Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.
Identifieur interne : 000999 ( PubMed/Corpus ); précédent : 000998; suivant : 000A00Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.
Auteurs : Si Min Zhang ; Ying Liao ; Tuan Ling Neo ; Yanning Lu ; Ding Xiang Liu ; Anders Vahlne ; James P. TamSource :
- The international journal of biochemistry & cell biology [ 1878-5875 ] ; 2018.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amyloidogenic Proteins (chemistry), Amyloidogenic Proteins (genetics), Amyloidogenic Proteins (metabolism), Animals, Gene Expression, HEK293 Cells, Hemagglutinins (genetics), Hemagglutinins (metabolism), Humans, Peptide Library, Peptides (chemical synthesis), Peptides (metabolism), Protein Binding, Protein Structure, Secondary, Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (chemistry), Sf9 Cells, Solid-Phase Synthesis Techniques, Spike Glycoprotein, Coronavirus (chemistry), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Spodoptera.
- MESH :
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Amyloidogenic Proteins, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemical , genetics : Amyloidogenic Proteins, Hemagglutinins, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemical , metabolism : Amyloidogenic Proteins, Hemagglutinins, Peptides, Recombinant Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- Amino Acid Sequence, Animals, Gene Expression, HEK293 Cells, Humans, Peptide Library, Protein Binding, Protein Structure, Secondary, Sf9 Cells, Solid-Phase Synthesis Techniques, Spodoptera.
Abstract
Self-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-β spine steric zippers within the amyloid-like fibrils, could bind to the protein-of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportunities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding β-zipper-forming peptide within the severe acute respiratory syndrome-associated coronavirus spike (S) protein and its application in viral detection. Peptide array scanning of overlapping peptides covering the entire length of S protein identified 34 putative self-binding peptides of six clusters, five of which contained octapeptide core consensus sequences. The Cluster I consensus octapeptide sequence GINITNFR was predicted by the Eisenberg's 3D profile method to have high amyloid-like fibrillation potential through steric β-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomerize and form amyloid-like fibrils. Taking advantage of this, C6 was further applied to detect the S protein expression in vitro by fluorescence staining. Meanwhile, the coiled-coil-forming Leu/Ile heptad repeat sequences within the S protein were under-represented during peptide array scanning, in agreement with that long peptide lengths were required to attain high helix-mediated interaction avidity. The data suggest that short β-zipper-like self-binding peptides within the S protein could be identified through combining the peptide scanning and predictive methods, and could be exploited as biochemical detection reagents for viral infection.
DOI: 10.1016/j.biocel.2018.05.012
PubMed: 29800727
Links to Exploration step
pubmed:29800727Le document en format XML
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Tam</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. 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Tam</name><affiliation><nlm:affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. Electronic address: jptam@ntu.edu.sg.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The international journal of biochemistry & cell biology</title><idno type="eISSN">1878-5875</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>Amyloidogenic Proteins (chemistry)</term><term>Amyloidogenic Proteins (genetics)</term><term>Amyloidogenic Proteins (metabolism)</term><term>Animals</term><term>Gene Expression</term><term>HEK293 Cells</term><term>Hemagglutinins (genetics)</term><term>Hemagglutinins (metabolism)</term><term>Humans</term><term>Peptide Library</term><term>Peptides (chemical synthesis)</term><term>Peptides (metabolism)</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>SARS Virus (chemistry)</term><term>Sf9 Cells</term><term>Solid-Phase Synthesis Techniques</term><term>Spike Glycoprotein, Coronavirus (chemistry)</term><term>Spike Glycoprotein, Coronavirus (genetics)</term><term>Spike Glycoprotein, Coronavirus (metabolism)</term><term>Spodoptera</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Hemagglutinins</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloidogenic Proteins</term><term>Hemagglutinins</term><term>Peptides</term><term>Recombinant Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Gene Expression</term><term>HEK293 Cells</term><term>Humans</term><term>Peptide Library</term><term>Protein Binding</term><term>Protein Structure, Secondary</term><term>Sf9 Cells</term><term>Solid-Phase Synthesis Techniques</term><term>Spodoptera</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Self-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-β