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During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores

Gerd Wengler^1,

Andreas Koschinski^2,

¹ Institut für Virologie der Veterinärmedizin, Justus-Liebig-Universität, D-35392 Giessen, Germany
² Rudolf-Buchheim-Institut für Pharmakologie, Justus-Liebig-Universität, D-35392 Giessen, Germany

Correspondence
Gerd Wengler
gerd.wengler{at}gmx.de

Studies using the alphavirus Semliki Forest virus have indicated that the viral E1 fusion protein forms two types of pore: fusion pores and ion-permeable pores. The formation of ion-permeable pores has not been generally accepted, partly because it was not evident how the protein might form these different pores. Here it is proposed that the choice of the target membrane determines whether a fusion pore or ion-permeable pores are formed. The fusion protein is activated in the endosome and for steric reasons only a fraction of the activated molecules can interact with the endosomal membrane. This target membrane reaction forms the fusion pore. It is proposed that the rest of the activated molecules interact with the membrane in which the protein is anchored and that this self-membrane reaction leads to formation of ion-permeable pores, which can be detected in the target membrane after fusion of the viral membrane into the target membrane.

These authors made equal contributions to this work.

This article has been cited by other articles:

				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]