Locations of Carbohydrate Sites on Alphavirus Glycoproteins Show that E1 Forms an Icosahedral Scaffold

There are 80 spikes on the surface of Sindbis virus arranged as an icosahedral surface lattice. Each spike consists of three copies of each of the glycoproteins E1 and E2. There are two glycosylation sites on E1 and two on E2. These four sites have been located by removal of the glycosylation recogn...

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Bibliographic Details
Published in:Cell 2001-04, Vol.105 (1), p.127-136
Main Authors: Pletnev, Sergei V., Zhang, Wei, Mukhopadhyay, Suchetana, Fisher, Bonnie R., Hernandez, Raquel, Brown, Dennis T., Baker, Timothy S., Rossmann, Michael G., Kuhn, Richard J.
Format: Article
Language:English
Subjects:
AE1 protein
AE2 protein
Alphavirus
Alphavirus - chemistry
Alphavirus - genetics
Alphavirus - ultrastructure
Amino Acid Motifs - genetics
Animals
Binding Sites - genetics
Carbohydrates - chemistry
Cell Line
Cricetinae
Cryoelectron Microscopy
E1 protein
E2 protein
Encephalitis Viruses, Tick-Borne - chemistry
Flavivirus
Glycosylation
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - genetics
Models, Molecular
Mutagenesis, Site-Directed
Protein Conformation
Ross River virus - chemistry
Sindbis virus
Sindbis Virus - chemistry
Sindbis Virus - ultrastructure
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - genetics
Viral Fusion Proteins - chemistry
Viral Fusion Proteins - genetics
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Summary:There are 80 spikes on the surface of Sindbis virus arranged as an icosahedral surface lattice. Each spike consists of three copies of each of the glycoproteins E1 and E2. There are two glycosylation sites on E1 and two on E2. These four sites have been located by removal of the glycosylation recognition motifs using site-specific mutagenesis, followed by cryoelectron microscopy. The positions of these sites have demonstrated that E2 forms the protruding spikes and that E1 must be long and narrow, lying flat on the viral surface, forming an icosahedral scaffold analogous to the arrangement of the E glycoprotein in flaviviruses. This arrangement of E1 leads to both dimeric and trimeric intermolecular contacts, consistent with the observed structural changes that occur on fusion with host cell membranes, suggesting a similar fusion mechanism for alpha- and flaviviruses.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(01)00302-6