Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions

Ebola virus is responsible for causing severe hemorrhagic fevers, with case fatality rates of up to 90%. Currently, no antiviral or vaccine is licensed against Ebola virus. A phosphatidylserine-targeting antibody (PGN401, bavituximab) has previously been shown to have broad-spectrum antiviral activi...

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Main Authors: S. D. Dowall, V. A. Graham, K. Corbin-Lickfett, C. Empig, K. Schlunegger, C. B. Bruce, L. Easterbrook, R. Hewson
Format: Article
Language:English
Published: Wiley 2015-01-01
Series:Journal of Immunology Research
Online Access:http://dx.doi.org/10.1155/2015/347903
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author S. D. Dowall
V. A. Graham
K. Corbin-Lickfett
C. Empig
K. Schlunegger
C. B. Bruce
L. Easterbrook
R. Hewson
author_facet S. D. Dowall
V. A. Graham
K. Corbin-Lickfett
C. Empig
K. Schlunegger
C. B. Bruce
L. Easterbrook
R. Hewson
author_sort S. D. Dowall
collection DOAJ
description Ebola virus is responsible for causing severe hemorrhagic fevers, with case fatality rates of up to 90%. Currently, no antiviral or vaccine is licensed against Ebola virus. A phosphatidylserine-targeting antibody (PGN401, bavituximab) has previously been shown to have broad-spectrum antiviral activity. Here, we demonstrate that PGN401 specifically binds to Ebola virus and recognizes infected cells. Our study provides the first evidence of phosphatidylserine-targeting antibody reactivity against Ebola virus.
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institution Kabale University
issn 2314-8861
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language English
publishDate 2015-01-01
publisher Wiley
record_format Article
series Journal of Immunology Research
spelling doaj-art-91c5ea9b8953419998449a915f3d39202025-02-03T05:52:07ZengWileyJournal of Immunology Research2314-88612314-71562015-01-01201510.1155/2015/347903347903Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified VirionsS. D. Dowall0V. A. Graham1K. Corbin-Lickfett2C. Empig3K. Schlunegger4C. B. Bruce5L. Easterbrook6R. Hewson7Public Health England, Porton Down, Wiltshire, Salisbury SP4 0JG, UKPublic Health England, Porton Down, Wiltshire, Salisbury SP4 0JG, UKPeregrine Pharmaceuticals, Inc., Tustin, CA 92780, USAPeregrine Pharmaceuticals, Inc., Tustin, CA 92780, USAPeregrine Pharmaceuticals, Inc., Tustin, CA 92780, USAPublic Health England, Porton Down, Wiltshire, Salisbury SP4 0JG, UKPublic Health England, Porton Down, Wiltshire, Salisbury SP4 0JG, UKPublic Health England, Porton Down, Wiltshire, Salisbury SP4 0JG, UKEbola virus is responsible for causing severe hemorrhagic fevers, with case fatality rates of up to 90%. Currently, no antiviral or vaccine is licensed against Ebola virus. A phosphatidylserine-targeting antibody (PGN401, bavituximab) has previously been shown to have broad-spectrum antiviral activity. Here, we demonstrate that PGN401 specifically binds to Ebola virus and recognizes infected cells. Our study provides the first evidence of phosphatidylserine-targeting antibody reactivity against Ebola virus.http://dx.doi.org/10.1155/2015/347903
spellingShingle S. D. Dowall
V. A. Graham
K. Corbin-Lickfett
C. Empig
K. Schlunegger
C. B. Bruce
L. Easterbrook
R. Hewson
Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
Journal of Immunology Research
title Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
title_full Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
title_fullStr Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
title_full_unstemmed Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
title_short Effective Binding of a Phosphatidylserine-Targeting Antibody to Ebola Virus Infected Cells and Purified Virions
title_sort effective binding of a phosphatidylserine targeting antibody to ebola virus infected cells and purified virions
url http://dx.doi.org/10.1155/2015/347903
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