Construction and expression of a bifunctional single-chain antibody against Bacillus cereus Spores

Applied and Environmental Microbiology

Volumn 64, Issue 7, 1998, Pages 2490-2496

  Koo, Kai ^a   Foegeding, Peggy M ^a   Swaisgood, Harold E ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIUM ANTIBODY; MONOCLONAL ANTIBODY; RNA POLYMERASE;

ANIMAL CELL; ARTICLE; BACILLUS CEREUS; BACTERIAL SPORE; BACTERIOPHAGE T7; CONTROLLED STUDY; FOOD PROCESSING; FOOD SAFETY; FOOD SPOILAGE; MOLECULAR CLONING; MOUSE; NONHUMAN; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

ANIMALIA; BACILLUS CEREUS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0031868030     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.7.2490-2496.1998     Document Type: Article

References (45)

1. Bassam, B. J., G. Caetano-Anolles, and P. M. Gresshoff. 1991. Fast and sensitive silver staining of DNA in polyacrylamide gels. Anal. Biochem. 196:80-83.
2. Berry, M. J., J. Davies, C. G. Smith, and I. Smith. 1991. Immobilization of Fv antibody fragments on porous silica and their utility in affinity chromatography. J. Chromatogr. 587:161-169.
3. Bird, R. E., K. D. Hardman, J. W. Jacobson, S. Johnson, B. M. Kaufman, S.-M. Lee, T. Lee, S. H. Pope, G. S. Riordan, and M. Whitlow. 1988. Single-chain antigen-binding proteins. Science 242:423-426.
4. Boyd, D., and J. Beckwith. 1990. The role of charged amino acids in the localization of secreted and membrane proteins. Cell 62:1031-1033.
5. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
6. Canaan-Haden, L., M. Ayala, M. E. Fernandez-de-Cossio, I. Pedroso, L. Rodes, and J. V. Cavilondo. 1995. Purification and application of a single-chain Fv antibody fragments specific to hepatitis B virus surface antigen. BioTechniques 19:606-613.
7. Carrier, A., F. Ducancel, N. B. Settiawan, L. Cattolico, B. Maillere, M. Leonetti, P. Drevet, A. Menez, and J. Boulain. 1995. Recombinant antibody-alkaline phosphatase conjugates for diagnosis of human IgGs: application to anti-HBsAg detection. J. Immunol. Methods 181:177-186.
8. Carroll, W. L., E. Mendel, and S. Levy. 1988. Hybridoma fusion cell lines contain an aberrant kappa transcript. Mol. Immunol. 25:991-995.
9. Christiansson, A. 1992. The toxicology of Bacillus cereus. Bull. Int. Dairy Fed. 275:30-35.
10. Chung, C. T., S. L. Niemela, and R. H. Miller. 1989. One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc. Natl. Acad. Sci. USA 86:2172-2175.
11. Clackson, T., H. R. Hoogenboom, A. D. Griffiths, and G. Winter. 1991. Making antibody fragments using phage display libraries. Nature 352:624-628.
12. Crielly, E. M., N. A. Logan, and A. Anderton. 1994. Studies on the Bacillus flora of milk and milk products. J. Appl. Bacteriol. 77:256-263.
13. Georgiou, G., J. N. Telford, M. L. Shuler, and D. B. Wilson. 1986. Localization of inclusion bodies in Escherichia coli overproducing β-lactamase or alkaline phosphatase. Appl. Environ. Microbiol. 52:1157-1161.
14. Glockshuber, R., M. Malia, I. Pfitzinger, and A. Pluckthun. 1990. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry 29:1362-1367.
15. Gottlieb, P. D. 1980. Immunoglobulin genes. Mol. Immunol. 17:1423-1435.
16. Huston, J. S., D. Levinson, M. Mudgett-Hunter, M.-S. Tai, J. Novotny, M. N. Margolies, R. J. Ridge, R. E. Bruccoleri, E. Haber, R. Crea, and H. Oppermann. 1988. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 85:5879-5883.
17. Huston, J. S., M. Mudgett-Hunter, M.-S. Tai, J. McCartney, F. Warren, E. Haber, and H. Oppermann. 1991. Protein engineering of single-chain Fv analogs and fusion proteins. Methods Enzymol. 203:46-88.
18. Johnson, K. M., C. L. Nelson, and F. F. Busta. 1982. Germination and heat resistance of Bacillus cereus spores from strains associated with diarrheal and emetic food-borne illnesses. J. Food Sci. 47:1268-1271.
19. Jones, S. T., and M. M. Bendig. 1991. Rapid PCR-cloning of full-length mouse immunoglobulin variable regions. Bio/Technology 9:88-89.
