Physico-chemical analysis of Bordetella pertussis antigens

Biologicals

Volumn 27, Issue 2, 1999, Pages 155-162

  Bolgiano, Barbara ^a   Crane, Dennis T ^a   Xing, Dorothy ^a   Williams, Laura ^a   Jones, Christopher ^a   Corbel, Michael J ^a  

^a NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; FORMALDEHYDE; HEMAGGLUTININ; OUTER MEMBRANE PROTEIN; PERTUSSIS TOXIN; PERTUSSIS VACCINE; TRYPTOPHAN;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DRUG DETOXIFICATION; FAST PROTEIN LIQUID CHROMATOGRAPHY; FLUORESCENCE SPECTROSCOPY; GEL FILTRATION CHROMATOGRAPHY; IMMUNOCHEMISTRY; MOLECULAR WEIGHT; PHYSICAL CHEMISTRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; QUALITY CONTROL; STANDARDIZATION; TOXICITY TESTING; VACCINE PRODUCTION;

BACTERIA (MICROORGANISMS); BORDETELLA PERTUSSIS;

EID: 0032726092     PISSN: 10451056     EISSN: None     Source Type: Journal    
DOI: 10.1006/biol.1999.0201     Document Type: Article

References (37)

1. Volkin DB, Burke CJ, Sanyal G. Analysis of vaccine stability. Brown F. New Approaches to Stabilisation of Vaccines Potency. Dev. Biol. Stand. 87:1996;135-142 Karger, Basel.
2. Jones C, Crane DT, Lemercinier X. Physicochemical studies of the structure and stability of polysaccharide-protein conjugate vaccines. Brown F. New Approaches to Stabilisation of Vaccines Potency. Dev. Biol. Stand. 87:1996;143-151 Karger, Basel.
3. Xing D K-L, Crane DT, Bolgiano B. Physicochemical and immunological studies on the stability of free and microsphere-encapsulated tetanus toxoid in vitro. Vaccine. 14:1996;1205-1213.
4. Crane DT, Bolgiano B, Jones C. Comparison of the diphtheria mutant toxin, CRM197, with a Haemophilus influenzae type- b polysaccharide-CRM197 conjugate by optical spectroscopy. Eur J Biochem. 246:1997;320-327.
5. 197conjugate vaccine in mice.
6. Witholt B, Alouf JE, Boulnois GJ. Bacterial Protein Toxins. 1992;Verlag, Stuttgart. p. 241-311.
7. Stein PE, Boodhoo A, Armstrong GD. The crystal structure of pertussis toxin. Structure. 2:1994;45-47.
8. Makhov AM, Hannah JH, Brennan MJ. Filamentous hemagglutinin of Bordetella pertussis. J Mol Biol. 241:1994;110-124.
9. Emsley P, Charles IG, Fairweather NF. Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature. 381:1996;90-92.
10. Choe S, Bennett MJ, Fujii G. The crystal structure of diphtheria toxin. Nature. 357:1992;216-222.
11. Mach H, Middaugh CR, Lewis RV. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal Biochemistry. 200:1992;74-80.
12. Nicosia A, Perugini M, Franzini C. Cloning and sequencing of the pertussis toxin genes: Operon structure and gene duplication. Proc Natl Acad Sci U S A. 83:1996;4631-4635.
13. Delise-Gathoye A-M, Locht C, Jacob F. Cloning, partial sequence, expression, and antigenic analysis of the filamentous hemagglutinin gene of Bordetella pertussis. Infect Immun. 58:1990;2895-2905.
14. Jacob-Dubuisson F, Buisine C, Mielcarek N. Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin. Mol Microbiol. 19:1996;65-78.
15. Seabrook RN, Atkinson T, Irons LI. A spectroscopic and conformational study of pertussis toxin. J Biochem. 198:1991;741-747.
16. Means GE, Feeney RE. Chemical Modification of Proteins. 1971;Holden-Day, London.
17. Petre J, Pizza M, Nencioni L. The reaction of bacterial toxins with formaldehyde and its use for antigen stabilization. Brown F. New Approaches to Stabilisation of Vaccines Potency. Dev. Biol. Stand. 87:1996;125-134 Karger, Basel.
