Author: Han, Baek-Sang; Jang, Ho-Young; Racine, Trina; Qiu, Xiangguo; Sin, Jeong-Im
Title: Purification and characterization of monoclonal IgG antibodies recognizing Ebola virus glycoprotein Document date: 2018_7_31
ID: v5oh0haa_3
Snippet: In this study, we obtained five monoclonal IgG antibodies by an immunization scheme using Ebola virus GP DNA and protein vaccines. The antibodies showed binding activity to the native forms of GP expressed on the cell surface or the mucin-like region of GP, but not the denatured form of GP. They also reacted specifically with GP, and remained reactive to GP at the lowest tested concentrations ranging from 1.953 to 7.8 ng/mL. However, none of the .....
Document: In this study, we obtained five monoclonal IgG antibodies by an immunization scheme using Ebola virus GP DNA and protein vaccines. The antibodies showed binding activity to the native forms of GP expressed on the cell surface or the mucin-like region of GP, but not the denatured form of GP. They also reacted specifically with GP, and remained reactive to GP at the lowest tested concentrations ranging from 1.953 to 7.8 ng/mL. However, none of the antibodies neutralized Ebola virus infection in vitro, suggesting that these IgG antibodies are unable to block Ebola virus infection. Thus, these IgG antibodies possess GP-binding activity but not Ebola virus-neutralizing activity.
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