The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus.
Identifieur interne : 000434 ( PubMed/Corpus ); précédent : 000433; suivant : 000435The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus.
Auteurs : Qingliang Shen ; Danyun Zeng ; Baoyu Zhao ; Veer S. Bhatt ; Pingwei Li ; Jae-Hyun ChoSource :
- ACS chemical biology [ 1554-8937 ] ; 2017.
English descriptors
- KwdEn :
- Binding Sites, Humans, Influenza A Virus, H1N1 Subtype (chemistry), Influenza A Virus, H1N1 Subtype (pathogenicity), Influenza Pandemic, 1918-1919, Protein Binding, Proto-Oncogene Proteins c-crk (chemistry), Proto-Oncogene Proteins c-crk (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism), src Homology Domains.
- MESH :
- chemical , chemistry : Proto-Oncogene Proteins c-crk, Viral Nonstructural Proteins.
- chemistry : Influenza A Virus, H1N1 Subtype.
- chemical , metabolism : Proto-Oncogene Proteins c-crk, Viral Nonstructural Proteins.
- pathogenicity : Influenza A Virus, H1N1 Subtype.
- Binding Sites, Humans, Influenza Pandemic, 1918-1919, Protein Binding, src Homology Domains.
Abstract
The 1918 Spanish influenza A virus (IAV) caused one of the most serious pandemics in history. The nonstructural protein 1 (NS1) of the 1918 IAV hijacks the interaction between human CrkII and JNK1. Little is, however, known about its molecular mechanism. Here, we performed X-ray crystallography, NMR relaxation dispersion experiment, and fluorescence spectroscopy to determine the structural, kinetic, and thermodynamic mechanisms underlying the hijacking of CrkII by 1918 IAV NS1. We observed that the interaction between a proline-rich motif in NS1 and the N-terminal SH3 domain of CrkII displays strikingly rapid kinetics and exceptionally high affinity with 100-fold faster kon and 3300-fold lower Kd compared to those for the CrkII-JNK1 interaction. These results provide molecular insight into the mechanism by which 1918 IAV NS1 hijacks CrkII and disrupts its interactions with critical cellular signaling proteins.
DOI: 10.1021/acschembio.7b00168
PubMed: 28368102
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pubmed:28368102Le document en format XML
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Bhatt</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Pingwei" sort="Li, Pingwei" uniqKey="Li P" first="Pingwei" last="Li">Pingwei Li</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Cho, Jae Hyun" sort="Cho, Jae Hyun" uniqKey="Cho J" first="Jae-Hyun" last="Cho">Jae-Hyun Cho</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28368102</idno><idno type="pmid">28368102</idno><idno type="doi">10.1021/acschembio.7b00168</idno><idno type="wicri:Area/PubMed/Corpus">000434</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000434</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus.</title><author><name sortKey="Shen, Qingliang" sort="Shen, Qingliang" uniqKey="Shen Q" first="Qingliang" last="Shen">Qingliang Shen</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Zeng, Danyun" sort="Zeng, Danyun" uniqKey="Zeng D" first="Danyun" last="Zeng">Danyun Zeng</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Zhao, Baoyu" sort="Zhao, Baoyu" uniqKey="Zhao B" first="Baoyu" last="Zhao">Baoyu Zhao</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Bhatt, Veer S" sort="Bhatt, Veer S" uniqKey="Bhatt V" first="Veer S" last="Bhatt">Veer S. Bhatt</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Li, Pingwei" sort="Li, Pingwei" uniqKey="Li P" first="Pingwei" last="Li">Pingwei Li</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author><author><name sortKey="Cho, Jae Hyun" sort="Cho, Jae Hyun" uniqKey="Cho J" first="Jae-Hyun" last="Cho">Jae-Hyun Cho</name><affiliation><nlm:affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</nlm:affiliation></affiliation></author></analytic><series><title level="j">ACS chemical biology</title><idno type="eISSN">1554-8937</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites</term><term>Humans</term><term>Influenza A Virus, H1N1 Subtype (chemistry)</term><term>Influenza A Virus, H1N1 Subtype (pathogenicity)</term><term>Influenza Pandemic, 1918-1919</term><term>Protein Binding</term><term>Proto-Oncogene Proteins c-crk (chemistry)</term><term>Proto-Oncogene Proteins c-crk (metabolism)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>src Homology Domains</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proto-Oncogene Proteins c-crk</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proto-Oncogene