mRNA display design of fibronectin-based intrabodies that detect and inhibit severe acute respiratory syndrome coronavirus nucleocapsid protein.
Identifieur interne : 001928 ( PubMed/Curation ); précédent : 001927; suivant : 001929mRNA display design of fibronectin-based intrabodies that detect and inhibit severe acute respiratory syndrome coronavirus nucleocapsid protein.
Auteurs : Hsiang-I Liao [États-Unis] ; C Anders Olson ; Seungmin Hwang ; Hongyu Deng ; Elaine Wong ; Ralph S. Baric ; Richard W. Roberts ; Ren SunSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Analyse de profil d'expression de gènes, Animaux, Anticorps monoclonaux (génétique), Anticorps monoclonaux (immunologie), Banque de peptides, Cellules Vero, Cellules cultivées, Données de séquences moléculaires, Fibronectines (génétique), Fibronectines (immunologie), Fibronectines (métabolisme), Humains, Immunoprécipitation, Protéines nucléocapside (antagonistes et inhibiteurs), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), RT-PCR, Rein (cytologie), Rein (métabolisme), Réplication virale, Similitude de séquences d'acides aminés, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Technique d'immunofluorescence, Virus du SRAS (physiologie).
- MESH :
- antagonistes et inhibiteurs : Protéines nucléocapside.
- cytologie : Rein.
- génétique : ARN messager, Anticorps monoclonaux, Fibronectines, Protéines nucléocapside.
- immunologie : Anticorps monoclonaux, Fibronectines.
- métabolisme : ARN messager, Fibronectines, Protéines nucléocapside, Rein.
- physiologie : Virus du SRAS.
- Analyse de profil d'expression de gènes, Animaux, Banque de peptides, Cellules Vero, Cellules cultivées, Données de séquences moléculaires, Humains, Immunoprécipitation, RT-PCR, Réplication virale, Similitude de séquences d'acides aminés, Syndrome respiratoire aigu sévère, Séquence d'acides aminés, Technique d'immunofluorescence.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (genetics), Antibodies, Monoclonal (immunology), Cells, Cultured, Chlorocebus aethiops, Fibronectins (genetics), Fibronectins (immunology), Fibronectins (metabolism), Fluorescent Antibody Technique, Gene Expression Profiling, Humans, Immunoprecipitation, Kidney (cytology), Kidney (metabolism), Molecular Sequence Data, Nucleocapsid Proteins (antagonists & inhibitors), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Peptide Library, RNA, Messenger (genetics), RNA, Messenger (metabolism), Reverse Transcriptase Polymerase Chain Reaction, SARS Virus (physiology), Sequence Homology, Amino Acid, Severe Acute Respiratory Syndrome, Vero Cells, Virus Replication.
- MESH :
- chemical , antagonists & inhibitors : Nucleocapsid Proteins.
- chemical , genetics : Antibodies, Monoclonal, Fibronectins, Nucleocapsid Proteins, RNA, Messenger.
- chemical , immunology : Antibodies, Monoclonal, Fibronectins.
- chemical , metabolism : Fibronectins, Nucleocapsid Proteins, RNA, Messenger.
- cytology : Kidney.
- metabolism : Kidney.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Cells, Cultured, Chlorocebus aethiops, Fluorescent Antibody Technique, Gene Expression Profiling, Humans, Immunoprecipitation, Molecular Sequence Data, Peptide Library, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Severe Acute Respiratory Syndrome, Vero Cells, Virus Replication.
Abstract
The nucleocapsid (N) protein of severe acute respiratory syndrome (SARS) coronavirus plays important roles in both viral replication and modulation of host cell processes. New ligands that target the N protein may thus provide tools to track the protein inside cells, detect interaction hot spots on the protein surface, and discover sites that could be used to develop new anti-SARS therapies. Using mRNA display selection and directed evolution, we designed novel antibody-like protein affinity reagents that target SARS N protein with high affinity and selectivity. Our libraries were based on an 88-residue variant of the 10th fibronectin type III domain from human fibronectin (10Fn3). This selection resulted in eight independent 10Fn3 intrabodies, two that require the N-terminal domain for binding and six that recognize the C terminus, one with Kd=1.7 nM. 10Fn3 intrabodies are well expressed in mammalian cells and are relocalized by N in SARS-infected cells. Seven of the selected intrabodies tested do not perturb cellular function when expressed singly in vivo and inhibit virus replication from 11- to 5900-fold when expressed in cells prior to infection. Targeting two sites on SARS-N simultaneously using two distinct 10Fn3s results in synergistic inhibition of virus replication.
