Identification and characterization of excreted-secreted products and surface coat antigens of animal and plant-parasitic nematodes

Parasitology

Volumn 118, Issue 4, 1999, Pages 397-405

  Lopez De Mendoza, M E ^a   Curtis, R H C ^a   Gowen, S ^b  

^a ROTHAMSTED RESEARCH   (United Kingdom)

^b UNIVERSITY OF READING   (United Kingdom)

Author keywords

Excreted secreted products; Haemonchus contortus; Meloidogyne incognita; Monoclonal antibodies; Surface coat; Trichinella spiralis

Indexed keywords

MEMBRANE ANTIGEN; MONOCLONAL ANTIBODY; SECRETORY PROTEIN;

ANTIGEN RECOGNITION; ARTICLE; CELL SECRETION; CONTROLLED STUDY; CROSS REACTION; ESOPHAGUS; HAEMONCHUS CONTORTUS; IMMUNOFLUORESCENCE; INTESTINE; NEMATODE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN LOCALIZATION; TRICHINELLA SPIRALIS;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTIGENS, HELMINTH; BLOTTING, WESTERN; ELECTROPHORESIS, POLYACRYLAMIDE GEL; EPITOPES; FEMALE; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; HAEMONCHUS; HELMINTH PROTEINS; PLANT DISEASES; TRICHINELLA SPIRALIS; TYLENCHOIDEA;

ANIMALIA; HAEMONCHUS CONTORTUS; MELOIDOGYNE INCOGNITA; NEMATODA; TRICHINELLA SPIRALIS;

EID: 0032916793     PISSN: 00311820     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0031182098003941     Document Type: Article

References (33)

