrasco, L .
JOURNAL OF VIROLOGY, 1998, 72 (05) :3560-3570
[6]   HUMAN VIRUS PROTEIN, POLIOVIRUS PROTEIN 2BC, INDUCES MEMBRANE PROLIFERATION AND BLOCKS THE EXOCYTIC PATHWAY IN THE YEAST SACCHAROMYCES-CEREVISIAE [J].
BARCO, A ;
CARRASCO, L .
EMBO JOURNAL, 1995, 14 (14) :3349-3364
[7]   The vaccinia virus A14.5L gene encodes a hydrophobic 53-amino-acid virion membrane protein that enhances virulence in mice and is conserved among vertebrate poxviruses [J].
Betakova, T ;
Wolffe, EJ ;
Moss, B .
JOURNAL OF VIROLOGY, 2000, 74 (09) :4085-4092
[8]   Cell killing by HIV-1 protease [J].
Blanco, R ;
Carrasco, L ;
Ventoso, I .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (02) :1086-1093
[9]   Modification of late membrane permeability in avian reovirus-infected cells -: Viroporin activity of the S1-encoded nonstructural p10 protein [J].
Bodelón, G ;
Labrada, L ;
Martínez-Costas, J ;
Benavente, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (20) :17789-17796
[10]   Cell surface CD4 inhibits HTV-1 particle release by interfering with Vpu activity [J].
Bour, S ;
Perrin, C ;
Strebel, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (47) :33800-33806