Viroporins

被引:306
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
  • [71] A functionally defined model for the M-2 proton channel of influenza A virus suggests a mechanism for its ion selectivity
    Pinto, LH
    Dieckmann, GR
    Gandhi, CS
    Papworth, CG
    Braman, J
    Shaughnessy, MA
    Lear, JD
    Lamb, RA
    DeGrado, WF
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (21) : 11301 - 11306
  • [72] INFLUENZA-VIRUS M2 PROTEIN HAS ION CHANNEL ACTIVITY
    PINTO, LH
    HOLSINGER, LJ
    LAMB, RA
    [J]. CELL, 1992, 69 (03) : 517 - 528
  • [73] A potassium channel protein encoded by chlorella virus PBCV-1
    Plugge, B
    Gazzarrini, S
    Nelson, M
    Cerana, R
    Van Etten, JL
    Derst, C
    DiFrancesco, D
    Moroni, A
    Thiel, G
    [J]. SCIENCE, 2000, 287 (5458) : 1641 - 1644
  • [74] THE SPECIFIC-INHIBITION OF INFLUENZA-A VIRUS MATURATION BY AMANTADINE - AN ELECTRON-MICROSCOPIC EXAMINATION
    RUIGROK, RWH
    HIRST, EMA
    HAY, AJ
    [J]. JOURNAL OF GENERAL VIROLOGY, 1991, 72 : 191 - 194
  • [75] The ion channel activity of the influenza virus M(2) protein affects transport through the Golgi apparatus
    Sakaguchi, T
    Leser, GP
    Lamb, RA
    [J]. JOURNAL OF CELL BIOLOGY, 1996, 133 (04) : 733 - 747
  • [76] Overexpression of the vaccinia virus A38L integral membrane protein promotes Ca2+ influx into infected cells
    Sanderson, CM
    Parkinson, JE
    Hollinshead, M
    Smith, GL
    [J]. JOURNAL OF VIROLOGY, 1996, 70 (02) : 905 - 914
  • [77] Poliovirus infection and expression of the poliovirus protein 2B provoke the disassembly of the Golgi complex, the organelle target for the antipoliovirus drug Ro-090179
    Sandoval, IV
    Carrasco, L
    [J]. JOURNAL OF VIROLOGY, 1997, 71 (06) : 4679 - 4693
  • [78] SANZ MA, 1994, J BIOL CHEM, V269, P12106
  • [79] Interfacial domains in Sindbis virus 6K protein - Detection and functional characterization
    Sanz, MA
    Madan, V
    Carrasco, L
    Nieva, JL
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (03) : 2051 - 2057
  • [80] Sindbis virus variant with a deletion in the 6K gene shows defects in glycoprotein processing and trafficking:: Lack of complementation by a wild-type 6K gene in trans
    Sanz, MA
    Carrasco, L
    [J]. JOURNAL OF VIROLOGY, 2001, 75 (16) : 7778 - 7784