The recognition of the Entamoeba histolytica galactose-inhibitable adherence lectin by antibodies was studied using sera obtained from subjects in South Africa with an amebic liver abscess or asymptomatically pathogenic or nonpathogenic E. histolytica infection and from uninfected regional controls. In addition, sera from healthy American controls or Americans known to be infected with other parasites were studied. Of the 95 sera containing antibodies to total parasite protein, 95% demonstrated antibodies to the 170-kDa heavy subunit but not to the 35-kDa light lectin subunit. All sera (n = 253) were tested by ELISA for antibodies to lectin: 99% from liver abscess patients and all 4 from individuals asymptomatically infected with pathogenic E. histolytica were positive; all from the 40 healthy American controls and the 29 infected with other parasites were negative (P less than .01). The prevalence of serum anti-lectin antibodies was identical (25%) in asymptomatic South Africans with either a nonpathogenic infection or a negative stool culture for E. histolytica. Thus, the presence of serum antibodies to lectin seems to indicate current or prior invasive amebiasis or asymptomatic intestinal infection with pathogenic E. histolytica.

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Entamoeba histolytica infection results in either asymptomatic colonization or invasive colitis and liver abscess. E. histolytica isolates from patients with invasive disease have characteristic isoenzyme proffles (pathogenic zymodemes), suggesting a role for parasite factors in determining the severity of infection. A galactose-specific cell surface lectin from a pathogenic zymodeme was shown to mediate in vitro adherence to human colonic mucins and contact-dependent killing of target cells. Six nonoverlapping antigenic determinants were identified on the 170-kilodalton heavy subunit of the pathogenic lectin. Anti-lectin monoclonal antibodies (MAb) directed against epitopes 1 and 2 enhanced adherence whereas MAb to epitopes 3 through 6 either inhibited or had no effect on adherence. We tested 50 pathogenic and nonpathogenic strains for reactivity to these anti-lectin MAb by radioimmunoassay. MAb to epitopes 1 through 6 reacted in the radioimmunoassay with all 16 pathogenic zymodeme strains tested. In contrast, only MAb to epitopes 1 and 2 bound to the lectin from nonpathogenic strains. Western immunoblots with anti-lectin antibodies showed that the 170-kilodalton heavy subunit was present in the nonpathogenic amebae. Adherence of the nonpathogenic SAW 760 strain to human erythrocytes was enhanced by MAb to epitope 1 and blocked by galactose, confirming the presence of a functionally active lectin. A lectin radioimmunoassay based on MAb to epitopes 1 and 3 proved to be a simple and rapid method to distinguish pathogenic from nonpathogenic amebae in culture. Further exploration of the functional consequences of the antigenic differences demonstrated for the lectin may lead to a better understanding of its role in pathogenesis.

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