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Science 13 February 1998:
Vol. 279. no. 5353, pp. 1034 - 1037
DOI: 10.1126/science.279.5353.1034

Reports

Distinct Cellular Interactions of Secreted and Transmembrane Ebola Virus Glycoproteins

Zhi-yong Yang, Rafael Delgado, Ling Xu, Robert F. Todd, Elizabeth G. Nabel, Anthony Sanchez, Gary J. Nabel *

The mechanisms by which Ebola virus evades detection and infects cells to cause hemorrhagic fever have not been defined, though its glycoprotein, synthesized in either a secreted or transmembrane form, is likely involved. Here the secreted glycoprotein was found to interact with neutrophils through CD16b, the neutrophil-specific form of the Fc gamma  receptor III, whereas the transmembrane glycoprotein was found to interact with endothelial cells but not neutrophils. A murine retroviral vector pseudotyped with the transmembrane glycoprotein preferentially infected endothelial cells. Thus, the secreted glycoprotein inhibits early neutrophil activation, which likely affects the host response to infection, whereas binding of the transmembrane glycoprotein to endothelial cells may contribute to the hemorrhagic symptoms of this disease.

Z-y. Yang and G. J. Nabel, Howard Hughes Medical Institute and Departments of Internal Medicine and Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
R. Delgado, L. Xu, R. F. Todd, E. G. Nabel, Department of Internal Medicine, University of Michigan, Ann Arbor, MI 48109, USA.
A. Sanchez, Centers for Disease Control and Prevention, Atlanta, GA 30333, USA.
*   To whom correspondence should be addressed.


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