Cloning and expression of two secretory acetylcholinesterases from the bovine lungworm, Dictyocaulus viviparus

Molecular and Biochemical Parasitology

Volumn 132, Issue 2, 2003, Pages 83-92

  Lazari, Ovadia ^a   Hussein, Ayman S ^b   Selkirk, Murray E ^b   Davidson, Amanda J ^a   Thompson, Fiona J ^c   Matthews, Jacqueline B ^a  

^a UNIVERSITY OF LIVERPOOL   (United Kingdom)

^b IMPERIAL COLLEGE LONDON   (United Kingdom)

^c UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Acetylcholinesterase; Dictyocaulus viviparus; Nematode

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINESTERASE; ACETYLCHOLINESTERASE 1; ACETYLCHOLINESTERASE 2; RECOMBINANT ENZYME; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CONTROLLED STUDY; DICTYOCAULUS VIVIPARUS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME GLYCOSYLATION; ENZYME SPECIFICITY; ISOENZYME ANALYSIS; MOLECULAR CLONING; NEMATODE; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; WORM;

BOVINAE; CAENORHABDITIS; CAENORHABDITIS ELEGANS; DICTYOCAULUS; DICTYOCAULUS VIVIPARUS; INSERTION SEQUENCES; PICHIA; PICHIA PASTORIS; VIVIPARUS;

EID: 0242266564     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2003.09.001     Document Type: Article

References (33)

1. Ogilvie B.M., Rothwell T.L., Bremner K.C., Schnitzerling H.J., Nolan J., Keith R.K. Acetylcholinesterase secretion by parasitic nematodes. I. Evidence for secretion of the enzyme by a number of species. Int. J. Parasitol. 3:1973;589-597.
2. McLaren D.J., Burt J.S., Ogilvie B.M. The anterior glands of adult Necator americanus (Nematoda: Strongyloidea). II. Cytochemical and functional studies. Int. J. Parasitol. 4:1974;39-46.
3. Pritchard D.I., Leggett K.V., Rogan M.T., McKean P.G., Brown A. Necator americanus secretory acetylcholinesterase and its purification from excretory-secretory products by affinity chromatography. Parasite Immunol. 13:1991;187-199.
4. Rhoads M.L. Cholinesterase in the parasitic nematode Stephanurus dentatus. Characterisation and sex dependence of a secretory cholinesterase. J. Biol. Chem. 256:1981;9316-9323.
5. McKeand J.B., Knox D.P., Duncan J.L., Kennedy M.W. The immunogenicity of the acetylcholinesterases of the cattle lungworm, Dictyocaulus viviparus. Int. J. Parasitol. 24:1994;501-510.
6. Lee D.L. Why do some nematode parasites of the alimentary tract secrete acetylcholinesterase? Int. J. Parasitol. 26:1996;499-508.
7. Hussein A.S., Harel M., Selkirk M.E. A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis. Mol. Biochem. Parasitol. 28:2002;125-134.
8. Combes D., Fedon Y., Grauso M., Toutant J.P., Arpagaus M. Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression. J. Mol. Biol. 300:2000;727-742.
9. Massoulié J., Anselmet A., Bon S., Krejci E., Legay C., Morel N. et al. Acetylcholinesterase: C-terminal domains, molecular forms and functional localisation. J. Physiol. 92:1998;183-190.
10. McKeand J.B., Knox D.P., Duncan J.L., Kennedy M.W. Genetic control of the antibody repertoire against excretory/secretory products and acetylcholinesterases of Dictyocaulus viviparus. Parasite Immunol. 16:1994;251-260.
11. Arpagaus M., Fedon Y., Cousin X., Chatonnet A., Berge J.B., Fournier D. et al. cDNA sequence, gene structure, and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans. J. Biol. Chem. 269:1994;9957-9965.
12. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nuc. Acids Res. 22:1994;4670-4680.
13. Massoulié J, Sussman JL, Doctor BP, Soreq H, Velan B, Cygler M, Rotundo R, Shafferman A, Silman I, Taylor P. In: Shafferman A, Velan B, editors. Multidisciplinary approaches to cholinesterase functions. New York: Plenum Press; 1992. p. 29-36.
14. Giles K. Interactions underlying subunit association in cholinesterases. Protein Eng. 10:1997;677-685.
15. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis. 18:1997;2714-2723.
16. Hussein A.S., Chacón M.R., Smith A.M., Tosado-Acevedo R., Selkirk M.E. Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. J. Biol. Chem. 274:1999;9312-9319.
17. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7:1961;88-95.
18. Grunder A.A., Sartori G., Stormont C. Genetic variation in red cell esterases of rabbits. Genetics. 52:1965;1345-1353.
19. Hodgkinson J.E., Love S., Lichtenfels J.R., Ramsey Y.R., Palfreman S., Matthews J.B. Evaluation of the specificity of five oligoprobes for identification of cyathostomin species from horses. Int. J. Parasitol. 31:2001;197-204.
20. Krause M., Hirsh D. A trans-spliced leader sequence on actin mRNA in Caenorhabditis elegans. Cell. 49:1987;753-761.
21. Huang X.Y., Hirsh D. A second trans-spliced RNA leader in the nematode Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 86(22):1989;8460-8644.
22. Schumacher M., Camp S., Maulet Y., Newton M., MacPhee-Quigley K., Taylor S.S.et al. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature. 319:1986;407-409.
23. Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L.et al. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholinebinding protein. Science. 253:1991;872-879.
24. Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C. et al. Quaternary ligand binding to aromatic residues in the active site gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA. 90:1993;9031-9035.
25. Massoulié J. The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals. 11:2002;130-143.
26. Cousin X., Bon S., Duval N., Massoulié J., Bon C. Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain: involvement of a positively charged residue in the peripheral site. J. Biol. Chem. 271:1996;15099-15108.
27. Nalivaeva NN, Turner AJ. Post-translational modifications of proteins: acetylcholinesterase as a model. Proteomics 2001:735-47.
28. Harel M., Sussman J.L., Krejci E., Bon S., Chanal P., Massoulié J.et al. Conversion of acetylcholinesterase to butyrylcholinesterase: modelling and mutagenesis. Proc. Natl. Acad. Sci. USA. 89:1992;10827-10831.
29. Vellom D.C., Radic Z., Li Y., Pickering N.A., Camp S., Taylor P. Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry. 32:1993;12-17.
30. Ordentlich A., Barak D., Kronman C., Flashner Y., Leitner M., Segall Y. et al. Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket. J. Biol. Chem. 268:1993;17083-17095.
31. Sato E., Koyama S., Okubo Y., Kubo K., Sekiguchi M. Acetylcholine stimulates alveolar macrophages to release inflammatory cell chemotactic activity. Am. J. Physiol. 274:1998;L970-L979.
32. Borovikova L.V., Ivanova S., Zhang M., Yang H., Botchkina G.I., Watkins L.R.et al. Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin. Nature. 405:2000;458-462.
33. Wang H., Yu M., Ochani M., Amella C.A., Tanovic M., Susarla S.et al. Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator of inflammation. Nature. 421:2003;384-388.