Piotte C, Arthaud L, Abad P, Rosso M N
Laboratoire de Biologie des Invertébrés, INRA, Antibes, France.
Mol Biochem Parasitol. 1999 Apr 30;99(2):247-56. doi: 10.1016/s0166-6851(99)00033-x.
A gene encoding a protein with strong homology with Caenorhabditis elegans and C. briggsae acetylcholinesterase ACE-1 was cloned from Meloidogyne incognita and M. javanica pre-parasitic juveniles. Both cDNAs have an ORF of 1968 bp for a deduced translation product of 656 amino acid residues. The key residues essential to acetylcholinesterase (AChE) structure and function are conserved in both sequences. M. incognita and M. javanica AChE share a homology of 98.8% at the amino acid level and 97% at the nucleotide level. Phylogenetic analysis showed that Meloidogyne and Caenorhabditis AChE form a cluster among AChE of triploblastic organisms. This Meloidogyne AChE is expressed in eggs, pre-parasitic juveniles and males and AChE activity was detected in situ in amphids of pre-parasitic juveniles. The opportunity of using AChE as a target in new strategies of nematode control is discussed.
从南方根结线虫和爪哇根结线虫的寄生前期幼虫中克隆出一个基因，该基因编码的蛋白质与秀丽隐杆线虫和briggsae乙酰胆碱酯酶ACE-1具有高度同源性。两个cDNA的开放阅读框（ORF）均为1968 bp，推导的翻译产物为656个氨基酸残基。乙酰胆碱酯酶（AChE）结构和功能所必需的关键残基在两个序列中均保守。南方根结线虫和爪哇根结线虫的AChE在氨基酸水平上的同源性为98.8%，在核苷酸水平上为97%。系统发育分析表明，根结线虫和秀丽隐杆线虫的AChE在三胚层生物的AChE中形成一个簇。这种根结线虫AChE在卵、寄生前期幼虫和雄虫中表达，并且在寄生前期幼虫的化感器中原位检测到AChE活性。本文还讨论了将AChE作为线虫防治新策略靶点的可能性。
