Mechanism of Human Antibody-Mediated Neutralization of Marburg Virus

Andrew I. Flyak, Philipp A. Ilinykh, Charles D. Murin, Tania Garron, Xiaoli Shen, Marnie L. Fusco, Takao Hashiguchi, Zachary A. Bornholdt, James C. Slaughter, Gopal Sapparapu, Curtis Klages, Thomas G. Ksiazek, Andrew B. Ward, Erica Ollmann Saphire, Alexander Bukreyev, James E. Crowe Jr.
  • Cell, February 2015, Elsevier
  • DOI: 10.1016/j.cell.2015.01.031

What is it about?

An adventure traveler visited Python Cave in Uganda and became seriously ill with Marburg infection, following exposure to fruit bats in that cave. Investigators in the Vanderbilt Vaccine Center used a powerful human hybridoma technique to make human monoclonal antibodies from this survivor's B cells. Study of the activity and the fine specificity of over 50 antibodies revealed new insights into how human antibodies inhibit Marburg, a filovirus related to Ebola.

Why is it important?

The work shows that most potent human antibodies to Marburg virus target the receptor binding domain on the viral surface glycoprotein. These antibodies are of interest because they provide insights into the mechanism of neutralization, but they also are important because several are being developed as therapeutic drugs for Marburg infection.

Perspectives

Dr James E Crowe
Vanderbilt University Medical Center

This paper shows the remarkable depth of information about virus immunity that can be obtained by careful study of a large panel of antibodies from a single donor, in this case antibodies to Marburg virus.

Read Publication

http://dx.doi.org/10.1016/j.cell.2015.01.031

The following have contributed to this page: Dr James E Crowe