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Ansuvimab

Ansuvimab, sold under the brand name Ebanga, is a monoclonal antibody medication used for the treatment of Ebolavirus (Zaire ebolavirus) infection.

The most common symptoms include fever, tachycardia (fast heart rate), diarrhea, vomiting, hypotension (low blood pressure), tachypnea (fast breathing) and chills; however, these are also common symptoms of Ebolavirus infection.

Ansuvimab was approved for medical use in the United States in December 2020. It is on the World Health Organization's List of Essential Medicines.

Ansuvimab is composed of a single monoclonal antibody (mAb) and was initially isolated from immortalized B-cells that were obtained from a survivor of the 1995 outbreak of Ebola virus disease in Kikwit, Democratic Republic of the Congo. In work supported by the United States National Institutes of Health and the Defense Advanced Projects Agency, the heavy and light chain sequences of ansuvimab mAb were cloned into Chinese hamster ovary cell lines and initial production runs were produced by Cook Phamica d.b.a. Catalent under contract with Medimmune.

Ansuvimab is a monoclonal antibody therapy that is infused intravenously into people with Ebola virus disease. Ansuvimab is a neutralizing antibody, meaning it binds to a protein on the surface of Ebola virus that is required to infect cells. Specifically, ansuvimab neutralizes infection by binding to a region of the Ebola virus envelope glycoprotein that, in the absence of ansuvimab, would interact with virus's cell receptor protein, Niemann-Pick C1 (NPC1). This "competition" by ansuvimab prevents Ebola virus from binding to NPC1 and "neutralizes" the virus's ability to infect the targeted cell.

Antibodies have antigen-binding fragment (Fab) regions and constant fragment (Fc) regions. The Neutralization of virus infection occurs when the Fab regions of antibodies binds to virus antigen(s) in a manner that blocks infection. Antibodies are also able to "kill" virus particles directly and/or kill infected cells using antibody-mediated "effector functions" such as opsonization, complement-dependent cytotoxicity, antibody-dependent cell-mediated cytotoxicity and antibody-dependent phagocytosis. These effector functions are contained in the Fc region of antibodies, but is also dependent on binding of the Fab region to antigen. Effector functions also require the use of complement proteins in serum or Fc-receptor on cell membranes. Ansuvimab has been found to be capable of killing cells by antibody-dependent cell-mediated cytotoxicity.

Ansuvimab is a monoclonal antibody that is being evaluated as a treatment for Ebola virus disease. Its discovery was led by the laboratory of Nancy Sullivan at the United States National Institutes of Health Vaccine Research Center and J. J. Muyembe-Tamfum from the Institut National pour la Recherche Biomedicale (INRB) in the Democratic Republic of Congo, working in collaboration with the Institute for Research in Biomedicine (IRB) (Bellinzona, Switzerland) and the United States Army Medical Research Institute of Infectious Diseases. Ansuvimab was isolated from the blood of a survivor of the 1995 outbreak of Ebola virus disease in Kikwit, Democratic Republic of Congo roughly ten years later.

In 2018, a Phase 1 clinical trial of ansuvimab was conducted by Martin Gaudinski within the Vaccine Research Center Clinical Trials Program that is led by Julie E. Ledgerwood. Ansuvimab is also being evaluated during the 2018 North Kivu Ebola outbreak.

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