A secretory cellulose-binding protein cDNA cloned from the root-knot nematode (Meloidogyne incognita)
A secretory cellulose-binding protein cDNA cloned from the root-knot nematode (Meloidogyne incognita)
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DOI：
10.1094/mpmi.1998.11.10.952
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发表时间：
1998-10-01
影响因子：
3.5
通讯作者：
Hussey, RS
中科院分区：
文献类型：
--
作者：
Ding, X;Shields, J;Hussey, RS
利用RNA指纹技术从南方根结线虫（Meloidogyne incognita）中克隆了一个分泌型纤维素结合蛋白的cDNA，命名为Mi-cbp-1，编码一个203个氨基酸的蛋白质，其N端含有一个分泌信号肽。推定的MI-CBP-1的C-末端序列与细菌型纤维素结合结构域相似，而N-末端序列与数据库中的任何蛋白质均未显示出显著的相似性。重组MI-CBP-1不具有纤维素酶活性，但与纤维素和植物细胞壁结合。incognita、M. arenaria和M. javanica，而不是M. Hapla、Heterodera glycines或Caecumhabditis elegans，在间接免疫荧光显微镜下，针对重组MwI-CBP-1的多克隆抗体在第二阶段幼虫的腹下腺细胞中强烈标记分泌颗粒，用多克隆抗体对第二阶段幼虫的口针分泌物中的MI-CBP-1进行酶联免疫吸附试验检测，表明MI-CBP-1可以通过线虫的口针分泌，提示纤维素结合蛋白可能在发病机制中起作用。
A cDNA encoding a secretory cellulose-binding protein was cloned from the root-knot nematode (Meloidogyne incognita) with RNA fingerprinting, The putative full-length cDNA, named Mi-cbp-1, encoded a 203 amino acid protein containing an N-terminal secretion signal peptide. The C-terminal sequence of the putative MI-CBP-1 was similar to a bacterial-type cellulose-binding domain, whereas the N-terminal sequence did not show significant similarity to any proteins in data bases. Recombinant MI-CBP-1 lacked cellulase activity, but bound to cellulose and plant cell walls, in Southern blot hybridization, Mi-cbp-1 hybridized with genomic DNA from M. incognita, M, arenaria, and M. javanica, but not M. hapla, Heterodera glycines, or Caenorhabditis elegans, Polyclonal antibodies raised against recombinant MwI-CBP-1 strongly labeled secretory granules in subventral gland cells of second-stage juveniles in indirect immunofluorescence microscopy, Enzyme-linked immunosorbent assay detection of MI-CBP-1 in stylet secretions of second-stage juveniles with the polyclonal antibodies indicated MI-CBP-1 could be secreted through the nematodes' stylet, suggesting that the cellulose-binding protein may have a role in pathogenesis.