Formation of membrane domains induced by the G and M proteins of vesicular stomatitis virus
Luan, Peng
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Permalink
https://hdl.handle.net/2142/23449
Description
Title
Formation of membrane domains induced by the G and M proteins of vesicular stomatitis virus
Author(s)
Luan, Peng
Issue Date
1994
Doctoral Committee Chair(s)
Glaser, Michael
Department of Study
Chemistry, Biochemistry
Discipline
Chemistry, Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
Vesicular stomatitis virus (VSV) buds from specialized regions or domains on the plasma membrane of infected cells. These domains are composed mainly of viral proteins and they are enriched in certain lipid species. The properties of the two envelope-associated proteins of VSV, the glycoprotein (G) and the matrix protein (M), were investigated in reconstituted lipid vesicles in order to understand the mechanism of virus budding and domain formation. Fluorescence resonance energy transfer and fluorescence digital imaging microscopy were used to determine if the proteins could alter the lateral distribution of the phospholipids in the vesicles. Large domains enriched in PA were formed when either the G or M protein was reconstituted into the vesicles. Analysis of the images showed that the M protein could further enrich the PA domains caused by the G protein. The M protein also had the ability to induce the formation of domains enriched in PS. When both the G and M proteins were incorporated into vesicles at the same time, sphingomyelin and cholesterol were also sequestered into domains. Both the G and M proteins co-localized with the domains induced by the proteins. Thus, the G and M proteins together could induce the formation of large domains enriched in PA, PS, sphingomyelin, cholesterol and the viral proteins. PC was excluded from the domains. Gramicidin was chosen to represent the distribution of an integral membrane protein when domains were induced by the G and M proteins. Gramicidin showed no lipid specificity and was excluded from the domains. Analysis of the images by the digital imaging system showed that the lipid composition of the domains closely resembled the composition of the VSV envelope. These observations suggest that the two envelope-associated proteins of VSV are important in the formation of domains during the process of virus budding from the plasma membrane of the host cells.
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