spine steric zippers within the amyloid-like fibrils, could bind to the protein-of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportunities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding β-zipper-forming peptide within the severe acute respiratory syndrome-associated coronavirus spike (S) protein and its application in viral detection. Peptide array scanning of overlapping peptides covering the entire length of S protein identified 34 putative self-binding peptides of six clusters, five of which contained octapeptide core consensus sequences. The Cluster I consensus octapeptide sequence GINITNFR was predicted by the Eisenberg's 3D profile method to have high amyloid-like fibrillation potential through steric β-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomerize and form amyloid-like fibrils. Taking advantage of this, C6 was further applied to detect the S protein expression in vitro by fluorescence staining. Meanwhile, the coiled-coil-forming Leu/Ile heptad repeat sequences within the S protein were under-represented during peptide array scanning, in agreement with that long peptide lengths were required to attain high helix-mediated interaction avidity. The data suggest that short β-zipper-like self-binding peptides within the S protein could be identified through combining the peptide scanning and predictive methods, and could be exploited as biochemical detection reagents for viral infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29800727</PMID><DateCompleted><Year>2019</Year><Month>03</Month><Day>28</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1878-5875</ISSN><JournalIssue CitedMedium="Internet"><Volume>101</Volume><PubDate><Year>2018</Year><Month>08</Month></PubDate></JournalIssue><Title>The international journal of biochemistry & cell biology</Title><ISOAbbreviation>Int. J. Biochem. Cell Biol.</ISOAbbreviation></Journal><ArticleTitle>Identification and application of self-binding zipper-like sequences in SARS-CoV spike protein.</ArticleTitle><Pagination><MedlinePgn>103-112</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1357-2725(18)30124-9</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.biocel.2018.05.012</ELocationID><Abstract><AbstractText>Self-binding peptides containing zipper-like sequences, such as the Leu/Ile zipper sequence within the coiled coil regions of proteins and the cross-β spine steric zippers within the amyloid-like fibrils, could bind to the protein-of-origin through homophilic sequence-specific zipper motifs. These self-binding sequences represent opportunities for the development of biochemical tools and/or therapeutics. Here, we report on the identification of a putative self-binding β-zipper-forming peptide within the severe acute respiratory syndrome-associated coronavirus spike (S) protein and its application in viral detection. Peptide array scanning of overlapping peptides covering the entire length of S protein identified 34 putative self-binding peptides of six clusters, five of which contained octapeptide core consensus sequences. The Cluster I consensus octapeptide sequence GINITNFR was predicted by the Eisenberg's 3D profile method to have high amyloid-like fibrillation potential through steric β-zipper formation. Peptide C6 containing the Cluster I consensus sequence was shown to oligomerize and form amyloid-like fibrils. Taking advantage of this, C6 was further applied to detect the S protein expression in vitro by fluorescence staining. Meanwhile, the coiled-coil-forming Leu/Ile heptad repeat sequences within the S protein were under-represented during peptide array scanning, in agreement with that long peptide lengths were required to attain high helix-mediated interaction avidity. The data suggest that short β-zipper-like self-binding peptides within the S protein could be identified through combining the peptide scanning and predictive methods, and could be exploited as biochemical detection reagents for viral infection.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Si Min</ForeName><Initials>SM</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore; Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liao</LastName><ForeName>Ying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Neo</LastName><ForeName>Tuan Ling</ForeName><Initials>TL</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Yanning</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Ding Xiang</ForeName><Initials>DX</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vahlne</LastName><ForeName>Anders</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Division of Clinical Microbiology, Department of Laboratory Medicine, Karolinska Institutet, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tam</LastName><ForeName>James P</ForeName><Initials>JP</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, Singapore. Electronic address: jptam@ntu.edu.sg.