Identification of a developmentally regulated sialidase in Eimeria tenella that is immunologically related to the Trypanosoma cruzi enzyme.

Sporozoites and merozoites of three species of Eimeria, E. tenella, E. maxima, and E. necatrix, that cause diarrhea in chickens worldwide, were examined for their expression of sialidase (SA) activity. The enzyme was found in three species, and the activity of merozoites was 10-20 times higher than that of sporozoites. The enzyme was resistant to degradation by proteases that are normally present in the intestine, a site inhabited by the Eimeria parasites, and it was relatively resistant to heat, with optimum activity being at 40 degrees C, which is within the range of temperature in the chicken intestine (40-43 degrees C). E. tenella SA was immunoprecipitated by monoclonal and polyclonal antibodies raised against the Trypanosoma cruzi SA (TCSA), and enzyme activity was neutralized by these antibodies. E. tenella SA was identified by immunoblots as a doublet of molecular weight 190,000 and 180,000 using, as a probe, anti-TCSA antibodies and antibodies against a synthetic peptide (TR) derived from the long tandem repeat domain of TCSA. Binding of the monoclonal and polyclonal antibodies to E. tenella was completely blocked by TR, but not by an irrelevant peptide (BR). Therefore, E. tenella expresses a developmentally regulated SA that is structurally related to the T. cruzi counterpart. Because of the high SA activity in merozoites, and by analogy with other SA-producing microbes that inhabit mucin-rich epithelia, we suggest that the Eimeria SA plays a role in desialylating intestinal mucins to reduce viscosity of the local environment and thereby facilitate parasite migration. The enzyme could also play a role in host cell-parasite interaction.