title: Ebola virus can be effectively neutralized by antibody produced in natural human infection.
abstract: The activity of antibodies against filoviruses is poorly understood but has important consequences for vaccine design and passive prophylaxis. To investigate this activity, a panel of recombinant human monoclonal antibodies to Ebola virus antigens was isolated from phage display libraries constructed from RNA from donors who recovered from infection in the 1995 Ebola virus outbreak in Kikwit, Democratic Republic of Congo. Antibodies reactive with nucleoprotein (NP), envelope glycoprotein (GP), and secreted envelope glycoprotein (sGP) were characterized by immunofluorescence and radioimmunoprecipitation assays. Four antibodies reacting strongly with sGP and weakly with GP and two antibodies reacting with NP were not neutralizing. An antibody specific for GP neutralized Ebola virus to 50% at 0.4 microgram/ml as the recombinant Fab fragment and to 50% at 0.3 microgram/ml (90% at 2.6 microgram/ml) as the corresponding whole immunoglobulin G1 molecule. The studies indicate that neutralizing antibodies are produced in infection by Ebola virus although probably at a relatively low frequency. The neutralizing antibody may be useful in vaccine design and as a prophylactic agent against Ebola virus infection.
authors.affiliation: Departments of Immunology and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
authors.forename: T
authors.initials: T
authors.lastname: Maruyama
authors.forename: L L
authors.initials: LL
authors.lastname: Rodriguez
authors.forename: P B
authors.initials: PB
authors.lastname: Jahrling
authors.forename: A
authors.initials: A
authors.lastname: Sanchez
authors.forename: A S
authors.initials: AS
authors.lastname: Khan
authors.forename: S T
authors.initials: ST
authors.lastname: Nichol
authors.forename: C J
authors.initials: CJ
authors.lastname: Peters
authors.forename: P W
authors.initials: PW
authors.lastname: Parren
authors.forename: D R
authors.initials: DR
authors.lastname: Burton
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology*; D000915:Antibody Affinity; D000956:Antigens, Viral / Q000276:immunology; D002522:Chlorocebus aethiops; D015023:Democratic Republic of the Congo / Q000453:epidemiology; D004196:Disease Outbreaks; D029043:Ebolavirus / Q000276:immunology*; D019085:Fluorescent Antibody Technique, Direct; D015723:Gene Library; D006023:Glycoproteins / Q000276:immunology*; D019142:Hemorrhagic Fever, Ebola / Q000097:blood / Q000453:epidemiology / Q000276:immunology*; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000276:immunology / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D019590:Nucleocapsid Proteins / Q000276:immunology*; D015531:Radioimmunoprecipitation Assay; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000276:immunology*; D014764:Viral Proteins
chemical_list: D000914:Antibodies, Viral; D000956:Antigens, Viral; D006023:Glycoproteins; D007140:Immunoglobulin Fab Fragments; D019590:Nucleocapsid Proteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C113189:envelope glycoprotein, Ebola virus; C113190:nucleocapsid protein, Ebola virus; C110613:secreted glycoprotein, Ebola virus