</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>2018</Year><Month>05</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Int J Biochem Cell Biol</MedlineTA><NlmUniqueID>9508482</NlmUniqueID><ISSNLinking>1357-2725</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D058227">Amyloidogenic Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006388">Hemagglutinins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019151">Peptide Library</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D058227" MajorTopicYN="N">Amyloidogenic Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006388" MajorTopicYN="N">Hemagglutinins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019151" MajorTopicYN="N">Peptide Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D061987" MajorTopicYN="N">Sf9 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D060327" MajorTopicYN="N">Solid-Phase Synthesis Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018411" MajorTopicYN="N">Spodoptera</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Class I viral fusion glycoprotein</Keyword><Keyword MajorTopicYN="Y">SARS-CoV spike protein</Keyword><Keyword MajorTopicYN="Y">Steric β-zipper</Keyword><Keyword MajorTopicYN="Y">self-binding peptides</Keyword><Keyword MajorTopicYN="Y">viral detection</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>12</Month><Day>07</Day></PubMedPubDate><PubMedPubDate 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IdType="pubmed">14760722</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2005 Jul 22;333(1):186-93</Citation><ArticleIdList><ArticleId IdType="pubmed">15939399</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2375-80</Citation><ArticleIdList><ArticleId IdType="pubmed">11226247</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2003 Oct 10;310(1):78-83</Citation><ArticleIdList><ArticleId IdType="pubmed">14511651</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2006 Mar 14;103(11):4074-8</Citation><ArticleIdList><ArticleId IdType="pubmed">16537487</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83</Citation><ArticleIdList><ArticleId IdType="pubmed">11331745</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Clin Microbiol. 2004 Jul;42(7):3196-206</Citation><ArticleIdList><ArticleId IdType="pubmed">15243082</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>AIDS. 2013 Apr 24;27(7):1081-90</Citation><ArticleIdList><ArticleId IdType="pubmed">23324659</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Science. 1991 Jul 12;253(5016):164-70</Citation><ArticleIdList><ArticleId IdType="pubmed">1853201</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochim Biophys Acta. 2010 Jul;1804(7):1405-12</Citation><ArticleIdList><ArticleId IdType="pubmed">20399286</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2005 Mar;79(5):2678-88</Citation><ArticleIdList><ArticleId IdType="pubmed">15708987</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Eur J Biochem. 2002 Feb;269(3):923-32</Citation><ArticleIdList><ArticleId IdType="pubmed">11846794</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 1999 Jul;73(7):5945-56</Citation><ArticleIdList><ArticleId IdType="pubmed">10364347</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2000 Jan 28;295(4):1055-71</Citation><ArticleIdList><ArticleId IdType="pubmed">10656810</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Sci. 2011 Dec;20(12):2125-9</Citation><ArticleIdList><ArticleId IdType="pubmed">21922588</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Cell Mol Life Sci. 2004 Oct;61(19-20):2428-30</Citation><ArticleIdList><ArticleId IdType="pubmed">15526150</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63</Citation><ArticleIdList><ArticleId IdType="pubmed">15604146</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2000 May 9;97(10):5129-34</Citation><ArticleIdList><ArticleId IdType="pubmed">10805776</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 2007 May 24;447(7143):453-7</Citation><ArticleIdList><ArticleId IdType="pubmed">17468747</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>PLoS One. 2015 Jul 31;10(7):e0134851</Citation><ArticleIdList><ArticleId IdType="pubmed">26230322</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nature. 2005 Jun 9;435(7043):773-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15944695</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Pept Res. 1995 Nov-Dec;8(6):345-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8838418</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Adv Protein Chem. 2005;70:11-35</Citation><ArticleIdList><ArticleId IdType="pubmed">15837512</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15748-53</Citation><ArticleIdList><ArticleId IdType="pubmed">15496474</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2005 Mar 25;280(12):11259-73</Citation><ArticleIdList><ArticleId IdType="pubmed">15640162</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Infect Dis. 2005 Feb 15;191(4):507-14</Citation><ArticleIdList><ArticleId IdType="pubmed">15655773</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2006 Jun;80(12):5757-67</Citation><ArticleIdList><ArticleId IdType="pubmed">16731915</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9770-4</Citation><ArticleIdList><ArticleId IdType="pubmed">7937889</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 1996 Sep 1;223(1):103-12</Citation><ArticleIdList><ArticleId IdType="pubmed">8806544</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>FEBS Lett. 2004 Oct 8;576(1-2):174-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15474033</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proteins. 