18. Domenighini M, Relman D, Capiau C. Genetic characterization of Bordetella pertussis filamentous haemagglutinin: A protein processed from an unusually large precursor. Mol Microbiol. 5:1990;787-800.
19. Li LJ, Dougan G, Novotny P. P. 70 pertactin, an outer-membrane protein from Bordetella parapertussis: Cloning, nucleotide sequence and surface expression in Escherichia coli. Molec Microbiol. 5:1991;409-417.
20. Makoff AJ, Oxer MD, Ballantine SP. Protective surface antigen P69 of Bordetella pertussis: Its characterization and very high level expression inEscherichia coli. Biotechnology. 8:1990;1030-1033.
21. Strickland EH. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit Rev Biochem. 1:1974;113-175.
22. Loosmore SM, Yacoob RK, Zealey GR. Hybrid genes over-express pertactin from Bordetella pertussis. Vaccine. 13:1995;571-580.
23. Yang JT, Wu C-SC, Martinez HM. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:1986;208-269.
24. Loewenstein E. Ueber Immunisierung mit atoxischen Toxinen und mit übercompensierten Toxin-antitoxin Mischungen bei Diphtherie. Z. Exp. Path. Ther. 15:1914;279-321.
25. Relyveld EH. A history of toxoids. Plotkin S, Fantini B. Vaccinia, vaccination and vaccinology: Jenner, Pasteur and their successors. 1996;95-105 Elsevier, Paris.
26. Nencioni L, Volpini G, Peppoloni S. Properties of pertussis toxin mutant PT-9K/129G after formaldehyde treatment. Infect Immun. 59:1991;625-630.
27. Rappuoli R. Toxin inactivation and antigen stabilization: Two different uses for formaldehyde. Vaccine. 12:1994;579-581.
28. Di Tommaso A, De Magistris MT, Bugnoli M. Formaldehyde treatment of proteins can constrain presentation to T cells by limiting antigen processing. Infect Immun. 62:1994;1830-1834.
29. Ibsen PH. The effect of formaldehyde, hydrogen peroxide and genetic detoxification of pertussis toxin on epitope recognition by murine monoclonal antibodies. Vaccine. 14:1996;359-368.
30. Cropley I, Douce G, Roberts M. Mucosal and systemic immunogenicity of a recombinant, non-ADP-ribosylating pertussis toxin: effects of formaldehyde treatment. Vaccine. 13:1995;1643-1648.
31. Burnette WN, Cieplak W, Mar VL. Pertussis toxin SI mutant with reduced enzyme activity and a conserved protective epitope. Science. 242:1988;72-74.
32. Pizza M, Covacci A, Bartoloni A. Mutants of pertussis toxin suitable for vaccine development. Science. 246:1989;497-500.
33. Barbieri JT, Armellini D, Molkentin J. Construction of the diphtheria toxin A fragment-C180 peptide fusion protein which elicits a neutralizing antibody response against diphtheria toxin and pertussis toxin. Infect Immun. 60:1992;5071-5077.
34. Lobet, Y, Feron, C, Dequesne, G, Site-specific alterations in the B oligomer the affect receptor-binding activities and mitogenicity of pertussis toxin, J Exp Med, 177, 79, 87.
35. Corbel, MJ, Reasons for instability of bacterial vaccines, Brown, F, New Approaches to Stabilisation of Vaccines Potency, Dev Biol Stand, 87, 113, 124, Karger, Basel, 1996.
36. Heron I. Definition of minimum standards for immunogenicity - potential problems of serological correlates - possible interference. Biologicals. 22:1994;389-390.
37. Corbel MJ, Xing DKL, Bolgiano B. Approaches to the control of acellular pertussis vaccines. Biologicals. 27:1999;133-141.