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Research Article Free access | 10.1172/JCI115931
Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Department of Medicine, University of Virginia School of Medicine, Charlottesville 22908.
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Published September 1, 1992 - More info
The human complement system is an important early host defense against infection. Entamoeba histolytica activates the complement system but is resistant to killing by complement C5b-9 complexes deposited on the membrane surface. Our aim was to identify components of the amebic plasma membrane that mediate resistance to human complement C5b-9 by screening for neutralizing monoclonal antibodies. A monoclonal antibody was identified that abrogated amebic resistance to C5b-9, and the mAb was shown to recognize the parasite's galactose-specific adhesin. The purified adhesin bound to C8 and C9 and conferred C5b-9 resistance to sensitive ameba upon reconstitution; these activities of the adhesin were inhibited by the antiadhesin mAb. The E. histolytica adhesin shared sequence similarities and antigenic cross-reactivity with CD59, a membrane inhibitor of C5b-9 in human blood cells, suggesting both molecular mimicry and shared complement-inhibitory functions.
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