1995 Jun;22(2):119-31</Citation><ArticleIdList><ArticleId IdType="pubmed">7567960</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Immunol Methods. 2002 Sep 1;267(1):13-26</Citation><ArticleIdList><ArticleId IdType="pubmed">12135797</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Sci. 1994 Oct;3(10):1629-37</Citation><ArticleIdList><ArticleId IdType="pubmed">7849580</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2008 Jul 4;371(3):356-60</Citation><ArticleIdList><ArticleId IdType="pubmed">18424264</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3487-92</Citation><ArticleIdList><ArticleId IdType="pubmed">20133726</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods Mol Biol. 1996;66:149-69</Citation><ArticleIdList><ArticleId IdType="pubmed">8959713</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Protein Eng Des Sel. 2009 Aug;22(8):531-6</Citation><ArticleIdList><ArticleId IdType="pubmed">19602569</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Curr Pharm Des. 2008;14(24):2428-38</Citation><ArticleIdList><ArticleId IdType="pubmed">18781992</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Antivir Ther. 2005;10(5):671-80</Citation><ArticleIdList><ArticleId IdType="pubmed">16152761</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochim Biophys Acta. 2014 Sep;1844(9):1675-83</Citation><ArticleIdList><ArticleId IdType="pubmed">24981796</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Lancet. 2004 Mar 20;363(9413):938-47</Citation><ArticleIdList><ArticleId IdType="pubmed">15043961</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Immunol. 2004 Sep 15;173(6):4050-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15356154</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1988 Aug;85(15):5409-13</Citation><ArticleIdList><ArticleId IdType="pubmed">3399498</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2008 Aug 5;47(31):8214-24</Citation><ArticleIdList><ArticleId IdType="pubmed">18616295</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Mol Biol. 2012 Aug 24;421(4-5):441-65</Citation><ArticleIdList><ArticleId IdType="pubmed">22244855</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2001 Sep 7;276(36):34156-61</Citation><ArticleIdList><ArticleId IdType="pubmed">11445568</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2000 Nov 14;39(45):13748-59</Citation><ArticleIdList><ArticleId IdType="pubmed">11076514</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochem Biophys Res Commun. 2008 May 2;369(2):344-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18279660</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Immunol. 2005 Apr 15;174(8):4908-15</Citation><ArticleIdList><ArticleId IdType="pubmed">15814718</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2002 Sep 20;277(38):35475-80</Citation><ArticleIdList><ArticleId IdType="pubmed">12095997</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2015 Mar 10;54(9):1819-30</Citation><ArticleIdList><ArticleId IdType="pubmed">25668103</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2003 Oct;77(20):10910-6</Citation><ArticleIdList><ArticleId IdType="pubmed">14512541</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Virology. 2011 Jul 20;416(1-2):65-74</Citation><ArticleIdList><ArticleId IdType="pubmed">21601229</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Biol Chem. 2006 Apr 28;281(17):11965-71</Citation><ArticleIdList><ArticleId IdType="pubmed">16507566</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation><ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Nat Chem. 2013 Mar;5(3):161-73</Citation><ArticleIdList><ArticleId IdType="pubmed">23422557</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Biochemistry. 2004 Nov 9;43(44):14064-71</Citation><ArticleIdList><ArticleId IdType="pubmed">15518555</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>Methods. 2004 Sep;34(1):151-60</Citation><ArticleIdList><ArticleId IdType="pubmed">15283924</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>BMC Biochem. 2007 Apr 12;8:6</Citation><ArticleIdList><ArticleId IdType="pubmed">17430579</ArticleId></ArticleIdList></Reference></ReferenceList><ReferenceList><Reference><Citation>J Virol. 2002 Sep;76(18):9079-86</Citation><ArticleIdList><ArticleId 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