Identification of a protein disulfide isomerase of Neospora caninum in excretory-secretory products and its IgA binding and enzymatic activities.
Identification of a protein disulfide isomerase of Neospora caninum in excretory-secretory products and its IgA binding and enzymatic activities.
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DOI：
10.1016/j.vetpar.2006.02.029
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发表时间：
2006-06
影响因子：
2.6
通讯作者：
M. Liao;Liqing Ma;H. Bannai;Eung‐goo Lee;Z. Xie;Xiaofei Tang;Houshuang Zhang;X. Xuan;K. Fujisaki
中科院分区：
文献类型：
--
作者：
M. Liao;Liqing Ma;H. Bannai;Eung‐goo Lee;Z. Xie;Xiaofei Tang;Houshuang Zhang;X. Xuan;K. Fujisaki
从犬新孢子虫速殖子溶胞产物和排泄分泌产物中鉴定出一种分子量为50kDa的蛋白质二硫键异构酶（NcPDI）。58.0%的牛泪液样本中的伊加抗体识别NcPDI，这表明PDI特异性抗体可能参与对寄生虫的防御。此外，PDI特异性抑制剂和NcPDI抗血清对N.犬速殖子此外，纯化的重组NcPDI在体外通过催化和复性还原RNase A并辅助天然溶菌酶的回收而显示出生物学活性。这些发现表明NcPDI具有PDI特异性酶活性，可能是新孢子虫病化疗的假定靶点。
A protein disulfide isomerase of Neospora caninum (NcPDI) with a molecular weight of 50kDa was identified in tachyzoite lysate and excretory–secretory (ES) products. The IgA antibody in 58.0% of the individual cattle tear samples recognized the NcPDI, which suggests that the PDI-specific antibody may be involved in defense against parasites. In addition, PDI-specific inhibitors and NcPDI antiserum showed inhibitory effects on the growth of N. caninum tachyzoites. Furthermore, the purified recombinant NcPDI demonstrated biological activities in vitro by catalysis and refolding of reduced RNase A and assisted in the recovery of native lysozyme. These findings indicate that NcPDI possesses PDI-specific enzymatic activity and could be a putative target for chemotherapy for neosporosis.