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Immunol Lett. 1991 May;28(2):167-74. doi: 10.1016/0165-2478(91)90116-r.

Acetylcholinesterase from Schistosoma mansoni: immunological characterization.

Immunology letters

B Espinoza, R Tarrab-Hazdai, S Himmeloch, R Arnon

Affiliations

  1. Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.

PMID: 1885212 DOI: 10.1016/0165-2478(91)90116-r

Abstract

The enzyme acetylcholinesterase (AChE) is present in the trematode Schistosoma mansoni, which infects humans and causes a severe disease called schistosomiasis or Bilharzia. We have purified this enzyme and raised polyclonal antibodies against it. The specificity of these antibodies against the schistosome enzyme was demonstrated by their capacity to precipitate exclusively AChE activity from cercariae extract and to recognize the 8S molecular form of the parasite's AChE. On the other hand, they did not cross-react at all with AChE from human erythrocytes. By employing immunogold electron microscopy, AChE was located on the surface, in the membranal bodies of the tegument and in the muscles of schistosomula. The antibodies raised against the purified AChE of S. mansoni are of protective value, as they led to efficient complement-mediated killing of schistosomula in vitro. It was also demonstrated that antibodies specific towards S. mansoni AChE are present in the sera of mice and of human patients infected with the parasite, suggesting that this enzyme partakes in the immune response towards the parasite during infection. These cumulative data, particularly the schistosomicidal activity of the antibodies and their lack of cross-reactivity with human AChE, are of significance in the consideration of the S. mansoni AChE for vaccination purposes.

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