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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
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| Zeitschriftentitel: | Journal of General Virology |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | Journal of General Virology, 85, 2004, 6, S. 1695-1701 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Microbiology Society
|
| Schlagwörter: |
| author_facet |
Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger |
|---|---|
| author |
Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger |
| spellingShingle |
Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger Journal of General Virology During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores Virology |
| author_sort |
wengler, gerd |
| spelling |
Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger 0022-1317 1465-2099 Microbiology Society Virology http://dx.doi.org/10.1099/vir.0.79845-0 <jats:p>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.</jats:p> During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores Journal of General Virology |
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Microbiology Society, 2004 |
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Microbiology Society, 2004 |
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0022-1317 1465-2099 |
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2004 |
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Microbiology Society |
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Journal of General Virology |
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| title |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_unstemmed |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_full |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_fullStr |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_full_unstemmed |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_short |
During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_sort |
during entry of alphaviruses, the e1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| topic |
Virology |
| url |
http://dx.doi.org/10.1099/vir.0.79845-0 |
| publishDate |
2004 |
| physical |
1695-1701 |
| description |
<jats:p>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.</jats:p> |
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| author | Wengler, Gerd, Koschinski, Andreas, Wengler, Gisela, Repp, Holger |
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| description | <jats:p>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.</jats:p> |
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| physical | 1695-1701 |
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| spelling | Wengler, Gerd Koschinski, Andreas Wengler, Gisela Repp, Holger 0022-1317 1465-2099 Microbiology Society Virology http://dx.doi.org/10.1099/vir.0.79845-0 <jats:p>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.</jats:p> During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores Journal of General Virology |
| spellingShingle | Wengler, Gerd, Koschinski, Andreas, Wengler, Gisela, Repp, Holger, Journal of General Virology, During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores, Virology |
| title | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_full | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_fullStr | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_full_unstemmed | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_short | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_sort | during entry of alphaviruses, the e1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| title_unstemmed | During entry of alphaviruses, the E1 glycoprotein molecules probably form two separate populations that generate either a fusion pore or ion-permeable pores |
| topic | Virology |
| url | http://dx.doi.org/10.1099/vir.0.79845-0 |