Investigation of interaction between two neutralizing monoclonal antibodies and SARS virus using biosensor based on imaging ellipsometry.
Identifieur interne : 001509 ( Ncbi/Curation ); précédent : 001508; suivant : 001510Investigation of interaction between two neutralizing monoclonal antibodies and SARS virus using biosensor based on imaging ellipsometry.
Auteurs : Cai Qi [République populaire de Chine] ; Jin-Zhu Duan ; Zhan-Hui Wang ; Yan-Yan Chen ; Pan-He Zhang ; Lin Zhan ; Xi-Yun Yan ; Wu-Chun Cao ; Gang JinSource :
- Biomedical microdevices [ 1387-2176 ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Antibodies, Monoclonal, Antibodies, Viral.
- chemistry : SARS Virus.
- instrumentation : Diagnostic Imaging.
- methods : Diagnostic Imaging.
- Biosensing Techniques, Humans.
Abstract
Two neutralizing human scFv, b1 and h12 were identified initially using ELISA,employing highly purified virus as the coating antigen. The biosensor technique based on imaging ellipsometry was employed directly to detect two neutralizing monoclonal antibodies and serial serum samples from 10 SARS patients and 12 volunteers who had not SARS. Further, the kinetic process of interaction between the antibodies and SARS-CoV was studied using the real-time function of the biosensor. The biosensor is consistent with ELISA that the antibody h12 showed a higher affinity in encountering the virus than antibody b1. The affinity of antibody b1 and antibody h12 was 9.5 x 10(6) M(-1) and 1.36 x 10(7) M(- 1), respectively. As a label free method, the biosensor based on imaging ellipsometry proved to be a more competent mechanism for measuring serum samples from SARS patients and the affinity between these antibodies and the SARS coronavirus.
DOI: 10.1007/s10544-006-8305-2
PubMed: 16718402
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Bei-si-huan West Road, Beijing 100080, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Mechanics, Chinese Academy of Sciences, #15, Bei-si-huan West Road, Beijing 100080</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Duan, Jin Zhu" sort="Duan, Jin Zhu" uniqKey="Duan J" first="Jin-Zhu" last="Duan">Jin-Zhu Duan</name></author><author><name sortKey="Wang, Zhan Hui" sort="Wang, Zhan Hui" uniqKey="Wang Z" first="Zhan-Hui" last="Wang">Zhan-Hui Wang</name></author><author><name sortKey="Chen, Yan Yan" sort="Chen, Yan Yan" uniqKey="Chen Y" first="Yan-Yan" last="Chen">Yan-Yan Chen</name></author><author><name sortKey="Zhang, Pan He" sort="Zhang, Pan He" uniqKey="Zhang P" first="Pan-He" last="Zhang">Pan-He Zhang</name></author><author><name sortKey="Zhan, Lin" sort="Zhan, Lin" uniqKey="Zhan L" first="Lin" last="Zhan">Lin Zhan</name></author><author><name sortKey="Yan, Xi Yun" sort="Yan, Xi Yun" uniqKey="Yan X" first="Xi-Yun" last="Yan">Xi-Yun Yan</name></author><author><name sortKey="Cao, Wu Chun" sort="Cao, Wu Chun" uniqKey="Cao W" first="Wu-Chun" last="Cao">Wu-Chun Cao</name></author><author><name sortKey="Jin, Gang" sort="Jin, Gang" uniqKey="Jin G" first="Gang" last="Jin">Gang Jin</name></author></analytic><series><title level="j">Biomedical microdevices</title><idno type="ISSN">1387-2176</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal (chemistry)</term><term>Antibodies, Viral (chemistry)</term><term>Biosensing Techniques</term><term>Diagnostic Imaging (instrumentation)</term><term>Diagnostic Imaging (methods)</term><term>Humans</term><term>SARS Virus (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anticorps antiviraux ()</term><term>Anticorps monoclonaux ()</term><term>Diagnostic par imagerie ()</term><term>Diagnostic par imagerie (instrumentation)</term><term>Humains</term><term>Techniques de biocapteur</term><term>Virus du SRAS ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="instrumentation" xml:lang="en"><term>Diagnostic Imaging</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Diagnostic Imaging</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biosensing Techniques</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps monoclonaux</term><term>Diagnostic par imagerie</term><term>Humains</term><term>Techniques de biocapteur</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two neutralizing human scFv, b1 and h12 were identified initially using ELISA,employing highly purified virus as the coating antigen. The biosensor technique based on imaging ellipsometry was employed directly to detect two neutralizing monoclonal antibodies and serial serum samples from 10 SARS patients and 12 volunteers who had not SARS. Further, the kinetic process of interaction between the antibodies and SARS-CoV was studied using the real-time function of the biosensor. The biosensor is consistent with ELISA that the antibody h12 showed a higher affinity in encountering the virus than antibody b1. The affinity of antibody b1 and antibody h12 was 9.5 x 10(6) M(-1) and 1.36 x 10(7) M(- 1), respectively. As a label free method, the biosensor based on imaging ellipsometry proved to be a more competent mechanism for measuring serum samples from SARS patients and the affinity between these antibodies and the SARS coronavirus.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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