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_39
Snippet: In summary, we found that among 12 GP-specific IgG-producing hybridomas, five were successfully sub-cloned to IgGproducing single clones. All of the five purified monoclonal IgG antibodies recognized GP in an antigen-specific and IgG dose-dependent manner. In particular, three recognized the native forms of GP expressed on the cell surface and remained reactive to GP at the lowest tested concentrations ranging from 1.953 to 7.8 ng/mL. However, th.....
Document: In summary, we found that among 12 GP-specific IgG-producing hybridomas, five were successfully sub-cloned to IgGproducing single clones. All of the five purified monoclonal IgG antibodies recognized GP in an antigen-specific and IgG dose-dependent manner. In particular, three recognized the native forms of GP expressed on the cell surface and remained reactive to GP at the lowest tested concentrations ranging from 1.953 to 7.8 ng/mL. However, these antibodies were unable to neutralize Ebola virus, suggesting that none of these purified antibodies can block Ebola virus infection. Taken together, the five purified IgG antibodies possess Ebola virus GP-binding activity but not Ebola virus neutralizing activity.
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