Ebola virus secretory glycoprotein (sGP) diminishes Fc gamma RIIIB-to-CR3 proximity on neutrophils

Previous studies have shown that Ebola virus' secretory glycoprotein (sGP) binds to Fc gamma RIIIB (CD16b) and inhibits L-selectin shedding. In this study, we test the hypothesis that sGP interferes with the physical linkage between CR3 and Fc gamma RIIIB. Neutrophils were stained with rhodamin...

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Veröffentlicht in:	The Journal of immunology (1950) 2000-01, Vol.164 (2), p.953-958
Hauptverfasser:	Kindzelskii, A L, Yang, Z, Nabel, G J, Todd, 3rd, R F, Petty, H R
Format:	Artikel
Sprache:	eng
Schlagworte:	Adult AFc receptors complement receptor 3 Cytophotometry Ebola virus Ebolavirus - immunology Energy Transfer - immunology Fc receptors Glycoproteins - physiology Humans Immunosuppressive Agents - pharmacology Macrophage-1 Antigen - metabolism Microscopy, Fluorescence Neutrophils - immunology Neutrophils - metabolism Receptor Aggregation - immunology Receptors, IgG - antagonists & inhibitors Receptors, IgG - metabolism secretory glycoprotein Spectrometry, Fluorescence Viral Proteins
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Zusammenfassung:	Previous studies have shown that Ebola virus' secretory glycoprotein (sGP) binds to Fc gamma RIIIB (CD16b) and inhibits L-selectin shedding. In this study, we test the hypothesis that sGP interferes with the physical linkage between CR3 and Fc gamma RIIIB. Neutrophils were stained with rhodamine-conjugated anti-CD16b mAb (which does not inhibit sGP binding) and fluorescein-conjugated anti-CR3 mAb reagents and then incubated in media with or without sGP. Physical proximity between fluorochrome-labeled CR3 and Fc gamma RIIIB on individual cells was measured by resonance energy transfer (RET) imaging, quantitative RET microfluorometry, and single-cell imaging spectrophotometry. Cells incubated with control supernatants displayed a significant RET signal, indicative of physical proximity (
ISSN:	0022-1767 1550-6606
DOI:	10.4049/jimmunol.164.2.953