Demonstration of a sialic acid-specific lectin and two distinct sialidases in Tritrichomonas foetus
2000
Babal, P. (Comenius University, Bratislava (Slovak Republic). Department of Pathology)
Tritrichomonas foetus is a sexually transmitted protozoan parasite of the bovine urogenital tract. This organism was shown to use a sialic acid-mediated adhesion mechanism. Size exclusion chromatography of the culture supernatant revealed a 728 kDa lectin and two distinct sialidases with molecular weights of 853 kDa (sialidase 1) and 254 kDa (sialidase 2). Antisera raised against the separated proteins identified distinct band patterns in western blots of electrophoresed whole T. foetus organisms. Cytochemistry of T. foetus with anti-lectin antibodies showed membrane localization. Sialidase 1 was detected only in the cytoplasm while sialidase 2 was linked to the membrane. The membrane expression of the lectin may indicate its involvement in the parasite adhesion to host sialylated glycoconjugates. The finding of two different sialidases, one of them membrane-bound, suggests different biological functions of the enzymes. Based on supposed sialic acid linkage specificity, the membrane located sialidase hydrolyses sialic acid mainly from mucin and the other sialidase, which is probably only secreted, acts on mucosal epithelial cell membranes
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