1. Appleton, J. A. & Usack, L. (1993). Identification of potential antigenic targets for rapid expulsion of Trichinella spiralis. Molecular and Biochemical Parasitology 58, 53-62.
2. Ashman, K., Mather, J., Wilshire, C., Jacobs, H. I. & Meesen, E. (1995). Isolation of larval surface glycoprotein form Haemonchus contortus and its possible role in evading host immunity. Molecular and Biochemical Parasitology 70, 175-179.
3. Bird, D. (1992). Mechanism of Meloidogyne host interaction. In Nematology from Molecular to Ecosystem, (ed. Gommers, F. J. & Maas, P. W. Th.), pp. 51-59. European Society of Nematology, Dundee, Scotland.
4. Bradford, M. M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilising the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
5. Cox, G. N., Shamansky, L. M. & Boisvenue, R. J. (1989). Identification and preliminary characterisation of cuticular surface proteins of Haemonchus contortus. Molecular and Biochemical Parasitology 36, 233-242.
6. Curtis, R. H. (1996). Identification and in situ and in vitro characterization of secreted proteins produced by plant-parasitic nematodes. Parasitology 113, 589-593.
7. Denkers, E. Y., Wassom, D. L., Krco, C. J. & Hayes, E. (1990). The mouse antibody response to Trichinella spiralis defines a single, immunodominant epitope shared by multiple antigens. Journal of Immunology 144, 3152-3159.
8. Despommier, D. D. (1983). Biology. In Trichinella and Trichinosis (ed. Campbell, W. C.), pp. 31-73. Plenum Press, New York.
9. 1, larvae localises to the cytoplasm and nucleoplasm of infected host cell. Experimental Parasitology 71, 27-38.
10. Devaney, E. & Jecock, R. M. (1991). The expression of the Mr 30000 antigen in the third stage larvae of Brugia pahangi. Parasite Immunology 13, 75-87.
11. Endo, B. V. & Wyss, U. (1992). Ultrastructure of cuticular exudations in parasitic juvenile Heterodera schachtii, as related to cuticle structure. Protoplasma 166, 67-77.
12. Gamble, H. R., Purcell, J. P. & Fetterer, R. H. (1989). Purification of a 44 kilodalton protease which mediates the ecdysis of infective Haemonchus contortus larvae. Molecular and Biochemical Parasitology 33, 49-58.
13. Gravato-Nobre, M. J. (1996). The importance of plant/nematode surface interactions in the infection of Arabidopsis thaliana by Meloidogyne incognita. Ph.D thesis. University of Nottingham.
14. Homan, W. L., Derksen, A. C. G. & Van Knapen, F. (1992). Identification of diagnostic antigens from Trichinella spiralis. Parasitology Research 78, 112-119.
15. Hussey, R. S. (1992). Secretions of esophageal glands in root-knot nematodes. In Nematology from Molecule to Ecosystem (ed. Gommers, F. J. & Maas, P. W. Th.), pp. 41-50. European Society of Nematology, Dundee, Scotland.
16. Jasmer, D. P., Yao, S. F., Vassilatis, D., Despommier, D. & Neary, S. M. (1994). Failure to detect Trichinella spiralis P43 in isolated host nuclei and in irradiated larvae of infected muscle-cells which express the infected cell phenotype. Molecular and Biochemical Parasitology 67, 225-234.
17. Kehayov, I. R., Kyukchiev, S. D., Tankov, C. V. & Komandarev, S. K. (1991). Trichinella spiralis: A 76- kDa excretory-secretory larval antigen identified by a monoclonal antibody. Experimental Parasitology 73, 150-160.
18. Kyhse-Andersen, J. (1984). Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. Journal of Biochemical and Biophysical Methods 10, 203-209.
19. Ko, R. C., Fan, L., Lee, D. L. & Compton, H. (1994). Changes in host muscles induced by excretory/secretory products of larval Trichinella spirallis and Trichinella pseudospiralis. Parasitology 108, 195-205.
20. Lee, D. L., Ko, R. C., Yi, X. Y. & Yeung, M. H. F. (1991). Trichinella spiralis: antigenic epitopes from the stichocytes detected in hypertrophie nuclei and cytoplasm of the parasitized muscle fibre (nurse cell) of the host. Parasitology 102, 117-123.
21. Lee, D. L. & Shivers, R. R. (1987). A freeze-fracture study of muscle fibres infected with Trichinella spiralis. Tissue and Cell 19, 665-671.
22. Ortega-Pierres, G., Mackenzie, C. D. Parkhouse, R. M. E. (1984). Protection against Trichinella spiralis induced by a monoclonal antibody that promotes killing of newborn larvae by granulocytes. Parasite Immunology 6, 275-284.
23. Philipp, M. R., Parkhouse, M. E. & Ogilvie, B. M. (1980). Changing proteins on the surface of a parasitic nematode. Nature, London 287, 538-540.
24. Philipp, M. R., Taylo, P. M., Parkhouse, M. E. & Ogilvie, B. M. (1981). Immune response to stage- specific surface antigens of the parasitic nematode Trichinella spiralis. Journal of Experimental Medicine 154, 210-215.
25. Robertson, W. M., Spiegel, Y., Jansson, H. B., Marban-Mendoza, N. & Zuckerman, B. M. (1989). Surface carbohydrates of plant parasitic nematodes. Nematologica 35, 180-186.
26. Schallig, H. D. F., Van Leewen, M. A. W. & Hendrix, W. M. L. (1994). Immune responses of Texel sheep to excretory-secretory products of adult Haemonchus contortus. Parasitology 108, 351-357.
27. Shamansky, L. M., Prat, D., Boisvenue, R. J. & Cox, G. N. (1989). Cuticle collagen genes of Haemonchus contortus and Caenorhabditis elegans are highly conserved. Molecular and Biochemical Parasitology 37, 73-86.
28. Spiegel, Y. & McClure, M. A. (1995). The surface-coat of plant-parasitic nematodes - chemical composition, origin and biological role a review. Journal of Nematology 27, 127-134.
29. Towbin, H., Staehelin, T. & Gordon, J. (1979). Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proceedings of the National Academy of Sciences, USA 76, 4350-4354.
30. Turcekova, L., Boroskova, Z., Tomasovicova, O., Reiterova, K. & Kincekova, J. (1997).Immunochemical analysis of larval antigens of Trichinella spiralis and T. pseudospiralis. Helminthologia 34, 241-243.
31. Vassilatis, D. K., Despommier, D. D., Polvere, R. I., Gold, A. M. & Van Der Ploeg, L. H. T. (1996). Trichinella pseudospiralis secretes a protein related to the Trichinella spiralis 43-kDa glycoprotein. Molecular and Biochemical Parasitologv 78, 25-31.
32. Vassilatis, D. K., Despommier, D., Misek, D. F., Polvere, R. I., Gold, A. M. & Van Der Ploeg, L. H. T. (1992).Analysis of a 43-kDa glycoprotein from the intracellular parasitic nematode Trichinella spiralis. Journal of Biological Chemistry 267, 18459-18465.
33. Woodward, M. P., Young, W. W. Jr. & Bloodgood, R. A. (1985). Detection of monoclonal antibodies specific for carbohydrate epitopes using periodate oxidation. Journal of Immunological Methods 78, 143-153.