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_38_1
Snippet: l supernatants from two hybridomas (E12 and E49) exhibited high binding activity to all five different recombinant GP1s (suggestive of antigen-non-specific binding) in an ELI-SA (data not shown). In addition, these cell supernatants also reacted with GP in an ELISA using HRP-conjugated IgM as well (data not shown), confirming that clones E12-10 and E49-3 are indeed from polyclonal cells producing IgG and IgM antibodies. It has been reported that .....
Document: l supernatants from two hybridomas (E12 and E49) exhibited high binding activity to all five different recombinant GP1s (suggestive of antigen-non-specific binding) in an ELI-SA (data not shown). In addition, these cell supernatants also reacted with GP in an ELISA using HRP-conjugated IgM as well (data not shown), confirming that clones E12-10 and E49-3 are indeed from polyclonal cells producing IgG and IgM antibodies. It has been reported that Ebola virus GP is responsible for binding to the host cell's receptor for viral entry [4, 5] . Ebola virus GP-specific antibodies including 2G4 monoclonal IgG antibodies are known to block viral infection to the host cells [6] . In this study, we observed that the five purified IgG antibodies were unable to block Ebola virus infection to the host cell in vitro. These data suggest that the five purified GP-specific IgG antibodies including three (rec-ognizing a native GP expressed on the cell surface) do not have any neutralizing activity toward Ebola virus infection.
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