| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Rudolf-Buchheim-Institut für Pharmakologie1, Justus-Liebig-Universität, D-35392 Giessen, Germany
2 Institut für Virologie der Veterinärmedizin2, Justus-Liebig-Universität, D-35392 Giessen, Germany
Correspondence
Gerd Wengler
gerd.wengler{at}gmx.de
Recently, we presented evidence that the E1 fusion protein of the alphavirus Semliki Forest virus forms ion-permeable pores in the target membrane after fusion. We proposed that the homologous fusion proteins of flaviviruses and hepatitis C virus form similar pores. To test this hypothesis for the E fusion protein of flaviviruses, the release of [3H]choline from liposomes by the flavivirus West Nile (WN) virus was determined. [3H]Choline was released at mildly acid pH. The pH threshold depended on the lipid composition. Release from certain liposomes was activated even at neutral pH. To identify the generation of individual pores, single cells were investigated with the patch-clamp technique. The formation of individual pores during low pH-induced WN virus entry at the plasma membrane occurred within seconds. These experiments were performed in parallel with Semliki Forest virus. The results indicated that, similar to alphavirus infection, infection with flaviviruses via endosomes leads to the formation of ion-permeable pores in the endosome after fusion, which allows the flow of protons from the endosome into the cytoplasm during virus entry. However, in vitro translation experiments of viral cores showed that, in contrast to alphaviruses, which probably need this proton flow for core disassembly, the genome RNA of WN virus present in the viral core is directly accessible for translation. For entry of flaviviruses, therefore, a second pathway for productive infection may exist, in which fusion of the viral membrane is activated at neutral pH by contact with a plasma membrane of appropriate lipid composition.
This article has been cited by other articles:
|
|
 |
|
  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, H. Repp, B. Unver, F. Dreyer, D. Brockmeier, A. Valeva, S. Bhakdi, and I. Walev Why Escherichia coli {alpha}-hemolysin induces calcium oscillations in mammalian cells--the pore is on its own FASEB J, May 1, 2006; 20(7): 973 - 975. [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]
|
|
|
|
|
|
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]
|
|
|
|
 |
|
 F. A. Rey Dengue virus envelope glycoprotein structure: New insight into its interactions during viral entry PNAS, June 10, 2003; 100(12): 6899 - 6901. [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 | |
