Functional characterisation of a cyst nematode acetylcholinesterase gene using Caenorhabditis elegans as a heterologous system

2009 ◽  
Vol 39 (7) ◽  
pp. 849-858 ◽  
Author(s):  
Joana C. Costa ◽  
Catherine J. Lilley ◽  
Howard J. Atkinson ◽  
Peter E. Urwin
Nematology ◽  
2000 ◽  
Vol 2 (8) ◽  
pp. 887-893 ◽  
Author(s):  
John Jones ◽  
Vivian Blok ◽  
Geert Smant

AbstractA family of secreted proteins (the SXP/RAL-2 proteins) has been identified in animal parasitic nematodes and Caenorhabditis elegans. In this paper, we describe two full length cDNA sequences from the potato cyst nematode Globodera rostochiensis which could encode proteins similar to SXP/ RAL-2 proteins. We show that although both genes are expressed in second stage juveniles and in sedentary females of G. rostochiensis, they have remarkably different spatial expression patterns. The mRNA derived from one of the genes (gr-sxp-1) was present in the hypodermis, as has been described previously for one of these genes in an animal parasitic nematode. However, expression of the mRNA from the other gene was restricted to the gland cells surrounding the amphidial sense organs (the sheath cells). In addition to providing the first description of SXP proteins from a plant parasitic nematode, this work provides the first detailed characterisation of a protein secreted from the amphids of a plant parasite. Les protéines SXP/ RAL-2 du nématode à kyste de la pomme de terre Globodera rostochiensis : les protéines sécrétées par l'hypoderme et les amphides - Une famille de protéines sécrétées - les protéines SXP/RAL-2 - avait déjà été identifiée chez les nématodes zooparasites et chez Caenorhabditis elegans. Dans cet article nous décrivons deux séquences en longueur totale de cADN provenant du nématode à kyste de la pomme de terre Globodera rostochiensis, séquences qui pourraient coder des protéines similaires aux protéines SXP/RAL-2. Nous montrons que, bien que l'un et l'autre gène s'expriment chez les juvéniles de deuxième stade et chez les femelles sédentaires de Globodera rostochiensis, ils possèdent des profils d'expression spatiale remarquablement différents. Le rARN dérivé à partir d'un de ces gènes (gr-sxp-1) était présent dants l'hypoderme, comme cela avait déjà été décrit pour l'un de ces gènes chez un nématode zooparasite. Cependant, l'expression du mRNA de l'autre gène était limitée aux cellules glandulaires entourant les organes sensoriels amphidiens (les cellules de la gaine). Offrant la première description de protéines SXP provenant de nématodes phytopathogènes, le présent travail fournit de plus la première caractérisation détaillée d'une protéine sécrétée par les amphides d'un nématode parasite de plantes.


2000 ◽  
Vol 111 (1) ◽  
pp. 41-49 ◽  
Author(s):  
Lee Robertson ◽  
Walter M Robertson ◽  
Miroslaw Sobczak ◽  
Johannes Helder ◽  
Emmanuel Tetaud ◽  
...  

1996 ◽  
Vol 109 (11) ◽  
pp. 2661-2672 ◽  
Author(s):  
M. Goedert ◽  
C.P. Baur ◽  
J. Ahringer ◽  
R. Jakes ◽  
M. Hasegawa ◽  
...  

Tau, MAP2 and MAP4 are structural microtubule-associated proteins (MAPs) that promote the assembly and stability of microtubules. They share three or four imperfect tandem repeats of an amino acid motif, which is involved in the binding to microtubules. All sequences to data containing this motif are of mammalian origin. We report here the cloning and functional characterisation of a new member of this family of proteins from the nematode Caenorhabditis elegans. This protein exists as two isoforms of 413 and 453 amino acids with four or five tandem repeats that are 50% identical to the tau/MAP2/MAP4 repeats. Both isoforms bind to microtubules and promote microtubule assembly, with the five-repeat isoform being more effective at promoting assembly than the four-repeat isoform. When expressed in COS cells, the five-repeat isoform co-localises with microtubules and induces the formation of microtubule bundles, whereas its expression in Sf9 cells leads to the extension of long unipolar processes. In view of its length, amino acid sequence and functional characteristics, we have named this invertebrate structural MAP ‘Protein with Tau-Like Repeats’ (PTL-1). In C. elegans PTL-1 is expressed in two places known to require microtubule function. It is first seen in the embryonic epidermis, when circumferentially oriented microtubules help to distribute forces generated during elongation. Later, it is found in mechanosensory neurons which contain unusual 15 protofilament microtubules required for the response to touch. These findings indicate that MAPs of the tau/MAP2/MAP4 family are found throughout much of the animal kingdom, where they may play a role in specialised processes requiring microtubules.


2002 ◽  
Vol 69 ◽  
pp. 117-134 ◽  
Author(s):  
Stuart M. Haslam ◽  
David Gems ◽  
Howard R. Morris ◽  
Anne Dell

There is no doubt that the immense amount of information that is being generated by the initial sequencing and secondary interrogation of various genomes will change the face of glycobiological research. However, a major area of concern is that detailed structural knowledge of the ultimate products of genes that are identified as being involved in glycoconjugate biosynthesis is still limited. This is illustrated clearly by the nematode worm Caenorhabditis elegans, which was the first multicellular organism to have its entire genome sequenced. To date, only limited structural data on the glycosylated molecules of this organism have been reported. Our laboratory is addressing this problem by performing detailed MS structural characterization of the N-linked glycans of C. elegans; high-mannose structures dominate, with only minor amounts of complex-type structures. Novel, highly fucosylated truncated structures are also present which are difucosylated on the proximal N-acetylglucosamine of the chitobiose core as well as containing unusual Fucα1–2Gal1–2Man as peripheral structures. The implications of these results in terms of the identification of ligands for genomically predicted lectins and potential glycosyltransferases are discussed in this chapter. Current knowledge on the glycomes of other model organisms such as Dictyostelium discoideum, Saccharomyces cerevisiae and Drosophila melanogaster is also discussed briefly.


1998 ◽  
Vol 3 (1) ◽  
pp. 6-10 ◽  
Author(s):  
Glenda A Walker ◽  
David W Walker ◽  
Gordon J Lithgow

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