Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus
Cloning and characterization of pectate lyases expressed in the esophageal gland of the pine wood nematode Bursaphelenchus xylophilus
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DOI：
10.1094/mpmi-19-0280
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发表时间：
2006-03-01
影响因子：
3.5
通讯作者：
Jones, JT
中科院分区：
文献类型：
--
作者：
Kikuchi, T;Shibuya, H;Jones, JT
从松材线虫（Bursaphelenchusxylophilus）中克隆了两个果胶酸裂解酶基因（Bx-pel-1和Bx-pel-2）。这些果胶酸裂解酶的推导的氨基酸序列与多糖裂解酶家族3蛋白质最相似。重组BxPEL 1对多聚半乳糖醛酸的活性最高，对高度甲基化的果胶的活性较低。重组BxPEL 1表现出完全依赖于Ca 2+的活性和最佳活性在55 ℃和pH 8至10像其他果胶酸裂解酶的多糖裂解酶家族3。蛋白质序列在其N-末端具有预测的信号肽，并且该基因仅在线虫的食道腺细胞中表达，表明果胶酸裂解酶可以分泌到植物组织中以帮助在树中的摄食和迁移。本研究表明，果胶酸裂解酶在植物寄生线虫中广泛分布，并在植物-线虫互作中发挥重要作用。
Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xylophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55 degrees C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate Iyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.