HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Wengler, G. Articles by Wengler, G. Search for Related Content PubMed PubMed Citation Articles by Wengler, G. Articles by Wengler, G. Agricola Articles by Wengler, G. Articles by Wengler, G.

In vitro analysis of factors involved in the disassembly of Sindbis virus cores by 60S ribosomal subunits identifies a possible role of low pH

Institut für Virologie der Veterinärmedizin, Justus-Liebig-Universität Giessen, 35392 Giessen, Germany¹

Author for correspondence: Gerd Wengler. Fax +49 641 23960. e-mail gerd.wengler{at}gmx.de

Disassembly of alphavirus cores early in infection involves interaction of the core with 60S ribosomal subunits. This interaction might be subjected to regulatory processes. We have established an in vitro system of core disassembly in order to identify cellular proteins involved in the regulation of disassembly. No evidence for the existence of such proteins was found, but it became apparent that certain organic solvents and detergents or a high proton concentration (pH 6·0) stimulated core disassembly. Alphaviruses infect cells by an endosomal pathway. The low pH in the endosome activates a fusion activity of the viral surface protein E1 and leads to fusion of the viral membrane with the endosomal membrane, followed by release of the core into the cytoplasm. Since the presence of the E1 protein in the plasma membrane of infected cells leads to increased membrane permeability at low pH, our findings indicate that disassembly of alphavirus cores could be regulated by the proton concentration. We propose that the viral membrane proteins present in the endosomal membrane after fusion form a pore, which allows the flow of protons from the endosome into the cytoplasm. This process would generate a region of low pH in the cytoplasm at the correct time and place to allow the efficient disassembly of the incoming viral core by 60S subunits.

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]

				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]

				G. Wengler, A. Koschinski, G. Wengler, and F. Dreyer Entry of alphaviruses at the plasma membrane converts the viral surface proteins into an ion-permeable pore that can be detected by electrophysiological analyses of whole-cell membrane currents J. Gen. Virol., January 1, 2003; 84(1): 173 - 181. [Abstract] [Full Text] [PDF]