Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.
Identifieur interne : 003F45 ( Main/Exploration ); précédent : 003F44; suivant : 003F46Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.
Auteurs : Fang Li [États-Unis] ; Marcelo Berardi ; Wenhui Li ; Michael Farzan ; Philip R. Dormitzer ; Stephen C. HarrisonSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- Complexes multiprotéiques (), Complexes multiprotéiques (métabolisme), Complexes multiprotéiques (ultrastructure), Concentration en ions d'hydrogène, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Glycoprotéines membranaires (ultrastructure), Liaison aux protéines, Microscopie électronique, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (métabolisme), Peptidyl-Dipeptidase A (ultrastructure), Pliage des protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Protéines de l'enveloppe virale (ultrastructure), Protéines recombinantes (), Protéines recombinantes (métabolisme), Protéines recombinantes (ultrastructure), Réactifs réticulants (), Récepteurs viraux (), Récepteurs viraux (métabolisme), Structure quaternaire des protéines, Structure tertiaire des protéines, Virus du SRAS (physiologie).
- MESH :
- métabolisme : Complexes multiprotéiques, Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Protéines recombinantes, Récepteurs viraux.
- physiologie : Virus du SRAS.
- ultrastructure : Complexes multiprotéiques, Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Protéines recombinantes.
- Complexes multiprotéiques, Concentration en ions d'hydrogène, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Liaison aux protéines, Microscopie électronique, Peptidyl-Dipeptidase A, Pliage des protéines, Protéines de l'enveloppe virale, Protéines recombinantes, Réactifs réticulants, Récepteurs viraux, Structure quaternaire des protéines, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Cross-Linking Reagents (chemistry), Hydrogen-Ion Concentration, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Membrane Glycoproteins (ultrastructure), Microscopy, Electron, Multiprotein Complexes (chemistry), Multiprotein Complexes (metabolism), Multiprotein Complexes (ultrastructure), Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (metabolism), Peptidyl-Dipeptidase A (ultrastructure), Protein Binding, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Recombinant Proteins (ultrastructure), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (ultrastructure).
- MESH :
- chemical , chemistry : Cross-Linking Reagents, Membrane Glycoproteins, Multiprotein Complexes, Peptidyl-Dipeptidase A, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Multiprotein Complexes, Peptidyl-Dipeptidase A, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- chemical , ultrastructure : Membrane Glycoproteins, Multiprotein Complexes, Peptidyl-Dipeptidase A, Recombinant Proteins, Viral Envelope Proteins.
- physiology : SARS Virus.
- Hydrogen-Ion Concentration, Microscopy, Electron, Protein Binding, Protein Folding, Protein Structure, Quaternary, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.
Abstract
The severe acute respiratory syndrome coronavirus enters cells through the activities of a spike protein (S) which has receptor-binding (S1) and membrane fusion (S2) regions. We have characterized four sequential states of a purified recombinant S ectodomain (S-e) comprising S1 and the ectodomain of S2. They are S-e monomers, uncleaved S-e trimers, cleaved S-e trimers, and dissociated S1 monomers and S2 trimer rosettes. Lowered pH induces an irreversible transition from flexible, L-shaped S-e monomers to clove-shaped trimers. Protease cleavage of the trimer occurs at the S1-S2 boundary; an ensuing S1 dissociation leads to a major rearrangement of the trimeric S2 and to formation of rosettes likely to represent clusters of elongated, postfusion trimers of S2 associated through their fusion peptides. The states and transitions of S suggest conformational changes that mediate viral entry into cells.