20. Kearney, J. F., A. Radbruch, B. Liesegang, and K. Rajewsky. 1979. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol. 123:1548-1550.
21. Keen, N. T., and S. Tamaki. 1986. Structure of two pectate lyase genes from Erwinia chrysanthemi EC16 and their high level expression in Escherichia coli. J. Bacteriol. 168:595-606.
22. Kipriyanov, S. M., G. Moldenhauer, and M. Little. 1997. High level production of soluble single chain antibodies in small-scale Escherichia coli cultures. J. Immunol. Methods 200:69-77.
23. Klein, P., M. Kanehisa, and C. DeLisi. 1985. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta 815:468-476.
24. Kretz, K., W. Callen, and V. Hedden. 1995. Cycle sequencing, p. 527-536. In C. W. Dieffenbach and G. S. Dveksler (ed.), PCR primer: a laboratory manual. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
25. Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
26. Lee, H. A., and M. R. A. Morgan. 1993. Food immunoassays: applications of polyclonal, monoclonal and recombinant antibodies. Trends Food Sci. Technol. 4:129-134.
27. Malby, R. L., J. B. Caldwell, L. C. Gruen, V. R. Barley, N. Ivancic, A. A. Kortt, G. G. Lilley, B. E. Power, R. G. Webster, P. M. Colman, and P. J. Hudson. 1993. Recombinant antineuraminidase single chain antibody: expression, characterization, and crystallization in complex with antigen. Proteins 16:57-63.
28. Maloy, S. R. 1990. Experimental techniques in bacterial genetics. Jones and Bartlett, Boston, Mass.
29. Marks, J. D., A. D. Griffiths, M. Malmqvist, T. P. Clackson, J. M. Bye, and G. Winter. 1992. By-passing immunization: building high affinity human antibodies by chain shuffling. Bio/Technology 10:779-783.
30. Molloy, P., L. Brydon, A. J. Porter, and W. J. Harris. 1995. Separation and concentration of bacteria with immobilized antibody fragments. J. Appl. Bacteriol. 78:359-365.
31. Neu, H. C., and L. A. Heppel. 1965. The release of enzymes from Escherichia coli by osmostic shock and during the formation of spheroplasts. J. Biol. Chem. 240:3685-3692.
32. Orlandi, R., D. H. Gussow, P. T. Jones, and G. Winter. 1989. Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. USA 86:3833-3837.
33. Owens, R. J., and R. J. Young. 1994. The genetic engineering of monoclonal antibodies. J. Immunol. Methods 168:149-165.
34. Phillips, T. M. 1992. Analytical techniques in immunochemistry, p. 263-300. Marcel Dekker, Inc., New York, N.Y.
35. Quinlan, J. J., and P. M. Foegeding. 1997. Monoclonal antibodies for use in detection of Bacillus and Clostridium spores. Appl. Environ. Microbiol. 63: 482-487.
36. Reiter, Y., U. Brinkmann, B. Lee, and I. Pastan. 1996. Engineering antibody Fv fragments for cancer detection and therapy: disulfide-stabilized Fv fragments. Nat. Biotechnol. 14:1239-1245.
37. Ross, G. W., and C. H. O'Callaghan. 1975. β-Lactamase assays. Methods Enzymol. 43:69-85.
38. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Plainview, N.Y.
39. Schmidt, T. G. M., and A. Skerra. 1993. The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment. Prot. Eng. 6:109-122.
40. Schmidt, T. G. M., and A. Skerra. 1994. One-step affinity purification of bacterially produced proteins by means of the "strep tag" and immobilized recombinant core streptavidin. J. Chromatogr. Ser. A 676:337-345.
41. Skerra, A., and A. Pluckthun. 1988. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240:1038-1041.
42. Studier, F. W., A. H. Rosenberg, J. J. Dunn, and J. W. Dubendorff. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:60-89.
43. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
44. Wels, W., I. Harwerth, M. Zwickl, N. Hardman, B. Groner, and N. E. Hynes. 1992. Construction, bacterial expression and characterization of a bifunctional single-chain antibody-phosphatase fusion protein targeted to human erbb-2 receptor. Bio/Technology 10:1128-1132.
45. Yamane, K., and S. Mizushima. 1988. Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 263:19690-19696.