no difference in ace1 but 18 non synonymous amino acid differences in ace2 were found in the fosthiazate resistance strain of Melidgyne incognita Huang et al. 2016
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Nematoda: NE > Chromadorea: NE > Tylenchida: NE > Tylenchina: NE > Tylenchoidea: NE > Meloidogynidae: NE > Meloidogyninae: NE > Meloidogyne: NE > Meloidogyne incognita group: NE > Meloidogyne incognita: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MMDYSIEDRKRIKSLKTNNGFCLSLRHLLYFPFVFLSQYVVSAAVYVNLS DGSPIFGSFVQAATGKYISQFLGVPFAEPPIGKLRFRRPIPKRPWREQWN ATTFRDSCVQSPDTYFGDFYGATMWNSNTPCSEDCLYLNIYVPGEIDREK RLPVLFWIYGGGFWSGTASLDVYDGKIFAGEENVIIVTVNYRVTVFGFLY LGREEAPGNMGLWDQLLALKWVYKNIQVFGGDPSLITLFGESAGGASVSM HMLSPLSQPYFTRSILQSGAATAPWAVENKQVALHRAVILYEYMKCGNGN MSHLAPDQWNMDEVLRCLHAASADKLRDSEWSPVMEFADFPWVPVIDGEF LVENIETSLKRGNFKKTQLLAGSNFDEAIYFIVYQLADVFPPAEFFEKKD FIKSRDVWIKSVSSLLPRQILKSSLALQSILNYYEPEGLPIESKNWVDSL DKMLGDFLFTCNVNEFALAHSEHGADTYYYMFSHRASQQTWPEWMGVLHG YEINFIFGEPYNRKQFKYTKEEQELSSRFMRFWANFARTGDPNRNPDNSY ISDWPPYNSKTMEYINLTIESDYIQKGARRIGTGPRRKHCNFWKFIPKLI SISADLGESFIKWKQQMDRWENDYMPEWENHFEQYKRHQMYRIKDEVGDN DVCGIK
References
Title: Expression and evolutionary analyses of three acetylcholinesterase genes (Mi-ace-1, Mi-ace-2, Mi-ace-3) in the root-knot nematode Meloidogyne incognita Cui R, Zhang L, Chen Y, Huang W, Fan C, Wu Q, Peng D, da Silva W, Sun X Ref: Experimental Parasitology, 176:75, 2017 : PubMed
The full cDNA of Mi-ace-3 encoding an acetylcholinesterase (AChE) in Meloidogyne incognita was cloned and characterized. Mi-ace-3 had an open reading frame of 1875 bp encoding 624 amino acid residues. Key residues essential to AChE structure and function were conserved. The deduced Mi-ACE-3 protein sequence had 72% amino acid similarity with that of Ditylenchus destructor Dd-AChE-3. Phylogenetic analyses using 41 AChEs from 24 species showed that Mi-ACE-3 formed a cluster with 4 other nematode AChEs. Our results revealed that the Mi-ace-3 cloned in this study, which is orthologous to Caenorhabditis elegans AChE, belongs to the nematode ACE-3/4 subgroup. There was a significant reduction in the number of galls in transgenic tobacco roots when Mi-ace-1, Mi-ace-2, and Mi-ace-3 were knocked down simultaneously, whereas little or no effect were observed when only one or two of these genes were knocked down. This is an indication that the functions of these three genes are redundant.
Title: Mutations in Acetylcholinesterase2 (ace2) increase the insensitivity of acetylcholinesterase to fosthiazate in the root-knot nematode Meloidogyne incognita Huang WK, Wu QS, Peng H, Kong LA, Liu SM, Yin HQ, Cui RQ, Zhan LP, Cui JK, Peng DL Ref: Sci Rep, 6:38102, 2016 : PubMed
The root-knot nematode Meloidogyne incognita causes severe damage to continuously cropping vegetables. The control of this nematode relies heavily on organophosphate nematicides in China. Here, we described resistance to the organophosphate nematicide fosthiazate in a greenhouse-collected resistant population (RP) and a laboratory susceptible population (SP) of M. incognita. Fosthiazate was 2.74-fold less toxic to nematodes from RP than that from SP. Quantitative real-time PCR revealed that the acetylcholinesterase2 (ace2) transcription level in the RP was significantly higher than that in the SP. Eighteen nonsynonymous amino acid differences in ace2 were observed between the cDNA fragments of the RP and SP. The acetylcholinesterase (AChE) protein activity in the RP was significantly reduced compared with that in the SP. After knocking down the ace2 gene, the ace2 transcription level was significantly decreased, but no negative impact on the infection of juveniles was observed. The 50% lethal concentration of the RNAi RP population decreased 40%, but the inhibition rate of fosthiazate against AChE activity was significantly increased in RP population. Thus, the increased fosthiazate insensitivity in the M. incognita resistant population was strongly associated with mutations in ace2. These results provide valuable insights into the resistance mechanism of root-knot nematode to organophosphate nematicides.
Title: Molecular cloning of an acetylcholinesterase gene from the plant parasitic nematodes, Meloidogyne incognita and Meloidogyne javanica Piotte C, Arthaud L, Abad P, Rosso MN Ref: Molecular & Biochemical Parasitology, 99:247, 1999 : PubMed
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.
