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 journalArticlepeer-review

61 Scopus citations


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 languageEnglish (US)
Pages (from-to)953-958
Number of pages6
JournalJournal of Immunology
Issue number2
StatePublished - Jan 15 2000
Externally publishedYes

ASJC Scopus subject areas

  • Immunology


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