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Science 30 October 1998:
Vol. 282. no. 5390, p. 841
DOI: 10.1126/science.282.5390.841s

This Week in Science

Z.-y. Yang et al. reported that the secreted glycoprotein (sGP) of Ebola virus interacted with human neutrophils through the CD16b surface receptor (Reports, 13 Feb., p. 1034).

T. Maruyama et al. comment that the study "did not exclude the possibility that the rabbit antibosdy used to detect the binding of Ebola sGP" mediated the interaction between virus and cell. They "performed flow cytometry to study the putative interaction of sGP with neutrophils" with human and rabbit monoclonal antibody fragments specific for sGP. They "could not detect any binding of sGP to neutrophils." They also did not observe absorption of sGP by purified neutrophils. They conclude that "Ebola sGP does not bind FcgRIIIb (CD16) or any other receptor on neutrophils.

In response, Yang et al. confirmed the inability to detect binding with an antibody fragment. However, they give several reasons for this result, and they performed a new experiment, which suggests that the explanation provided by Maruyama et al. "does not account for all of the available data." "Additional studies," they say, "will be required to determine whether CD16 is directly or indirectly responsible for the interaction." (Yang et al. also provide a correction to the far-left graph of figure 1A of their report.)The full text of these comments can be seen at www.sciencemag.org/cgi/content/full/282/5390/843a





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Science. ISSN 0036-8075 (print), 1095-9203 (online)