Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction.
Identifieur interne : 001820 ( Ncbi/Merge ); précédent : 001819; suivant : 001821Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction.
Auteurs : Xiaoyu Xue [République populaire de Chine] ; Haitao Yang ; Wei Shen ; Qi Zhao ; Jun Li ; Kailin Yang ; Cheng Chen ; Yinghua Jin ; Mark Bartlam ; Zihe RaoSource :
- Journal of molecular biology [ 0022-2836 ] ; 2007.
Descripteurs français
- KwdFr :
- Calbindines, Endopeptidases (métabolisme), Expression des gènes, Glutathione transferase (métabolisme), Protéine G liant le calcium S100 (isolement et purification), Protéines de fusion recombinantes (métabolisme), Protéines de la matrice virale (), Protéines de la matrice virale (antagonistes et inhibiteurs), Protéines de la matrice virale (biosynthèse), Protéines de la matrice virale (métabolisme), Protéines virales (biosynthèse), Vecteurs génétiques, Virus du SRAS.
- MESH :
- antagonistes et inhibiteurs : Protéines de la matrice virale.
- biosynthèse : Protéines de la matrice virale, Protéines virales.
- isolement et purification : Protéine G liant le calcium S100.
- métabolisme : Endopeptidases, Glutathione transferase, Protéines de fusion recombinantes, Protéines de la matrice virale.
- Calbindines, Expression des gènes, Protéines de la matrice virale, Vecteurs génétiques, Virus du SRAS.
English descriptors
- KwdEn :
- Calbindins, Endopeptidases (metabolism), Gene Expression, Genetic Vectors, Glutathione Transferase (metabolism), Recombinant Fusion Proteins (metabolism), S100 Calcium Binding Protein G (isolation & purification), SARS Virus, Viral Matrix Proteins (antagonists & inhibitors), Viral Matrix Proteins (biosynthesis), Viral Matrix Proteins (chemistry), Viral Matrix Proteins (metabolism), Viral Proteins (biosynthesis).
- MESH :
- chemical , antagonists & inhibitors : Viral Matrix Proteins.
- chemical , biosynthesis : Viral Matrix Proteins, Viral Proteins.
- chemical , chemistry : Viral Matrix Proteins.
- chemical , isolation & purification : S100 Calcium Binding Protein G.
- chemical , metabolism : Endopeptidases, Glutathione Transferase, Recombinant Fusion Proteins, Viral Matrix Proteins.
- chemical : Calbindins.
- Gene Expression, Genetic Vectors, SARS Virus.
Abstract
The viral proteases have proven to be the most selective and useful for removing the fusion tags in fusion protein expression systems. As a key enzyme in the viral life-cycle, the main protease (M(pro)) is most attractive for drug design targeting the SARS coronavirus (SARS-CoV), the etiological agent responsible for the outbreak of severe acute respiratory syndrome (SARS) in 2003. In this study, SARS-CoV M(pro) was used to specifically remove the GST tag in a new fusion protein expression system. We report a new method to produce wild-type (WT) SARS-CoV M(pro) with authentic N and C termini, and compare the activity of WT protease with those of three different types of SARS-CoV M(pro) with additional residues at the N or C terminus. Our results show that additional residues at the N terminus, but not at the C terminus, of M(pro) are detrimental to enzyme activity. To explain this, the crystal structures of WT SARS-CoV M(pro) and its complex with a Michael acceptor inhibitor were determined to 1.6 Angstroms and 1.95 Angstroms resolution respectively. These crystal structures reveal that the first residue of this protease is important for sustaining the substrate-binding pocket and inhibitor binding. This study suggests that SARS-CoV M(pro) could serve as a new tag-cleavage endopeptidase for protein overproduction, and the WT SARS-CoV M(pro) is more appropriate for mechanistic characterization and inhibitor design.
