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