Construction of a fusion protein carrying antigenic determinants of enteric clostridial toxins

FEMS Microbiology Letters

Volumn 225, Issue 2, 2003, Pages 325-329

  Belyi, Iouri F ^a   Varfolomeeva, Nina A ^a  

^a GAMALEYA RESEARCH INSTITUTE OF EPIDEMIOLOGY AND MICROBIOLOGY   (Russian Federation)

Author keywords

Clostridium; Enteric infection; Fusion protein; Immunization; Toxin

Indexed keywords

BACTERIAL VACCINE; CLOSTRIDIUM TOXIN; CLOSTRIDIUM VACCINE; EPITOPE; HYBRID PROTEIN; UNCLASSIFIED DRUG; VIRULENCE FACTOR; BACTERIAL PROTEIN; BACTERIAL TOXIN; BACTERIUM ANTIBODY; ENTEROTOXIN; ENTEROTOXIN, CLOSTRIDIUM; TCDA PROTEIN, CLOSTRIDIUM DIFFICILE; TOXB PROTEIN, CLOSTRIDIUM DIFFICILE;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIBODY SPECIFICITY; ANTIGENICITY; ARTICLE; BACTERIAL GENE; CHIMERA; CLOSTRIDIUM; CLOSTRIDIUM DIFFICILE; CLOSTRIDIUM PERFRINGENS; CONTROLLED STUDY; DATA ANALYSIS; ENTEROBACTERIACEAE; GENE CONSTRUCT; GENETIC ANALYSIS; IMMUNIZATION; INTESTINE INFECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; RABBIT; STRUCTURE ANALYSIS; ANIMAL; BLOOD; ENZYME LINKED IMMUNOSORBENT ASSAY; GENETICS; IMMUNOLOGY; ISOLATION AND PURIFICATION; MOLECULAR CLONING; MOUSE; PATHOGENICITY; POLYACRYLAMIDE GEL ELECTROPHORESIS; WESTERN BLOTTING;

CLOSTRIDIUM; CLOSTRIDIUM DIFFICILE; CLOSTRIDIUM PERFRINGENS; CLOSTRIDIUM PERFRINGENS A; ORYCTOLAGUS CUNICULUS;

ANIMALS; ANTIBODIES, BACTERIAL; BACTERIAL PROTEINS; BACTERIAL TOXINS; BLOTTING, WESTERN; CLONING, MOLECULAR; CLOSTRIDIUM DIFFICILE; CLOSTRIDIUM PERFRINGENS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENTEROTOXINS; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES; IMMUNIZATION; MICE; RABBITS; RECOMBINANT FUSION PROTEINS;

EID: 1642400628     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(03)00560-3     Document Type: Article

References (24)

1. Samore M.H. Epidemiology of nosocomial Clostridium difficile infection. Compr. Ther. 19:1993;151-156.
2. Asha N.J., Wilcox M.H. Laboratory diagnosis of Clostridium perfringens antibiotic-associated diarrhoea. J. Med. Microbiol. 51:2002;891-894.
3. Abrahao C., Carman R.J., Hahn H., Liesenfeld O. Similar frequency of detection of Clostridium perfringens enterotoxin and Clostridium difficile toxins in patients with antibiotic-associated diarrhea. Eur. J. Clin. Microbiol. Infect. Dis. 20:2001;676-677.
4. Kelly C.P., LaMont J.T. Clostridium difficile infection. Annu. Rev. Med. 49:1998;375-390.
5. McClane B.A. Clostridium perfringens enterotoxin: structure, action and detection. J. Food Saf. 12:1992;237-252.
6. Aktories K. Bacterial toxins that target Rho proteins. J. Clin. Invest. 99:1997;827-829.
7. Just I., Hofmann F., Aktories K. Molecular mode of action of the large clostridial toxins. Curr. Top. Microbiol. Immunol. 250:2000;55-84.
8. Kink J.A., Williams J.A. Antibodies to recombinant Clostridium difficile toxins A and B are an effective treatment and prevent relapse of C. difficile-associated disease in a hamster model of infection. Infect. Immun. 66:1998;2018-2025.
9. Ryan E.T., Butterton J.R., Smith R.N., Carroll P.A., Crean T.I., Calderwood S.B. Protective immunity against Clostridium difficile toxin A induced by oral immunization with a live, attenuated Vibrio cholerae vector strain. Infect. Immun. 65:1997;2941-2949.
10. Ward S.J., Douce G., Dougan G., Wren B.W. Local and systemic neutralizing antibody responses induced by intranasal immunization with the nontoxic binding domain of toxin A from Clostridium difficile. Infect. Immun. 67:1999;5124-5132.
11. McClane B.A. New insights into the genetics and regulation of expression of Clostridium perfringens enterotoxin. Curr. Top. Microbiol. Immunol. 225:1998;37-55.
12. McClane B.A. Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes. Toxicology. 87:1994;43-67.
13. Matsuda M., Ozutsumi K., Iwashi H., Sugimoto N. Primary action of Clostridium perfringens type A enterotoxin on HeLa and Vero cells in the absence of extracellular calcium: rapid and characteristic changes in membrane permeability. Biochem. Biophys. Res. Commun. 141:1986;704-710.
14. Katahira J., Sugiyama H., Inoue N., Horiguchi Y., Matsuda M., Sugimoto N. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. J. Biol. Chem. 272:1997;26652-26658.
15. Fujita K., Katahira J., Horiguchi Y., Sonoda N., Furuse M., Tsukita S. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS Lett. 476:2000;258-261.
16. Mietzner T.A., Kokai-Kun J.F., Hanna P.C., McClane B.A. A conjugated synthetic peptide corresponding to the C-terminal region of Clostridium perfringens type A enterotoxin elicits an enterotoxin-neutralizing antibody response in mice. Infect. Immun. 60:1992;3947-3951.
17. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
18. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
19. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
20. 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;4350-4353.
21. Reed L.J., Muench H. A simple method for estimation of 50 per cent endpoints. Am. J. Hyg. 27:1938;493-497.
22. The recombinant protein handbook. http://www.amershambiosciences.com.
23. Kato H., Kato N., Katow S., Maegawa T., Nakamura S., Lyerly D.M. Deletions in the repeating sequences of the toxin A gene of toxin A-negative, toxin B-positive Clostridium difficile strains. FEMS Microbiol. Lett. 175:1999;197-203.
24. McClane B.A., Wnek A.P., Hulkower K.I., Hanna P.C. Divalent cation involvement in the action of Clostridium perfringens type A enterotoxin. J. Biol. Chem. 263:1988;2423-2435.