Cloning, sequencing and expression of a cDNA encoding an antigen from the Myxosporean parasite causing the proliferative kidney disease of salmonid fish

Molecular and Biochemical Parasitology

Volumn 83, Issue 2, 1996, Pages 153-161

  Saulnier, Denis ^a   Brémont, Michel ^a   De Kinkelin, Pierre ^a  

^a CEMAGREF   (France)

Author keywords

antigenicity; cDNA sequence; Myxosporeans; PKX; recombinant proteins

Indexed keywords

COMPLEMENTARY DNA; MONOCLONAL ANTIBODY;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGENICITY; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; FISH; GENE EXPRESSION; IMMUNOBLOTTING; KIDNEY DISEASE; MOLECULAR CLONING; NONHUMAN; PARASITOSIS; PRIORITY JOURNAL; PROTOZOON; TROUT;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, PROTOZOAN; CLONING, MOLECULAR; DNA, COMPLEMENTARY; ESCHERICHIA COLI; FISH DISEASES; GENE EXPRESSION; KIDNEY DISEASES; MOLECULAR SEQUENCE DATA; ONCORHYNCHUS MYKISS; PROTOZOAN INFECTIONS; PROTOZOAN INFECTIONS, ANIMAL; RECOMBINANT FUSION PROTEINS; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA; ESCHERICHIA COLI; MYXOSPOREA; ONCORHYNCHUS MYKISS; PROTOZOA; SALMONIDAE; UNIDENTIFIED AGENTS;

EID: 0030596202     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(96)02761-2     Document Type: Article

References (30)

1. [1] Ferguson, H.W. and Adair, B. (1977) Protozoa associated with proliferative kidney disease in rainbow trout, Salmo gairdneri. Vet. Rec. 100, 158-159.
2. [2] Hedrick, R.P., Mac Connell, E. and de Kinkelin, P. (1993) Proliferative kidney disease of salmonid fish. In: Annual Rev. of Fish Diseases, VoI III (Faisal, M. and Hetrick, F., eds.), pp. 277-290. Pergamon Press. New York.
3. [3] Lom, J. (1987) Myxosporea a new look at long-known parasites of fish. Parasitol. Today 3, 327-332.
4. [4] Kent, M.L. and Hedrick, R.P. (1985) PKX, the causative agent of proliferative kidney disease (PKD) in Pacific salmonid fishes and its affinities with the Myxozoa. J. Protozool. 32, 254-260.
5. [5] Lom, J. (1989) Phylum Myxozoa. In: Hanbook of Protista (Margolis, L., Orliss, J.O., Melkonian, M. and Chapman, D.J. eds.), pp. 36-52. Jones and Bartlett. Boston.
6. [6] El-Matbouli, M., Fischer-Scherl, T. and Hoffmann, R. (1992) Present knowledge on the life cycle, taxonomy, pathology and therapy of some Myxosporea spp important for freshwater fish. In: Annual Rev. of Fish Diseases, Vol II (Faisal, M. and Hetrick, F. eds.) pp. 367-402. Pergamon Press. New York.
7. [7] Adams, A., Richards, R.H. and Marin de Mateo, M. (1992) Development of monoclonal antibodies to PKX, the causative agent of proliferative kidney disease. J. Fish Dis. 15, 515-521.
8. [8] Saulnier, D. and de Kinkelin, P. (1995) Antigenic and biochemical study of PKX, the myxosporean causative agent of proliferative kidney disease of salmonid fish. Dis. Aquat. Org. 27, 103-114
9. [9] Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
10. [10] D'Silva, J., Mulcahy, M.F. and de Kinkelin, P. (1984) Experimental transmission of proliferative kidney disease in rainbow trout, Salmo gairdneri Richardson. J. Fish Dis. 7, 235-239.
11. [11] Chomczynski, P. and Sacchi, N. (1987) Single step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
12. [12] Maniatis, T., Fritisch, E.F. and Sambrook, J. (1989) Molecular cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York.
13. [13] Young, R.A. and Davis, R.W. (1983) Efficient isolation of genes by using antibody probes. Proc. Natl. Acad. Sci. USA 80, 1194-1198.
14. [14] Blake, M.S., Johnston, K.H., Russell-Jones, G.J. and Gotschlich, E.G. (1984) A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on western-blots. Anal. Biochem. 136, 175-179.
15. [15] Short, J.L., Fernandez, J.M., Sorge, J.A. and Huse, W.D. (1988) λ ZAP: A bacteriophage with in vivo excision properties. Nucleic Acids Res. 16, 7583-7600.
16. [16] McCombie, W.R., Heiner, C., Kelley, J.M., Fitzgerald, M.G. and Gocayne, J.D. (1992) Rapid and reliable fluorescent cycle sequencing of double-stranded templates. DNA Seq. 2, 289-296.
17. [17] Genetics Computer Group (1991) Program manual for the GCG package, Version 7, April 1991, Madison, WI.
18. [18] Altschul, S.F., Gish W., Miller, W., Myers, E. and Lipman, D.J. (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
19. [19] Studier, F.W. and Moffatt, B.A. (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189, 113-120.
20. [20] DeLuca, D., Wilson, M. and Warr, G.W. (1983) Lymphocytes heterogeneity in the trout, Salmo gairdneri, defined with monoclonal antibodies to IgM. Eur. J. Immunol. 13, 546-551.
21. [21] McPherson, M.J., Quirke, P. and Taylor, G.R. (1992) PCR: A practical approach, Oxford University Press, Oxford.
22. [22] Walravens, K., Kettmann, R., Collard, A., Coppe, P. and Burny, A. (1990) sequence comparison between the fusion protein of human and bovine respiratory syncytial viruses. J. Gen. Virol. 71, 3009-3014.
23. [23] Favaloro, J.M., Coppel, R.L., Corcoran, L.M., Foote, S.J., Brown, G.V., Anders, R.F. and Kemp, D.J. (1986) Structure of the RESA gene of Plasmodium falciparum, Nucleic Acids Res. 14, 8265-8277.
24. [24] Weber, J.L. (1987) Analysis of sequences from the extremely A + T-rich genome of Plasmodium falciparum. Gene 52, 103-109.
25. [25] Landschulz, W.H., Johnson, P.F. and McKnight, S.L. (1988) The leucine zipper: A hypothetical structure common a new class of DNA binding protein. Science 240, 1759-1764.
26. [26] McCormack, K., Campanelli, J.T., Ramaswami, M., Mathew, M.K. and Tanouye, M.A. (1989) Leucine-zipper motif update. Nature 340, 103.
27. [27] Buckland, R. and Wild, F. (1989) Leucine zippers motif extends. Nature 338, 547.
28. [28] Hoop, M.J. and Geert, A.B. (1992) Import of proteins into peroxisomes and other microbodies. Biochem. J. 286, 657-669.
29. [29] Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292.
30. [30] Bonekamp, F. and Jensen, K.F. (1988) The AGG codon is translated slowly in E. coli even at low expression level. Nucleic Acids Res. 16, 3013-3024.