Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Identifieur interne : 000C99 ( Main/Exploration ); précédent : 000C98; suivant : 000D00Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Auteurs : Lei Yan [République populaire de Chine] ; Bing Meng [République populaire de Chine] ; Jiangchao Xiang [République populaire de Chine] ; Ian A. Wilson [République populaire de Chine] ; Bei Yang [République populaire de Chine]Source :
- Acta crystallographica. Section D, Structural biology [ 2059-7983 ] ; 2018.
Descripteurs français
- KwdFr :
- Alignement de séquences, Conformation des protéines, Coronavirus humain 229E (isolement et purification), Coronavirus humain 229E (physiologie), Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus (), Humains, Infections à coronavirus (virologie), Modèles moléculaires, Protéines de fusion recombinantes (), Séquence d'acides aminés.
- MESH :
- isolement et purification : Coronavirus humain 229E.
- physiologie : Coronavirus humain 229E.
- virologie : Infections à coronavirus.
- Alignement de séquences, Conformation des protéines, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Humains, Modèles moléculaires, Protéines de fusion recombinantes, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Coronavirus 229E, Human (isolation & purification), Coronavirus 229E, Human (physiology), Coronavirus Infections (virology), Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Recombinant Fusion Proteins (chemistry), Sequence Alignment, Spike Glycoprotein, Coronavirus (chemistry).
- MESH :
- chemical , chemistry : Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- isolation & purification : Coronavirus 229E, Human.
- physiology : Coronavirus 229E, Human.
- virology : Coronavirus Infections.
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Models, Molecular, Protein Conformation, Sequence Alignment.
Abstract
Human coronavirus 229E (HCoV-229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV-229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six-helix membrane-fusion structure termed the fusion core. Here, the complete fusion-core structure of HCoV-229E has been determined at 1.86 Å resolution, representing the most complete post-fusion conformation thus far among published human alphacoronavirus (α-HCoV) fusion-core structures. The overall structure of the HCoV-229E fusion core is similar to those of SARS, MERS and HCoV-NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side-by-side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α-HCoVs and β-HCoVs at certain positions and that the HCoV-229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure-based design of pan-coronavirus small molecules or peptides to inhibit viral fusion.
DOI: 10.1107/S2059798318008318
PubMed: 30198895
Affiliations:
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Wilson</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210</wicri:regionArea><wicri:noRegion>Shanghai 201210</wicri:noRegion></affiliation></author><author><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210</wicri:regionArea><wicri:noRegion>Shanghai 201210</wicri:noRegion></affiliation></author></analytic><series><title level="j">Acta crystallographica. Section D, Structural biology</title><idno type="eISSN">2059-7983</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Coronavirus 229E, Human (isolation & purification)</term><term>Coronavirus 229E, Human (physiology)</term><term>Coronavirus Infections (virology)</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Sequence Alignment</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Coronavirus humain 229E (isolement et purification)</term><term>Coronavirus humain 229E (physiologie)</term><term>Cristallographie aux rayons X</term><term>Glycoprotéine de spicule des coronavirus ()</term><term>Humains</term><term>Infections à coronavirus (virologie)</term><term>Modèles moléculaires</term><term>Protéines de fusion recombinantes ()</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Coronavirus humain 229E</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus humain 229E</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus 229E, Human</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à coronavirus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronavirus Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Conformation des protéines</term><term>Cristallographie aux rayons X</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Modèles moléculaires</term><term>Protéines de fusion recombinantes</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human coronavirus 229E (HCoV-229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV-229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six-helix membrane-fusion structure termed the fusion core. Here, the complete fusion-core structure of HCoV-229E has been determined at 1.86 Å resolution, representing the most complete post-fusion conformation thus far among published human alphacoronavirus (α-HCoV) fusion-core structures. The overall structure of the HCoV-229E fusion core is similar to those of SARS, MERS and HCoV-NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side-by-side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α-HCoVs and β-HCoVs at certain positions and that the HCoV-229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure-based design of pan-coronavirus small molecules or peptides to inhibit viral fusion.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Yan, Lei" sort="Yan, Lei" uniqKey="Yan L" first="Lei" last="Yan">Lei Yan</name></noRegion><name sortKey="Meng, Bing" sort="Meng, Bing" uniqKey="Meng B" first="Bing" last="Meng">Bing Meng</name><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name><name sortKey="Xiang, Jiangchao" sort="Xiang, Jiangchao" uniqKey="Xiang J" first="Jiangchao" last="Xiang">Jiangchao Xiang</name><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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