SrasV1, PascalFrancis, Corpus, bibRecord, 000174

RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein

Identifieur interne : 000174 ( PascalFrancis/Corpus ); précédent : 000173; suivant : 000175

RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein

Auteurs : Dae-Gyun Ahn ; Il-Ji Jeon ; JUNG DONG KIM ; Min-Sun Song ; Seung-Ryul Han ; Seong-Wook Lee ; Hyungil Jung ; Jong-Won Oh

Source :

Analyst : (London. 1877. Print) [ 0003-2654 ] ; 2009.

RBID : Pascal:09-0485565

Descripteurs français

Pascal (Inist)
- Marqueur, Enrichissement chimique, Constante dissociation, Mobilité électrophorétique, Analyse chimique, Chimiluminescence, Composé ultratrace, Méthode immunologique, Protéine, Anticorps.

English descriptors

KwdEn :
- Antibody, Chemical analysis, Chemical enrichment, Chemiluminescence, Dissociation constant, Electrophoretic mobility, Immunological method, Marker, Protein, Ultratrace compound.

Abstract

Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A11	`04`	`1`		`@1 SONG (Min-Sun)`
A11	`05`	`1`		`@1 HAN (Seung-Ryul)`
A11	`06`	`1`		`@1 LEE (Seong-Wook)`
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C01	`01`		`ENG`	@0 Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.
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Format Inist (serveur)

NO :	PASCAL 09-0485565 INIST
ET :	RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein
AU :	AHN (Dae-Gyun); JEON (Il-Ji); JUNG DONG KIM; SONG (Min-Sun); HAN (Seung-Ryul); LEE (Seong-Wook); JUNG (Hyungil); OH (Jong-Won)
AF :	Department of Biotechnology, Yonsei University/Seoul 120-749/Corée, République de (1 aut., 2 aut., 3 aut., 7 aut., 8 aut.); Department of Molecular Biology, Dankook University/448-701/Corée, République de (4 aut., 5 aut., 6 aut.)
DT :	Publication en série; Niveau analytique
SO :	Analyst : (London. 1877. Print); ISSN 0003-2654; Coden ANALAO; Royaume-Uni; Da. 2009; Vol. 134; No. 9; Pp. 1896-1901; Bibl. 30 ref.
LA :	Anglais
EA :	Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.
CC :	001C04F; 001C04G
FD :	Marqueur; Enrichissement chimique; Constante dissociation; Mobilité électrophorétique; Analyse chimique; Chimiluminescence; Composé ultratrace; Méthode immunologique; Protéine; Anticorps
ED :	Marker; Chemical enrichment; Dissociation constant; Electrophoretic mobility; Chemical analysis; Chemiluminescence; Ultratrace compound; Immunological method; Protein; Antibody
SD :	Marcador; Enriquecimiento químico; Constante disociación; Movilidad electroforética; Análisis químico; Quimioluminiscencia; Compuesto ultrahuella; Método inmunológico; Proteína; Anticuerpo
LO :	INIST-1036.354000196204190230
ID :	09-0485565

Links to Exploration step

Pascal:09-0485565

Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.</div>
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<fC01 i1="01" l="ENG"><s0>Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>001C04F</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>001C04G</s0>
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<fC03 i1="01" i2="X" l="FRE"><s0>Marqueur</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Marker</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Marcador</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Enrichissement chimique</s0>
<s5>02</s5>
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<s5>02</s5>
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<s5>02</s5>
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<s5>03</s5>
</fC03>
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<s5>03</s5>
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<s5>03</s5>
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<s5>04</s5>
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<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Movilidad electroforética</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Analyse chimique</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Chemical analysis</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Análisis químico</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Chimiluminescence</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Chemiluminescence</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Quimioluminiscencia</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Composé ultratrace</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Ultratrace compound</s0>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Compuesto ultrahuella</s0>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Méthode immunologique</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Immunological method</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Método inmunológico</s0>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Protéine</s0>
<s5>15</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Protein</s0>
<s5>15</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Proteína</s0>
<s5>15</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Anticorps</s0>
<s5>16</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Antibody</s0>
<s5>16</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Anticuerpo</s0>
<s5>16</s5>
</fC03>
<fN21><s1>348</s1>
</fN21>
<fN44 i1="01"><s1>OTO</s1>
</fN44>
<fN82><s1>OTO</s1>
</fN82>
</pA>
</standard>
<server><NO>PASCAL 09-0485565 INIST</NO>
<ET>RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein</ET>
<AU>AHN (Dae-Gyun); JEON (Il-Ji); JUNG DONG KIM; SONG (Min-Sun); HAN (Seung-Ryul); LEE (Seong-Wook); JUNG (Hyungil); OH (Jong-Won)</AU>
<AF>Department of Biotechnology, Yonsei University/Seoul 120-749/Corée, République de (1 aut., 2 aut., 3 aut., 7 aut., 8 aut.); Department of Molecular Biology, Dankook University/448-701/Corée, République de (4 aut., 5 aut., 6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Analyst : (London. 1877. Print); ISSN 0003-2654; Coden ANALAO; Royaume-Uni; Da. 2009; Vol. 134; No. 9; Pp. 1896-1901; Bibl. 30 ref.</SO>
<LA>Anglais</LA>
<EA>Severe acute respiratory syndrome coronavirus (SARS-CoV) is the etiological agent of a newly emerged disease SARS. The SARS-CoV nucleocapsid (N) protein is one of the most abundant structural proteins and serves as a diagnostic marker for accurate and sensitive detection of the virus. Using a SELEX (systematic evolution of ligand by exponential enrichment) procedure and recombinant N protein, we selected a high-affinity RNA aptamer capable of binding to N protein with a dissociation constant of 1.65 nM. Electrophoretic mobility shift assays and RNA competition experiments showed that the selected aptamer recognized selectively the C-terminal region of N protein with high specificity. Using a chemiluminescence immunosorbent assay and a nanoarray aptamer chip with the selected aptamer as an antigen-capturing agent, we could sensitively detect N protein at a concentration as low as 2 pg/ml. These aptamer-antibody hybrid immunoassays may be useful for rapid, sensitive detection of SARS-CoV N protein.</EA>
<CC>001C04F; 001C04G</CC>
<FD>Marqueur; Enrichissement chimique; Constante dissociation; Mobilité électrophorétique; Analyse chimique; Chimiluminescence; Composé ultratrace; Méthode immunologique; Protéine; Anticorps</FD>
<ED>Marker; Chemical enrichment; Dissociation constant; Electrophoretic mobility; Chemical analysis; Chemiluminescence; Ultratrace compound; Immunological method; Protein; Antibody</ED>
<SD>Marcador; Enriquecimiento químico; Constante disociación; Movilidad electroforética; Análisis químico; Quimioluminiscencia; Compuesto ultrahuella; Método inmunológico; Proteína; Anticuerpo</SD>
<LO>INIST-1036.354000196204190230</LO>
<ID>09-0485565</ID>
</server>
</inist>
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RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein

RNA aptamer-based sensitive detection of SARS coronavirus nucleocapsid protein

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