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. 1992 Sep;90(3):1131–1137. doi: 10.1172/JCI115931

Inhibition of the complement membrane attack complex by the galactose-specific adhesion of Entamoeba histolytica.

L L Braga 1, H Ninomiya 1, J J McCoy 1, S Eacker 1, T Wiedmer 1, C Pham 1, S Wood 1, P J Sims 1, W A Petri Jr 1
PMCID: PMC329975  PMID: 1381719

Abstract

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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