Parasite-host glycan interactions during Trypanosoma cruzi infection: trans-Sialidase rides the show.

Parasite-host glycan interactions during Trypanosoma cruzi infection: trans-Sialidase rides the show.
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DOI:
10.1016/j.bbadis.2020.165692
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发表时间:
2020-05-01
期刊:
Biochimica et biophysica acta. Molecular basis of disease
影响因子:
--
通讯作者:
Leguizamón MS
Leguizamón MS
中科院分区:
其他
文献类型:
--
作者:
Campetella O;Buscaglia CA;Mucci J;Leguizamón MS

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许多重要的病原体-宿主相互作用依赖于高度特异的碳水化合物结合事件。在查加斯病的病原体--克氏锥虫中,与唾液酸(SA)残基有关的糖相互作用是寄生虫感染性、逃避免疫监视和致病的关键。虽然不能重新合成SA,但T.ruzi显示了一种独特的反式唾液酸酶(TS)酶,该酶能够从宿主供体糖结合物中切割末端SA残基,并将其转移到寄生虫表面粘蛋白上,从而产生保护/粘连结构。此外,这种寄生虫将TS送入血流,作为一种修改表面SA信号的方式,从而凭借其自身的优势改变哺乳动物宿主靶细胞的信号/功能特性。在这里,我们讨论了T.ruzi TS的致病方面:它的分子适应,它在感染过程中参与的多种相互作用,以及TS重塑的唾液糖表型提供的一系列新的和吸引人的干预查加斯病的靶点。
Many important pathogen-host interactions rely on highly specific carbohydrate binding events. In the case of the protozoan Trypanosoma cruzi, the causative agent of Chagas disease, glycointeractions involving sialic acid (SA) residues are pivotal for parasite infectivity, escape from immune surveillance and pathogenesis. Though unable to synthesize SA de novo, T. cruzi displays a unique trans-Sialidase (TS) enzyme, which is able to cleave terminal SA residues from host donor glycoconjugates and transfer them onto parasite surface mucins, thus generating protective/adhesive structures. In addition, this parasite sheds TS into the bloodstream, as a way of modifying the surface SA signature, and thereby the signaling/functional properties of mammalian host target cells on its own advantage. Here, we discuss the pathogenic aspects of T. cruzi TS: its molecular adaptations, the multiplicity of interactions in which it is involved during infections, and the array of novel and appealing targets for intervention in Chagas disease provided by TS-remodeled sialoglycophenotypes.
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