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Glycobiology vol 2 no 6 pp. 549-551, 1992
© 1992

research-article

Resialylation of sialidase-treated sheep and human erythrocytes by Trypanosoma cruzi trans-sialidase: restoration of complement resistance of desialylated sheep erythrocytes

Stephen Tomlinson, Lain Pontes de Carvalho, Filip Vandekerckhove and Victor Nussenzweig

Department of Pathology, New York University Medical Center 550 First Avenue, New York, NY 10016, USA

Received on July 14, 1992; accepted on September 7, 1992

Trypanosoma cruzi trans-sialidase (TS) is a recently described enzyme which transfers {alpha}(2–3)-linked sialic acid from host-derived sialylated glycoconjugates to parasite surface molecules [Schenkman et al. (1991) Cell, 65, 1117]. We report here on the ability of TS to transfer sialic acid from donor sialyl-{alpha}(2–3)lactose to sialidase-treated sheep and human erythrocytes. Up to ~50% resialylation of both desialylated red cells could be attained. Resialylation of desialylated sheep erythrocytes restores their resistance to lysis by human complement. This ascribes a possible biological role for T.cruzi TS and demonstrates directly that sialic acid is solely responsible for preventing alternative pathway activation of human complement by sheep erythrocytes.

complement erythrocytes sialic acid sialidase trans-sialidase


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