Complement resistance of pathogenic Entamoeba histolytica mediated by trypsin-sensitive surface component(s).
Pathogenic forms of the protozoan parasite Entamoeba histolytica were reported previously to resist the cytolytic effect of the alternative complement pathway (AP) only temporarily during exposure to complement. In contrast, nonpathogenic forms of E. histolytica had been found to show AP resistance as a stable property. We studied the mechanisms of AP resistance of the two forms. Upon exposure to AP activity, resistant pathogenic or nonpathogenic forms bound significantly less C3 products than complement-sensitive pathogenic amebae, indicating that the two resistant forms both inhibited AP amplification. Various enzymatic treatments and inhibition of membrane mobility by cytochalasin B and glutaraldehyde fixation showed that the mechanisms of AP inhibition differed between pathogenic and nonpathogenic forms; in contrast to nonpathogenic forms, pathogenic amebae required intact membrane mobility and a trypsin-sensitive surface component(s) to inhibit AP activation.
Hamelmann
C
C
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
Urban
B
B
Foerster
B
B
Horstmann
R D
RD
D000818:Animals; D003176:Complement C3 / Q000378:metabolism*; D003170:Complement Pathway, Alternative; D003571:Cytochalasin B / Q000494:pharmacology; D003602:Cytotoxicity, Immunologic; D004748:Entamoeba histolytica / Q000187:drug effects / Q000276:immunology* / Q000472:pathogenicity; D005976:Glutaral / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D009439:Neuraminidase / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D010738:Type C Phospholipases / Q000494:pharmacology
D003176:Complement C3; D003571:Cytochalasin B; D010738:Type C Phospholipases; D009439:Neuraminidase; D014357:Trypsin; D005976:Glutaral