DOI: 10.1128/JVI.02744-05
PubMed: 16809285
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 002185
- to stream PubMed, to step Curation: 002185
- to stream PubMed, to step Checkpoint: 002252
- to stream Ncbi, to step Merge: 001556
- to stream Ncbi, to step Curation: 001556
- to stream Ncbi, to step Checkpoint: 001556
- to stream Main, to step Merge: 004150
- to stream Main, to step Curation: 003F45
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.</title><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Molecular Medicine, Children's Hospital, 320 Longwood Ave., Boston, MA 02115, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Molecular Medicine, Children's Hospital, 320 Longwood Ave., Boston, MA 02115</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Berardi, Marcelo" sort="Berardi, Marcelo" uniqKey="Berardi M" first="Marcelo" last="Berardi">Marcelo Berardi</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Dormitzer, Philip R" sort="Dormitzer, Philip R" uniqKey="Dormitzer P" first="Philip R" last="Dormitzer">Philip R. Dormitzer</name></author><author><name sortKey="Harrison, Stephen C" sort="Harrison, Stephen C" uniqKey="Harrison S" first="Stephen C" last="Harrison">Stephen C. Harrison</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16809285</idno><idno type="pmid">16809285</idno><idno type="doi">10.1128/JVI.02744-05</idno><idno type="wicri:Area/PubMed/Corpus">002185</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002185</idno><idno type="wicri:Area/PubMed/Curation">002185</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002185</idno><idno type="wicri:Area/PubMed/Checkpoint">002252</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002252</idno><idno type="wicri:Area/Ncbi/Merge">001556</idno><idno type="wicri:Area/Ncbi/Curation">001556</idno><idno type="wicri:Area/Ncbi/Checkpoint">001556</idno><idno type="wicri:doubleKey">0022-538X:2006:Li F:conformational:states:of</idno><idno type="wicri:Area/Main/Merge">004150</idno><idno type="wicri:Area/Main/Curation">003F45</idno><idno type="wicri:Area/Main/Exploration">003F45</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.</title><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Molecular Medicine, Children's Hospital, 320 Longwood Ave., Boston, MA 02115, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Laboratory of Molecular Medicine, Children's Hospital, 320 Longwood Ave., Boston, MA 02115</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Berardi, Marcelo" sort="Berardi, Marcelo" uniqKey="Berardi M" first="Marcelo" last="Berardi">Marcelo Berardi</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Dormitzer, Philip R" sort="Dormitzer, Philip R" uniqKey="Dormitzer P" first="Philip R" last="Dormitzer">Philip R. Dormitzer</name></author><author><name sortKey="Harrison, Stephen C" sort="Harrison, Stephen C" uniqKey="Harrison S" first="Stephen C" last="Harrison">Stephen C. Harrison</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cross-Linking Reagents (chemistry)</term><term>Hydrogen-Ion Concentration</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (metabolism)</term><term>Membrane Glycoproteins (ultrastructure)</term><term>Microscopy, Electron</term><term>Multiprotein Complexes (chemistry)</term><term>Multiprotein Complexes (metabolism)</term><term>Multiprotein Complexes (ultrastructure)</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Peptidyl-Dipeptidase A (ultrastructure)</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (metabolism)</term><term>Recombinant Proteins (ultrastructure)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Envelope Proteins (ultrastructure)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexes multiprotéiques ()</term><term>Complexes multiprotéiques (métabolisme)</term><term>Complexes multiprotéiques (ultrastructure)</term><term>Concentration en ions d'hydrogène</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Glycoprotéines membranaires (ultrastructure)</term><term>Liaison aux protéines</term><term>Microscopie électronique</term><term>Peptidyl-Dipeptidase A ()</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Peptidyl-Dipeptidase A (ultrastructure)</term><term>Pliage des protéines</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines de l'enveloppe virale (ultrastructure)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines recombinantes (ultrastructure)</term><term>Réactifs réticulants ()</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cross-Linking Reagents</term><term>Membrane Glycoproteins</term><term>Multiprotein Complexes</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Multiprotein Complexes</term><term>Peptidyl-Dipeptidase A</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Membrane Glycoproteins</term><term>Multiprotein Complexes</term><term>Peptidyl-Dipeptidase A</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Glycoprotéines membranaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Glycoprotéines membranaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Microscopy, Electron</term><term>Protein Binding</term><term>Protein Folding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Tertiary</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Concentration en ions d'hydrogène</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Liaison aux protéines</term><term>Microscopie électronique</term><term>Peptidyl-Dipeptidase A</term><term>Pliage des protéines</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Réactifs réticulants</term><term>Récepteurs viraux</term><term>Structure quaternaire des protéines</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus enters cells through the activities of a spike protein (S) which has receptor-binding (S1) and membrane fusion (S2) regions. We have characterized four sequential states of a purified recombinant S ectodomain (S-e) comprising S1 and the ectodomain of S2. They are S-e monomers, uncleaved S-e trimers, cleaved S-e trimers, and dissociated S1 monomers and S2 trimer rosettes. Lowered pH induces an irreversible transition from flexible, L-shaped S-e monomers to clove-shaped trimers. Protease cleavage of the trimer occurs at the S1-S2 boundary; an ensuing S1 dissociation leads to a major rearrangement of the trimeric S2 and to formation of rosettes likely to represent clusters of elongated, postfusion trimers of S2 associated through their fusion peptides. The states and transitions of S suggest conformational changes that mediate viral entry into cells.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><noCountry><name sortKey="Berardi, Marcelo" sort="Berardi, Marcelo" uniqKey="Berardi M" first="Marcelo" last="Berardi">Marcelo Berardi</name><name sortKey="Dormitzer, Philip R" sort="Dormitzer, Philip R" uniqKey="Dormitzer P" first="Philip R" last="Dormitzer">Philip R. Dormitzer</name><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name><name sortKey="Harrison, Stephen C" sort="Harrison, Stephen C" uniqKey="Harrison S" first="Stephen C" last="Harrison">Stephen C. Harrison</name><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></noCountry><country name="États-Unis"><region name="Massachusetts"><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 003F45 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 003F45 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:16809285
|texte= Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:16809285" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |