Ebola virus secretory glycoprotein (sGP) diminishes FcγRIIIB-to-CR3 proximity on neutrophils

Andrei L. Kindzelskii; Zhi Yong Yang; Gary J. Nabel; Robert F. Todd; Howard R. Petty

Ebola virus secretory glycoprotein (sGP) diminishes FcγRIIIB-to-CR3 proximity on neutrophils

Andrei L. Kindzelskii, Zhi Yong Yang, Gary J. Nabel, Robert F. Todd, Howard R. Petty

Research output: Contribution to journal › Article › peer-review

Abstract

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

Original language	English (US)
Pages (from-to)	953-958
Number of pages	6
Journal	Journal of Immunology
Volume	164
Issue number	2
State	Published - Jan 15 2000
Externally published	Yes

ASJC Scopus subject areas

Immunology

Cite this

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AU - Kindzelskii, Andrei L.

AU - Yang, Zhi Yong

AU - Nabel, Gary J.

AU - Todd, Robert F.

AU - Petty, Howard R.

PY - 2000/1/15

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Ebola virus secretory glycoprotein (sGP) diminishes FcγRIIIB-to-CR3 proximity on neutrophils

Abstract

ASJC Scopus subject areas

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