國家衛生研究院 NHRI:Item 3990099045/4724
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    Please use this identifier to cite or link to this item: http://ir.nhri.org.tw/handle/3990099045/4724


    Title: Identification of SARS CoV neutralizing epitope
    Authors: Lia, SC;Chong, P;Yeh, CT;Liu, L;Chi, HY;Jan, JT;Liu, HW;Chen, A;Wang, YC
    Contributors: Vaccine Research and Development Center
    Abstract: The spike (S) glycoprotein is thought to play a complex and central role in the biology and athogenesis of SARS coronavirus infection. In this study, a fragment (amino acid 268-1255) of SARS-CoV S protein was cloned into the prokaryotic expression vector, pET101/D-TOPO, and the recombinant protein (rS268) was expressed and purified to near homogeneity. After immunization with rS268, S protein-specific rabbit antisera and BALB/c monoclonal antibodies were induced and confirmed using ELISA, Western blot and IFA. Both rabbit antiserum and BALB/c monoclonal antibodies were found to be effectively neutralizing the infection of Vero E6 cells by SARS CoV in a dose-dependent manner. Further studies revealed the mode of action of these neutralizing monoclonal antibodies that inhibited the entry of SARS-CoV into Vero E6 cells. Systematic epitope mapping showed that all these neutralizing monoclonal antibodies recognized a 15-residues peptide (CB-119) corresponding to residues 143-1157 (SPDVDLGDISGINAS) that was located to the second heptad repeat (HR2) region near to the C-terminal end of the SARS-CoV spike protein. The current results implicated that the second heptad repeat region of spike protein could be a good target for vaccine development against SARS CoV.
    Date: 2005
    Relation: Biopolymers. 2005;80(4):594.
    Link to: http://dx.doi.org/10.1002/bip.20325
    JIF/Ranking 2023: http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=NHRI&SrcApp=NHRI_IR&KeyISSN=0006-3525&DestApp=IC2JCR
    Cited Times(WOS): https://www.webofscience.com/wos/woscc/full-record/WOS:000229901200511
    Appears in Collections:[Pele Choi-Sing Chong] Conference Papers/Meeting Abstract

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