DOI: 10.1016/j.jmb.2006.11.073
PubMed: 17189639
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pubmed:17189639Le document en format XML
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type="abstract" xml:lang="en">The viral proteases have proven to be the most selective and useful for removing the fusion tags in fusion protein expression systems. As a key enzyme in the viral life-cycle, the main protease (M(pro)) is most attractive for drug design targeting the SARS coronavirus (SARS-CoV), the etiological agent responsible for the outbreak of severe acute respiratory syndrome (SARS) in 2003. In this study, SARS-CoV M(pro) was used to specifically remove the GST tag in a new fusion protein expression system. We report a new method to produce wild-type (WT) SARS-CoV M(pro) with authentic N and C termini, and compare the activity of WT protease with those of three different types of SARS-CoV M(pro) with additional residues at the N or C terminus. Our results show that additional residues at the N terminus, but not at the C terminus, of M(pro) are detrimental to enzyme activity. To explain this, the crystal structures of WT SARS-CoV M(pro) and its complex with a Michael acceptor inhibitor were determined to 1.6 Angstroms and 1.95 Angstroms resolution respectively. These crystal structures reveal that the first residue of this protease is important for sustaining the substrate-binding pocket and inhibitor binding. This study suggests that SARS-CoV M(pro) could serve as a new tag-cleavage endopeptidase for protein overproduction, and the WT SARS-CoV M(pro) is more appropriate for mechanistic characterization and inhibitor design.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17189639</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>366</Volume><Issue>3</Issue><PubDate><Year>2007</Year><Month>Feb</Month><Day>23</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J. Mol. Biol.</ISOAbbreviation></Journal><ArticleTitle>Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction.</ArticleTitle><Pagination><MedlinePgn>965-75</MedlinePgn></Pagination><Abstract><AbstractText>The viral proteases have proven to be the most selective and useful for removing the fusion tags in fusion protein expression systems. As a key enzyme in the viral life-cycle, the main protease (M(pro)) is most attractive for drug design targeting the SARS coronavirus (SARS-CoV), the etiological agent responsible for the outbreak of severe acute respiratory syndrome (SARS) in 2003. In this study, SARS-CoV M(pro) was used to specifically remove the GST tag in a new fusion protein expression system. We report a new method to produce wild-type (WT) SARS-CoV M(pro) with authentic N and C termini, and compare the activity of WT protease with those of three different types of SARS-CoV M(pro) with additional residues at the N or C terminus. Our results show that additional residues at the N terminus, but not at the C terminus, of M(pro) are detrimental to enzyme activity. To explain this, the crystal structures of WT SARS-CoV M(pro) and its complex with a Michael acceptor inhibitor were determined to 1.6 Angstroms and 1.95 Angstroms resolution respectively. These crystal structures reveal that the first residue of this protease is important for sustaining the substrate-binding pocket and inhibitor binding. This study suggests that SARS-CoV M(pro) could serve as a new tag-cleavage endopeptidase for protein overproduction, and the WT SARS-CoV M(pro) is more appropriate for mechanistic characterization and inhibitor design.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Xue</LastName><ForeName>Xiaoyu</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Tsinghua-Nankai-IBP Joint Research Group for Structural Biology, Tsinghua University, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Haitao</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Wei</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Zhao</LastName><ForeName>Qi</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Jun</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Kailin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Cheng</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Yinghua</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Bartlam</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Rao</LastName><ForeName>Zihe</ForeName><Initials>Z</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2HOB</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>12</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064026">Calbindins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064030">S100 Calcium Binding Protein G</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>108502-71-2</RegistryNumber><NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D064026" MajorTopicYN="N">Calbindins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005822" MajorTopicYN="N">Genetic Vectors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064030" MajorTopicYN="N">S100 Calcium Binding Protein G</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014763" MajorTopicYN="N">Viral Matrix Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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IdType="doi">10.1016/j.jmb.2006.11.073</ArticleId><ArticleId IdType="pmc">PMC7094453</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Biochemistry. 1984 Feb 14;23(4):644-50</Citation><ArticleIdList><ArticleId IdType="pubmed">6370301</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell. 1994 Jun 3;77(5):761-71</Citation><ArticleIdList><ArticleId IdType="pubmed">7515772</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Chem Biol. 2004 Oct;11(10):1445-53</Citation><ArticleIdList><ArticleId IdType="pubmed">15489171</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2002 Nov 1;277(44):41954-9</Citation><ArticleIdList><ArticleId IdType="pubmed">12176979</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation><ArticleIdList><ArticleId IdType="pubmed">12690091</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2004 Sep 10;574(1-3):131-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15358553</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biotechnology (N Y). 