Purification and characterization of monoclonal IgG antibodies recognizing Ebola virus glycoprotein

Han, Baek-Sang; Jang, Ho-Young; Racine, Trina; Qiu, Xiangguo; Sin, Jeong-Im

ily [2] . Ebola virus has a negative sense RNA genome that encodes 7 different proteins and is surrounded by an envelope that contains the virally expressed glycoprotein (GP). There are five species of Ebola virus including, Zaire ebolavirus, Sudan ebolavirus, Tai Forest ebolavirus, Bundibugyo ebolavirus and Reston ebolavirus, all of which were named after the places where they were first discovered [3] . Ebola virus GP is associated with viral attachment to the host cell receptor prior to viral entry into the cells [4, 5] . To date, neutralizing antibodies targeting Ebola virus GP have been reported to be somewhat effective at reducing the severity of Ebola virus infection and disease progression in animal models and humans. For example, when Ebola virus-infected monkeys were treated within 24 hours following Ebola virus challenge with ZMAb (composed of three monoclonal antibodies [MAbs] against Ebola virus GP), all survived from Ebola virus infection, while all monkeys without ZMAb treatment died within five days of viral infection [6, 7] Furthermore, ZMapp (Mapp Biopharmaceutical) treatment is known to be effective at reducing mortality rates in patients infected with Ebola virus [8] . Despite the severity of Ebola virus infection, there are currently neither preventive vaccines nor therapeutic drugs readily available for use. Thus, development of vaccines or more effective drugs against Ebola viral infection is highly demanding.