Characterization of a cDNA encoding a subtilisin-like serine protease (NC-p65) of Neospora caninum

Molecular and Biochemical Parasitology

Volumn 103, Issue 2, 1999, Pages 211-223

  Louie, Kitland ^a   Conrad, Patricia A ^a  

^a Immunol   (United States)

Author keywords

NC p65; Neospora caninum; Subtilase; Subtilisin like serine protease

Indexed keywords

SERINE PROTEINASE; SUBTILISIN; SYNAPTOTAGMIN;

AMINO ACID SEQUENCE; ARTICLE; DNA DETERMINATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; GENE AMPLIFICATION; MOLECULAR CLONING; NEOSPORA CANINUM; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; ZYMOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, PROTOZOAN; ANTIGENS, PROTOZOAN; BASE SEQUENCE; DNA, COMPLEMENTARY; MOLECULAR SEQUENCE DATA; NEOSPORA; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBTILISINS;

EID: 0032886822     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00127-9     Document Type: Article

References (52)

1. Thilsted J.P., Dubey J.P. Neosporosis-like abortions in a herd of dairy cattle. J. Vet. Diagn. Invest. 1:1989;205-209.
2. Anderson M.L., Blanchard P.C., Barr B.C., Dubey J.P., Hoffman R.L. Neospora-like protozoan infection as a major cause of abortion in California dairy cattle. J. Am. Vet. Med. Assoc. 198:1991;241-244.
3. Nietfeld J.C., Dubey J.P., Anderson M.L., Libal M.C., Yaeger M.J., Neiger R.D. Neospora-like protozoan infection as a cause of abortion in dairy cattle. J. Vet. Diagn. Invest. 4:1992;223-226.
4. Anderson M.L., Palmer C.W., Thurmond M.C. et al. Evaluation of abortions in cattle attributable to neosporosis in selected dairy herds in California. J. Am. Vet. Med. Assoc. 207:1995;1206-1210.
5. Barr B.C., Anderson M.L., Dubey J.P., Conrad P.A. Neospora-like protozoal infections associated with bovine abortions. Vet. Pathol. 28:1991;110-116.
6. Anderson M.L., Barr B.C., Conrad P.A. Protozoal causes of reproductive failure in domestic ruminants. Vet. Clin. N. Am. Food. Anim. Pract. 10:1994;439-461.
7. Barr B.C., Conrad P.A., Breitmeyer R. et al. Congenital Neospora infection in calves born from cows that had previously aborted Neospora-infected fetuses: Four cases (1990-1992). J. Am. Vet. Med. Assoc. 202:1993;113-117.
8. Anderson M.L., Reynolds J.P., Rowe J.D. et al. Evidence of vertical transmission of Neospora sp. infection in dairy cattle. J. Am. Vet. Med. Assoc. 210:1997;1169-1172.
9. Pare J., Thurmond M.C., Hietala S.K. Congenital Neospora caninum infection in dairy cattle and associated calfhood mortality. Can. J. Vet. Res. 60:1996;133-139.
10. Thurmond M.C., Hietala S.K. Effect of congenitally acquired Neospora caninum infection on risk of abortion and subsequent abortions in dairy cattle. Am. J. Vet. Res. 58:1997;1381-1385.
11. Wouda W., Moen A.R., Schukken Y.H. Abortion risk in progeny of cows after a Neospora caninum epidemic. Theriogenology. 49:1998;1311-1316.
12. Louie K., Sverlow K.W., Barr B.C., Anderson M.L., Conrad P.A. Cloning and characterization of two recombinant Neospora protein fragments and their use in serodiagnosis of bovine neosporosis. Clin. Diagn. Lab. Immunol. 4:1997;692-699.
13. Conrad P.A., Barr B.C., Sverlow K.W. et al. In vitro isolation and characterization of a Neospora sp. from aborted bovine foetuses. Parasitology. 106:1993;239-249.
14. Avis H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc. Natl. Acad. Sci. USA. 69:1972;1408-1412.
15. Altschul S.F., Gish W., Miller W., Myers E.W., Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215:1990;403-410.
16. Altschul S.F., Boguski M.S., Gish W., Wootton J.C. Issues in searching molecular sequence databases. Nat. Genet. 6:1994;119-129.
17. Pearson W.R., Lipman D. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. 85:1988;2444-2448.
18. Devereux J.R., Haeberli R., Smithies O. A comprehensive set of sequence analysis programs for the Vax. Nucleic Acids Res. 12:1984;387-395.
19. Kroll D.J., Abdel-Hafiz H.A., Marcell T. et al. A multifunctional prokaryotic protein expression system: overproduction, affinity purification, and selective detection. DNA Cell Biol. 12:1993;441-453.
20. Studier F.W., Rosenberg A.H., Dunn J.J., Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:1990;60-89.
21. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:1970;680-685.
22. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
23. Harlow E, Lane D. Antibodies: A Laboratory Manual. Cold Spring Harbor: Cold Spring Harbor Laboratory Press, 1988.
