Resialylation of sialidase-treated sheep and human erythrocytes by Trypanosoma cruzi trans-sialidase: restoration of complement resistance of desialylated sheep erythrocytes.
Resialylation of sialidase-treated sheep and human erythrocytes by Trypanosoma cruzi trans-sialidase: restoration of complement resistance of desialylated sheep erythrocytes.
复制标题
克氏锥虫转唾液酸酶对经唾液酸酶处理的绵羊和人红细胞进行再唾液酸化：恢复去唾液酸化绵羊红细胞的补体抗性。
DOI：
10.1093/glycob/2.6.549
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发表时间：
1992
期刊：
影响因子：
4.3
通讯作者：
Nussenzweig,V
中科院分区：
文献类型：
--
作者：
Tomlinson,S;PontesdeCarvalho,L;Vandekerckhove,F;Nussenzweig,V
Trypanosoma cruzitrans-sialidase (TS) is a recently described enzyme which transfers α(2–3)-linked sialic acid from host-derived sialylated glycoconjugates to parasite surface molecules [Schenkmanet al. (1991)Cell, 65, 1117]. We report here on the ability of TS to transfer sialic acid from donor sialyl-α(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 forT.cruziTS and demonstrates directly that sialic acid is solely responsible for preventing alternative pathway activation of human complement by sheep erythrocytes.
