Locations of Carbohydrate Sites on Alphavirus Glycoproteins Show that E1 Forms an Icosahedral Scaffold
Identifieur interne : 003465 ( Main/Exploration ); précédent : 003464; suivant : 003466Locations of Carbohydrate Sites on Alphavirus Glycoproteins Show that E1 Forms an Icosahedral Scaffold
Auteurs : Sergei V. Pletnev [États-Unis] ; Wei Zhang [États-Unis] ; Suchetana Mukhopadhyay [États-Unis] ; Bonnie R. Fisher [États-Unis] ; Raquel Hernandez [États-Unis] ; Dennis T. Brown [États-Unis] ; Timothy S. Baker [États-Unis] ; Michael G. Rossmann [États-Unis] ; Richard J. Kuhn [États-Unis]Source :
- Cell [ 0092-8674 ] ; 2001.
English descriptors
- Teeft :
- Academic press, Alphavirus, Amino, Amino acid sequence, Amino acids, Biol, Blue contours, Bottom panel, Carbohydrate, Carbohydrate difference density, Carbohydrate difference peaks, Carbohydrate moieties, Carbohydrate site, Carbohydrate sites, Cell biol, Cheng, Cryoelectron microscopy, Cryoem, Cryoem density, Cryoem reconstructions, Crystal structure, Difference maps, Dimer, Encephalitis virus, Equivalenced sites, Experimental procedures, Flavivirus, Fusion peptide, Fusion process, Garoff, Glycoprotein, Glycoprotein spikes, Glycosylation, Glycosylation site, Glycosylation sites, Green contours, Grid points, Growth properties, Growth rates, Host cell membranes, Hydrophobic interaction, Icosahedral, Icosahedral axis, Icosahedral lattice, Icosahedral scaffold, Icosahedral surface lattice, Influenza virus, Kielian, Lattice, Lipid bilayer, Mature virions, Medium size plaques, Membrane, Membrane fusion, Membrane protein, Moiety, Mutant, Mutant virus, Mutant viruses, Mutation, Mutation sites, Native sinv, Nucleocapsid, Pink contours, Plaque, Plaque size, Plasma membrane, Potential glycosylation sites, Rossmann, Schlesinger, Semliki, Semliki forest virus, Semliki forest virus spike, Sindbis, Sindbis virus, Sinv, Sinv glycoproteins, Spike, Strauss, Structural changes, Supplemental table, Surface glycoprotein, Symmetry axes, Tbev, Transmembrane domain, Trimer, Viral, Viral membrane, Viral surface, Virion, Virol, Virus, Virus mutants, Virus production.
Abstract
Abstract: 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.
Url:
DOI: 10.1016/S0092-8674(01)00302-6
Affiliations:
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Pletnev</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Indiana</region></placeName><wicri:cityArea>Department of Biological Sciences, Purdue University, West Lafayette</wicri:cityArea></affiliation></author><author><name sortKey="Zhang, Wei" sort="Zhang, Wei" uniqKey="Zhang W" first="Wei" last="Zhang">Wei Zhang</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Indiana</region></placeName><wicri:cityArea>Department of Biological Sciences, Purdue University, West Lafayette</wicri:cityArea></affiliation></author><author><name sortKey="Mukhopadhyay, Suchetana" sort="Mukhopadhyay, Suchetana" uniqKey="Mukhopadhyay S" first="Suchetana" last="Mukhopadhyay">Suchetana Mukhopadhyay</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Indiana</region></placeName><wicri:cityArea>Department of Biological Sciences, Purdue University, West Lafayette</wicri:cityArea></affiliation></author><author><name sortKey="Fisher, Bonnie R" sort="Fisher, Bonnie R" uniqKey="Fisher B" first="Bonnie R." last="Fisher">Bonnie R. Fisher</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Indiana</region></placeName><wicri:cityArea>Department of Biological Sciences, Purdue University, West Lafayette</wicri:cityArea></affiliation></author><author><name sortKey="Hernandez, Raquel" sort="Hernandez, Raquel" uniqKey="Hernandez R" first="Raquel" last="Hernandez">Raquel Hernandez</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Department of Molecular and Structural, Biochemistry, North Carolina State University, Raleigh</wicri:cityArea></affiliation></author><author><name sortKey="Brown, Dennis T" sort="Brown, Dennis T" uniqKey="Brown D" first="Dennis T." last="Brown">Dennis T. 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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.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li><li>Indiana</li></region></list><tree><country name="États-Unis"><region name="Indiana"><name sortKey="Pletnev, Sergei V" sort="Pletnev, Sergei V" uniqKey="Pletnev S" first="Sergei V." last="Pletnev">Sergei V. Pletnev</name></region><name sortKey="Baker, Timothy S" sort="Baker, Timothy S" uniqKey="Baker T" first="Timothy S." last="Baker">Timothy S. Baker</name><name sortKey="Brown, Dennis T" sort="Brown, Dennis T" uniqKey="Brown D" first="Dennis T." last="Brown">Dennis T. Brown</name><name sortKey="Fisher, Bonnie R" sort="Fisher, Bonnie R" uniqKey="Fisher B" first="Bonnie R." last="Fisher">Bonnie R. Fisher</name><name sortKey="Hernandez, Raquel" sort="Hernandez, Raquel" uniqKey="Hernandez R" first="Raquel" last="Hernandez">Raquel Hernandez</name><name sortKey="Kuhn, Richard J" sort="Kuhn, Richard J" uniqKey="Kuhn R" first="Richard J." last="Kuhn">Richard J. Kuhn</name><name sortKey="Mukhopadhyay, Suchetana" sort="Mukhopadhyay, Suchetana" uniqKey="Mukhopadhyay S" first="Suchetana" last="Mukhopadhyay">Suchetana Mukhopadhyay</name><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name><name sortKey="Rossmann, Michael G" sort="Rossmann, Michael G" uniqKey="Rossmann M" first="Michael G." last="Rossmann">Michael G. Rossmann</name><name sortKey="Zhang, Wei" sort="Zhang, Wei" uniqKey="Zhang W" first="Wei" last="Zhang">Wei Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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