DOI: 10.1074/jbc.M901547200
PubMed: 19364769
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(antagonists & inhibitors)</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Peptide Library</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>SARS Virus (physiology)</term><term>Sequence Homology, Amino Acid</term><term>Severe Acute Respiratory Syndrome</term><term>Vero Cells</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>ARN messager (métabolisme)</term><term>Analyse de profil d'expression de gènes</term><term>Animaux</term><term>Anticorps monoclonaux (génétique)</term><term>Anticorps monoclonaux (immunologie)</term><term>Banque de peptides</term><term>Cellules Vero</term><term>Cellules cultivées</term><term>Données de séquences moléculaires</term><term>Fibronectines (génétique)</term><term>Fibronectines (immunologie)</term><term>Fibronectines (métabolisme)</term><term>Humains</term><term>Immunoprécipitation</term><term>Protéines nucléocapside (antagonistes et inhibiteurs)</term><term>Protéines nucléocapside (génétique)</term><term>Protéines nucléocapside (métabolisme)</term><term>RT-PCR</term><term>Rein (cytologie)</term><term>Rein (métabolisme)</term><term>Réplication virale</term><term>Similitude de séquences d'acides aminés</term><term>Syndrome respiratoire aigu sévère</term><term>Séquence d'acides aminés</term><term>Technique d'immunofluorescence</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Fibronectins</term><term>Nucleocapsid Proteins</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Fibronectins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fibronectins</term><term>Nucleocapsid Proteins</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Rein</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Kidney</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term><term>Anticorps monoclonaux</term><term>Fibronectines</term><term>Protéines nucléocapside</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Fibronectines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Kidney</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Fibronectines</term><term>Protéines nucléocapside</term><term>Rein</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cells, Cultured</term><term>Chlorocebus aethiops</term><term>Fluorescent Antibody Technique</term><term>Gene Expression Profiling</term><term>Humans</term><term>Immunoprecipitation</term><term>Molecular Sequence Data</term><term>Peptide Library</term><term>Reverse Transcriptase Polymerase Chain Reaction</term><term>Sequence Homology, Amino Acid</term><term>Severe Acute Respiratory Syndrome</term><term>Vero Cells</term><term>Virus Replication</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de profil d'expression de gènes</term><term>Animaux</term><term>Banque de peptides</term><term>Cellules Vero</term><term>Cellules cultivées</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Immunoprécipitation</term><term>RT-PCR</term><term>Réplication virale</term><term>Similitude de séquences d'acides aminés</term><term>Syndrome respiratoire aigu sévère</term><term>Séquence d'acides aminés</term><term>Technique d'immunofluorescence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The nucleocapsid (N) protein of severe acute respiratory syndrome (SARS) coronavirus plays important roles in both viral replication and modulation of host cell processes. New ligands that target the N protein may thus provide tools to track the protein inside cells, detect interaction hot spots on the protein surface, and discover sites that could be used to develop new anti-SARS therapies. Using mRNA display selection and directed evolution, we designed novel antibody-like protein affinity reagents that target SARS N protein with high affinity and selectivity. Our libraries were based on an 88-residue variant of the 10th fibronectin type III domain from human fibronectin (10Fn3). This selection resulted in eight independent 10Fn3 intrabodies, two that require the N-terminal domain for binding and six that recognize the C terminus, one with Kd=1.7 nM. 10Fn3 intrabodies are well expressed in mammalian cells and are relocalized by N in SARS-infected cells. Seven of the selected intrabodies tested do not perturb cellular function when expressed singly in vivo and inhibit virus replication from 11- to 5900-fold when expressed in cells prior to infection. Targeting two sites on SARS-N simultaneously using two distinct 10Fn3s results in synergistic inhibition of virus replication.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19364769</PMID><DateCompleted><Year>2009</Year><Month>08</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>26</Issue><PubDate><Year>2009</Year><Month>Jun</Month><Day>26</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>mRNA display design of fibronectin-based intrabodies that detect and inhibit severe acute respiratory syndrome coronavirus nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>17512-20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M901547200</ELocationID><Abstract><AbstractText>The nucleocapsid (N) protein of severe acute respiratory syndrome (SARS) coronavirus plays important roles in both viral replication and modulation of host cell processes. New ligands that target the N protein may thus provide tools to track the protein inside cells, detect interaction hot spots on the protein surface, and discover sites that could be used to develop new anti-SARS therapies. Using mRNA display selection and directed evolution, we designed novel antibody-like protein affinity reagents that target SARS N protein with high affinity and selectivity. Our libraries were based on an 88-residue variant of the 10th fibronectin type III domain from human fibronectin (10Fn3). This selection resulted in eight independent 10Fn3 intrabodies, two that require the N-terminal domain for binding and six that recognize the C terminus, one with Kd=1.7 nM. 10Fn3 intrabodies are well expressed in mammalian cells and are relocalized by N in SARS-infected cells. Seven of the selected intrabodies tested do not perturb cellular function when expressed singly in vivo and inhibit virus replication from 11- to 5900-fold when expressed in cells prior to infection. Targeting two sites on SARS-N simultaneously using two distinct 10Fn3s results in synergistic inhibition of virus replication.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liao</LastName><ForeName>Hsiang-I</ForeName><Initials>HI</Initials><AffiliationInfo><Affiliation>Department of Molecular and Medical Pharmacology, California Nano System Institute, UCLA, Los Angeles, CA 90095, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Olson</LastName><ForeName>C Anders</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Seungmin</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Deng</LastName><ForeName>Hongyu</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Elaine</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Baric</LastName><ForeName>Ralph S</ForeName><Initials>RS</Initials></Author><Author ValidYN="Y"><LastName>Roberts</LastName><ForeName>Richard W</ForeName><Initials>RW</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ren</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM060416</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 GM60416</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>04</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005353">Fibronectins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019151">Peptide Library</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005353" MajorTopicYN="N">Fibronectins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005455" MajorTopicYN="N">Fluorescent Antibody Technique</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020869" MajorTopicYN="Y">Gene Expression Profiling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007668" MajorTopicYN="N">Kidney</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019590" MajorTopicYN="N">Nucleocapsid Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019151" MajorTopicYN="N">Peptide Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020133" MajorTopicYN="N">Reverse Transcriptase Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014709" 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