Structural and functional properties of Trypanosoma trans-sialidase.
Structural and functional properties of Trypanosoma trans-sialidase.
复制标题
锥虫转唾液酸酶的结构和功能特性。
DOI：
10.1146/annurev.mi.48.100194.002435
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发表时间：
1994
影响因子：
10.5
通讯作者：
Nussenzweig,V
中科院分区：
文献类型：
--
作者：
Schenkman,S;Eichinger,D;Pereira,ME;Nussenzweig,V
Sialic acids and sialidases play important roles in cellular interactions and modulate the recognition of pathogenic microbes by mammalian host cells. Protozoan parasites of the genus Trypanosoma express a unique sialic acid-metabolizing enzyme. This enzyme, named trans-sialidase (TS), catalyzes the transfer of sialic acids from host glycoconjugates to acceptor molecules of the parasite plasma membrane. In African trypanosomes, the agents of sleeping sickness, TS is found only in forms developing within the insect vector, and the enzyme sialylates the major surface protein. In Trypanosoma cruzi, the causative agent of Chagas' disease in Central and South America, TS is expressed both in the insect and mammalian forms of the parasite. The T. cruzi enzyme has been biochemically characterized, and the gene encoding the enzyme has been cloned. The enzyme sialylates abundant mucin-like molecules present on the surface of the parasite. Several lines of evidence suggest that TS and sialic acid acceptors on the surface of T. cruzi participate in host-parasite interactions and mediate the initial stages of the trypanosomes' invasion of host cells.
