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Antibody Treatment of Ebola and Sudan Virus Infection via a Uniquely Exposed Epitope within the Glycoprotein Receptor-Binding Site CELL REPORTS Howell, K. A., Qiu, X., Brannan, J. M., Bryan, C., Davidson, E., Holtsberg, F. W., Wec, A. Z., Shulenin, S., Biggins, J. E., Douglas, R., Enterlein, S. G., Turner, H. L., Pallesen, J., Murin, C. D., He, S., Kroeker, A., Vu, H., Herbert, A. S., Fusco, M. L., Nyakatura, E. K., Lai, J. R., Keck, Z., Foung, S. K., Saphire, E. O., Zeitlin, L., Ward, A. B., Chandran, K., Doranz, B. J., Kobinger, G. P., Dye, J. M., Aman, M. J. 2016; 15 (7): 1514-1526

Abstract

Previous efforts to identify cross-neutralizing antibodies to the receptor-binding site (RBS) of ebolavirus glycoproteins have been unsuccessful, largely because the RBS is occluded on the viral surface. We report a monoclonal antibody (FVM04) that targets a uniquely exposed epitope within the RBS; cross-neutralizes Ebola (EBOV), Sudan (SUDV), and, to a lesser extent, Bundibugyo viruses; and shows protection against EBOV and SUDV in mice and guinea pigs. The antibody cocktail ZMapp™ is remarkably effective against EBOV (Zaire) but does not cross-neutralize other ebolaviruses. By replacing one of the ZMapp™ components with FVM04, we retained the anti-EBOV efficacy while extending the breadth of protection to SUDV, thereby generating a cross-protective antibody cocktail. In addition, we report several mutations at the base of the ebolavirus glycoprotein that enhance the binding of FVM04 and other cross-reactive antibodies. These findings have important implications for pan-ebolavirus vaccine development and defining broadly protective antibody cocktails.

View details for DOI 10.1016/j.celrep.2016.04.026

View details for Web of Science ID 000376165300015

View details for PubMedID 27160900

View details for PubMedCentralID PMC4871745