1994 Jun;12(6):601-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7764949</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2003 Nov 11;100(23):13190-5</Citation><ArticleIdList><ArticleId IdType="pubmed">14585926</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11000-7</Citation><ArticleIdList><ArticleId IdType="pubmed">10500114</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Apr 20;43(15):4568-74</Citation><ArticleIdList><ArticleId IdType="pubmed">15078103</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Biochem. 1985 Sep 2;151(2):217-24</Citation><ArticleIdList><ArticleId IdType="pubmed">2863141</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):392-7</Citation><ArticleIdList><ArticleId IdType="pubmed">11856823</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Lancet. 2003 Jul 26;362(9380):263-70</Citation><ArticleIdList><ArticleId IdType="pubmed">12892955</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2005 Jan 7;280(1):164-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15507456</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2004 Jan 16;279(3):1637-42</Citation><ArticleIdList><ArticleId IdType="pubmed">14561748</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Comp Neurol. 1997 Nov 10;388(1):64-88</Citation><ArticleIdList><ArticleId IdType="pubmed">9364239</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation><ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Biochem. 1981 Apr;115(3):491-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7238516</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 May 4;43(17):4906-12</Citation><ArticleIdList><ArticleId IdType="pubmed">15109248</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Curr Top Microbiol Immunol. 2005;287:57-94</Citation><ArticleIdList><ArticleId IdType="pubmed">15609509</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Nov 30;43(47):14958-70</Citation><ArticleIdList><ArticleId IdType="pubmed">15554703</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 2003 Jun 13;300(5626):1763-7</Citation><ArticleIdList><ArticleId IdType="pubmed">12746549</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Eng. 2001 Dec;14(12):993-1000</Citation><ArticleIdList><ArticleId IdType="pubmed">11809930</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Struct Biol. 2000 Nov;7 Suppl:970-2</Citation><ArticleIdList><ArticleId IdType="pubmed">11104003</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Gene. 1988 Jul 15;67(1):31-40</Citation><ArticleIdList><ArticleId IdType="pubmed">3047011</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2005 Jun 17;280(24):22741-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15831489</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 2003 May 15;423(6937):240</Citation><ArticleIdList><ArticleId IdType="pubmed">12748632</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2005 Nov 18;354(1):25-40</Citation><ArticleIdList><ArticleId IdType="pubmed">16242152</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Nov 1;61(Pt 11):964-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16511208</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2004 Oct 22;576(3):325-30</Citation><ArticleIdList><ArticleId IdType="pubmed">15498556</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>PLoS Biol. 2005 Oct;3(10):e324</Citation><ArticleIdList><ArticleId IdType="pubmed">16128623</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Expr Purif. 2002 Jun;25(1):8-15</Citation><ArticleIdList><ArticleId IdType="pubmed">12071693</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Neurochem. 1995 Jul;65(1):381-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7790883</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Chem Neuroanat. 1997 Dec;14(1):51-61</Citation><ArticleIdList><ArticleId IdType="pubmed">9498166</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2005 Sep 2;280(35):31257-66</Citation><ArticleIdList><ArticleId IdType="pubmed">15788388</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 1967 Apr 20;27(2):157-62</Citation><ArticleIdList><ArticleId IdType="pubmed">6035483</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation><ArticleIdList><ArticleId IdType="pubmed">12711465</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Anal Biochem. 1997 Oct 15;252(2):238-45</Citation><ArticleIdList><ArticleId IdType="pubmed">9344409</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2005 Nov 11;353(5):1137-51</Citation><ArticleIdList><ArticleId IdType="pubmed">16219322</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Bartlam, Mark" sort="Bartlam, Mark" uniqKey="Bartlam M" first="Mark" last="Bartlam">Mark Bartlam</name><name sortKey="Chen, Cheng" sort="Chen, Cheng" uniqKey="Chen C" first="Cheng" last="Chen">Cheng Chen</name><name sortKey="Jin, Yinghua" sort="Jin, Yinghua" uniqKey="Jin Y" first="Yinghua" last="Jin">Yinghua Jin</name><name sortKey="Li, Jun" sort="Li, Jun" uniqKey="Li J" first="Jun" last="Li">Jun Li</name><name sortKey="Rao, Zihe" sort="Rao, Zihe" uniqKey="Rao Z" first="Zihe" last="Rao">Zihe Rao</name><name sortKey="Shen, Wei" sort="Shen, Wei" uniqKey="Shen W" first="Wei" last="Shen">Wei Shen</name><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name><name sortKey="Yang, Kailin" sort="Yang, Kailin" uniqKey="Yang K" first="Kailin" last="Yang">Kailin Yang</name><name sortKey="Zhao, Qi" sort="Zhao, Qi" uniqKey="Zhao Q" first="Qi" last="Zhao">Qi Zhao</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Xue, Xiaoyu" sort="Xue, Xiaoyu" uniqKey="Xue X" first="Xiaoyu" last="Xue">Xiaoyu Xue</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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