24. Lantz M.S., Ciborowski P. Zymographic techniques for detection and characterization of microbial proteases. Methods Enzymol. 235:1994;563-594.
25. Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 15:1987;8125-8132.
26. Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
27. Bairoch A., Bucher P. PROSITE: recent developments. Nucleic Acids Res. 22:1994;3583-3589.
28. Bucher P., Karplus K., Mooeri M., Hofmann K. A flexible motif search technique based on generalized profiles. Comput. Chem. 20:1996;3-23.
29. Pearson W.R. Effective protein sequence comparison. Methods Enzymol. 266:1997;227-259.
30. Bork P., Gibson T.J. Applying motif and profile searches. Methods Enzymol. 266:1996;162-184.
31. Siezen R.J., Leunissen J.A.M. Subtilases: The superfamily of subtilisin-like serine proteases. Protein Sci. 6:1997;501-523.
32. Blackman M.J., Fujioka H., Stafford W.H.L. et al. A subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoites. J. Biol. Chem. 273:1998;23398-23409.
33. Lechner S., Eschenbacher K., Entzeroth R., Mehlhorn H., Ruger W. cDNA clones of Sarcocystis muris (Apicomplexa) encoding a repetitive, arginine-rich region of a putative microneme antigen. Parasitol. Res. 80:1994;352-354.
34. Ossorio P.N., Schwartzman J.D., Boothroyd J.C. A Toxoplasma gondii rhoptry protein associated with host cell penetration has unusual charge asymmetry. Mol. Biochem. Parasitol. 50:1992;1-16.
35. Favaloro J.M., Coppel R.L., Corcoran L.M. et al. Structure of the RESA gene of Plasmodium falciparum. Nucleic Acids Res. 14:1986;8265-8277.
36. Kemp D.J., Coppel R.L., Anders R.F. Repetitive proteins and genes of malaria. Ann. Rev. Microbiol. 41:1987;181-208.
37. Nussenzweig V., Nussenzweig R.S. Circumsporozoite proteins of malaria parasites. Cell. 42:1985;401-403.
38. Rawlings N.D., Barrett A.J. Families of serine peptidases. Methods Enzymol. 244:1994;19-61.
39. Siezen RJ, Leunissen JAM, Shinde U. Homology analysis of the pre-peptides of subtilisin-like serine proteases (subtilases). In: Shinde U, editor. Intramolecular chaperones and folding. Austin: R.G. Landes Company, 1995, p. 231-53.
40. Wong S., Doi R.H. Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis. J. Biol. Chem. 261:1986;10176-10181.
41. Wells J.A., Ferrari E., Henner D.J., Estell D.A., Chen E.Y. Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis. Nucleic Acids Res. 11:1983;7911-7925.
42. Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D. Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein. J. Bacteriol. 159:1984;811-819.
43. Siezen R.J., de Vos W.M., Leunissen J.A.M., Dijkstra B.W. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteases. Protein Eng. 7:1991;719-737.
44. Cole R.A., Lindsay D.S., Dubey J.P., Toivio-Kinnucan M.A., Blagburn B.L. Characterization of a murine monoclonal antibody generated against Neospora caninum tachyzoites by use of western blot analysis and immunoelectron microscopy. Am. J. Vet. Res. 55:1994;1717-1722.
45. Suzuki M., Taguchi S., Yamada S., Kojima S., Miura K.I., Momose H. A novel member of the subtilisin-like protease family from Streptomyces albogriseolus. J. Bacteriol. 179:1997;430-438.
46. Russell A.J., Fersht A.R. Rational modification of enzyme catalysis by engineering surface charge. Nature (Lond.). 328:1987;496-500.
47. Brenner C., Fuller R.S. Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease. Proc. Natl. Acad. Sci. USA. 89:1998;922-926.
48. Forney J.R., Yang S., Du C., Healey M.C. Efficacy of serine protease inhibitors against Cryptosporidium parvum infection in a bovine fallopian tube epithelial cell culture system. J. Parasitol. 82:1996;638-640.
49. Bailly E., Jambou R., Savel J., Jaureguiberry G. Plasmodium falciparum: differential sensitivity in vitro to E-64 (cysteine protease inhibitor) and Pepstatin A (aspartyl protease inhibitor). J. Protozool. 39:1992;593-599.
50. Fuller A.L., McDougald L.R. Reduction in cell entry of Eimeria tenella (coccidia) sporozoites by protease inhibitors, and partial characterization of proteolytic activity associated with intact sporozoites and merozoites. J. Parasitol. 76:1990;464-467.
51. 33 as a noncovalently associated complex with other fragments of the MSP1. Mol. Biochem. Parasitol. 50:1992;307-316.
52. Blackman M.J., Scott-Finnigan T.J., Shai S., Holder A.A. Antibodies inhibit the protease-mediated processing of a malaria merozoite surface protein. J. Exp. Med. 180:1994;389-393.