Article
Recombinant human monoclonal antibodies to Ebola virus.
Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.
The Journal of Infectious Diseases (impact factor:
6.41).
03/1999;
179 Suppl 1:S235-9.
DOI:10.1086/514280
pp.S235-9
Source: PubMed
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Citations (0)
- Cited In (3)
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Article: Pre- and postexposure prophylaxis of Ebola virus infection in an animal model by passive transfer of a neutralizing human antibody.
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ABSTRACT: A neutralizing human monoclonal antibody, KZ52, protects guinea pigs from lethal Ebola Zaire virus challenge. Administration before or up to 1 h after challenge resulted in dose-dependent protection by the antibody. Interestingly, some antibody-treated animals survived despite developing high-level viremia, suggesting that the mechanism of protection by KZ52 may extend beyond reduction of viremia by virus neutralization. KZ52 is a promising candidate for immunoprophylaxis of Ebola virus infection.Journal of Virology 07/2002; 76(12):6408-12. · 5.40 Impact Factor -
Article: Structural basis for differential neutralization of ebolaviruses.
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ABSTRACT: There are five antigenically distinct ebolaviruses that cause hemorrhagic fever in humans or non-human primates (Ebola virus, Sudan virus, Reston virus, Taï Forest virus, and Bundibugyo virus). The small handful of antibodies known to neutralize the ebolaviruses bind to the surface glycoprotein termed GP₁,₂. Curiously, some antibodies against them are known to neutralize in vitro but not protect in vivo, whereas other antibodies are known to protect animal models in vivo, but not neutralize in vitro. A detailed understanding of what constitutes a neutralizing and/or protective antibody response is critical for development of novel therapeutic strategies. Here, we show that paradoxically, a lower affinity antibody with restricted access to its epitope confers better neutralization than a higher affinity antibody against a similar epitope, suggesting that either subtle differences in epitope, or different characteristics of the GP₁,₂ molecules themselves, confer differential neutralization susceptibility. Here, we also report the crystal structure of trimeric, prefusion GP₁,₂ from the original 1976 Boniface variant of Sudan virus complexed with 16F6, the first antibody known to neutralize Sudan virus, and compare the structure to that of Sudan virus, variant Gulu. We discuss new structural details of the GP₁-GP₂ clamp, thermal motion of various regions in GP₁,₂ across the two viruses visualized, details of differential interaction of the crystallized neutralizing antibodies, and their relevance for virus neutralization.Viruses 04/2012; 4(4):447-70. · 1.50 Impact Factor -
Article: Antibodies for biodefense.
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ABSTRACT: Potential bioweapons are biological agents (bacteria, viruses, and toxins) at risk of intentional dissemination. Biodefense, defined as development of therapeutics and vaccines against these agents, has seen an increase, particularly in the US following the 2001 anthrax attack. This review focuses on recombinant antibodies and polyclonal antibodies for biodefense that have been accepted for clinical use. These antibodies aim to protect against primary potential bioweapons, or category A agents as defined by the Centers for Disease Control and Prevention (Bacillus anthracis, Yersinia pestis, Francisella tularensis, botulinum neurotoxins, smallpox virus, and certain others causing viral hemorrhagic fevers) and certain category B agents. Potential for prophylactic use is presented, as well as frequent use of oligoclonal antibodies or synergistic effect with other molecules. Capacities and limitations of antibodies for use in biodefense are discussed, and are generally applicable to the field of infectious diseases.mAbs 11/2011; 3(6):517-27.
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Keywords
2 donors
antibodies
bone marrow RNA
characteristic punctate staining pattern
Democratic Republic
donor serum
Fabs
functional terms
Human Fab
IFAs
Kikwit
libraries
Major interest
panning
SGP
subtype Zaire
uninfected cells
virion membrane preparation
virus cell lysate
weak binders