| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Institut für Virologie der Veterinärmedizin and
2 Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität, D-35392 Giessen, Germany
Correspondence
Gerd Wengler
gerd.wengler{at}gmx.de
Alphaviruses are small enveloped viruses that have been used extensively as model enveloped viruses. During infection, virus particles are taken up into endosomes, where a low pH activates the viral fusion protein, E1. Fusion of the viral and the endosomal membranes releases the viral core into the cytoplasm where cores are disassembled by interaction with 60S ribosomal subunits. Recently, we have shown that in vitro this disassembly is strongly stimulated by low pH. We have proposed that after entry of the core into the cytoplasm, the viral membrane proteins that have been transferred to the endosomal membrane form an ion-permeable pore in the endosome. The resulting flow of protons from the endosome into the cytoplasm through this pore could generate a low-pH environment for core disassembly in vivo. Here we report two types of analysis aimed at the identification of such pores. First, the release of [3H]choline from the interior of liposomes was analysed in the presence of virus particles and viral proteins. Secondly, cells were infected with Sindbis or Semliki Forest alphaviruses at the plasma membrane and the possible generation of ion-permeable pores during this process was analysed by whole-cell voltage clamp analysis of the membrane current. The results obtained indicated that the proposed pores are in fact generated and allowed us to identify the formation of individual pores. Available evidence indicates that the alphavirus E1 protein probably forms these pores. Proteins homologous to the alphavirus E1 protein are present in flaviviruses and hepatitis C virus.
This article has been cited by other articles:
|
|
 |
|
  K. Tamm, A. Merits, and I. Sarand Mutations in the nuclear localization signal of nsP2 influencing RNA synthesis, protein expression and cytotoxicity of Semliki Forest virus J. Gen. Virol., March 1, 2008; 89(3): 676 - 686. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Wengler, G. Wengler, and A. Koschinski A short treatment of cells with the lanthanide ions La3+, Ce3+, Pr3+ or Nd3+ changes the cellular chemistry into a state in which RNA replication of flaviviruses is specifically blocked without interference with host-cell multiplication J. Gen. Virol., November 1, 2007; 88(11): 3018 - 3026. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Koschinski, G. Wengler, G. Wengler, and H. Repp Rare earth ions block the ion pores generated by the class II fusion proteins of alphaviruses and allow analysis of the biological functions of these pores J. Gen. Virol., December 1, 2005; 86(12): 3311 - 3320. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. T. Tosteson, H. Wang, A. Naumov, and M. Chow Poliovirus binding to its receptor in lipid bilayers results in particle-specific, temperature-sensitive channels J. Gen. Virol., June 1, 2004; 85(6): 1581 - 1589. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Wengler, A. Koschinski, G. Wengler, and H. Repp During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores J. Gen. Virol., June 1, 2004; 85(6): 1695 - 1701. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Koschinski, G. Wengler, G. Wengler, and H. Repp The membrane proteins of flaviviruses form ion-permeable pores in the target membrane after fusion: identification of the pores and analysis of their possible role in virus infection J. Gen. Virol., July 1, 2003; 84(7): 1711 - 1721. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