Proteins c-crk</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Humans</term><term>Influenza Pandemic, 1918-1919</term><term>Protein Binding</term><term>src Homology Domains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 1918 Spanish influenza A virus (IAV) caused one of the most serious pandemics in history. The nonstructural protein 1 (NS1) of the 1918 IAV hijacks the interaction between human CrkII and JNK1. Little is, however, known about its molecular mechanism. Here, we performed X-ray crystallography, NMR relaxation dispersion experiment, and fluorescence spectroscopy to determine the structural, kinetic, and thermodynamic mechanisms underlying the hijacking of CrkII by 1918 IAV NS1. We observed that the interaction between a proline-rich motif in NS1 and the N-terminal SH3 domain of CrkII displays strikingly rapid kinetics and exceptionally high affinity with 100-fold faster k<sub>on</sub> and 3300-fold lower K<sub>d</sub> compared to those for the CrkII-JNK1 interaction. These results provide molecular insight into the mechanism by which 1918 IAV NS1 hijacks CrkII and disrupts its interactions with critical cellular signaling proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28368102</PMID><DateCompleted><Year>2017</Year><Month>09</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>02</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1554-8937</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>5</Issue><PubDate><Year>2017</Year><Month>05</Month><Day>19</Day></PubDate></JournalIssue><Title>ACS chemical biology</Title><ISOAbbreviation>ACS Chem. Biol.</ISOAbbreviation></Journal><ArticleTitle>The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus.</ArticleTitle><Pagination><MedlinePgn>1199-1203</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acschembio.7b00168</ELocationID><Abstract><AbstractText>The 1918 Spanish influenza A virus (IAV) caused one of the most serious pandemics in history. The nonstructural protein 1 (NS1) of the 1918 IAV hijacks the interaction between human CrkII and JNK1. Little is, however, known about its molecular mechanism. Here, we performed X-ray crystallography, NMR relaxation dispersion experiment, and fluorescence spectroscopy to determine the structural, kinetic, and thermodynamic mechanisms underlying the hijacking of CrkII by 1918 IAV NS1. We observed that the interaction between a proline-rich motif in NS1 and the N-terminal SH3 domain of CrkII displays strikingly rapid kinetics and exceptionally high affinity with 100-fold faster k<sub>on</sub> and 3300-fold lower K<sub>d</sub> compared to those for the CrkII-JNK1 interaction. These results provide molecular insight into the mechanism by which 1918 IAV NS1 hijacks CrkII and disrupts its interactions with critical cellular signaling proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Qingliang</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zeng</LastName><ForeName>Danyun</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Baoyu</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhatt</LastName><ForeName>Veer S</ForeName><Initials>VS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Pingwei</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Jae-Hyun</ForeName><Initials>JH</Initials><Identifier Source="ORCID">0000-0002-6190-6151</Identifier><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University , College Station, Texas 77843, United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>ACS Chem Biol</MedlineTA><NlmUniqueID>101282906</NlmUniqueID><ISSNLinking>1554-8929</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C085820">INS1 protein, influenza virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050737">Proto-Oncogene Proteins c-crk</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053118" MajorTopicYN="N">Influenza A Virus, H1N1 Subtype</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064149" MajorTopicYN="N">Influenza Pandemic, 1918-1919</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050737" MajorTopicYN="N">Proto-Oncogene Proteins c-crk</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018909" MajorTopicYN="N">src Homology Domains</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>9</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28368102</ArticleId><ArticleId IdType="doi">10.1021/acschembio.7b00168</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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