Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Identifieur interne : 000978 ( PubMed/Corpus ); précédent : 000977; suivant : 000979Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Auteurs : Lei Yan ; Bing Meng ; Jiangchao Xiang ; Ian A. Wilson ; Bei YangSource :
- Acta crystallographica. Section D, Structural biology [ 2059-7983 ] ; 2018.
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
Links to Exploration step
pubmed:30198895Le document en format XML
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Wilson</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:30198895</idno><idno type="pmid">30198895</idno><idno type="doi">10.1107/S2059798318008318</idno><idno type="wicri:Area/PubMed/Corpus">000978</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000978</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.</title><author><name sortKey="Yan, Lei" sort="Yan, Lei" uniqKey="Yan L" first="Lei" last="Yan">Lei Yan</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Meng, Bing" sort="Meng, Bing" uniqKey="Meng B" first="Bing" last="Meng">Bing Meng</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Xiang, Jiangchao" sort="Xiang, Jiangchao" uniqKey="Xiang J" first="Jiangchao" last="Xiang">Jiangchao Xiang</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A" last="Wilson">Ian A. Wilson</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Bei" sort="Yang, Bei" uniqKey="Yang B" first="Bei" last="Yang">Bei Yang</name><affiliation><nlm:affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</nlm:affiliation></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="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="physiology" xml:lang="en"><term>Coronavirus 229E, Human</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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30198895</PMID><DateCompleted><Year>2018</Year><Month>11</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2059-7983</ISSN><JournalIssue CitedMedium="Internet"><Volume>74</Volume><Issue>Pt 9</Issue><PubDate><Year>2018</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Acta crystallographica. Section D, Structural biology</Title><ISOAbbreviation>Acta Crystallogr D Struct Biol</ISOAbbreviation></Journal><ArticleTitle>Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.</ArticleTitle><Pagination><MedlinePgn>841-851</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1107/S2059798318008318</ELocationID><Abstract><AbstractText>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.</AbstractText><CopyrightInformation>open access.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Lei</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meng</LastName><ForeName>Bing</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xiang</LastName><ForeName>Jiangchao</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wilson</LastName><ForeName>Ian A</ForeName><Initials>IA</Initials><AffiliationInfo><Affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Bei</ForeName><Initials>B</Initials><Identifier Source="ORCID">0000-0001-5389-3859</Identifier><AffiliationInfo><Affiliation>Shanghai Institute for Advanced Immunochemical Studies, ShanghaiTech University, 393 Middle Huaxia Road, Shanghai 201210, People's Republic of China.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>UM1 AI100663</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>31600619</GrantID><Agency>National Natural Science Foundation of China</Agency><Country></Country></Grant><Grant><GrantID>16PJ1407500</GrantID><Agency>Science and Technology Commission of Shanghai Municipality</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Acta Crystallogr D Struct Biol</MedlineTA><NlmUniqueID>101676043</NlmUniqueID><ISSNLinking>2059-7983</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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