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Science 6 June 1986:
Vol. 232. no. 4755, pp. 1258 - 1264
DOI: 10.1126/science.3704651
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Articles

Science, Vol 232, Issue 4755, 1258-1264
Copyright © 1986 by American Association for the Advancement of Science

articles

Pertussis toxin gene: nucleotide sequence and genetic organization

C Locht and JM Keith

The current pertussis vaccines, although efficacious, in some instances produce undesirable side effects. Molecular engineering of pertussis toxin, the major protective antigen, could provide a safer, new generation of vaccines against whooping cough. As a first critical step in the development of such a vaccine, the complete nucleotide sequence of the pertussis toxin gene was determined and the amino acid sequences of the individual subunits were deduced. All five subunits are coded by closely linked cistrons. A promoter-like structure was found in the 5'-flanking region, suggesting that the toxin is expressed through a polycistronic messenger RNA. The order of the cistrons is S1, S2, S4, S5, and S3. All subunits contain signal peptides of variable length. The calculated molecular weights of the mature subunits are 26,024 for S1, 21,924 for S2, 21,873 for S3, 12,058 for S4, and 11,013 for S5. Subunits S2 and S3 share 70% amino acid homology and 75% nucleotide homology. Subunit S1 contains two regions of eight amino acids homologous to analogous regions in the A subunit of both cholera and Escherichia coli heat labile toxins.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Molecular Pathogenesis, Epidemiology, and Clinical Manifestations of Respiratory Infections Due to Bordetella pertussis and Other Bordetella Subspecies.
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Analysis of Subassemblies of Pertussis Toxin Subunits In Vivo and Their Interaction with the Ptl Transport Apparatus.
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Infect. Immun. 72, 5365-5372
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Temporal Expression of Pertussis Toxin and Ptl Secretion Proteins by Bordetella pertussis.
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Antibody-Mediated Neutralization of Pertussis Toxin-Induced Mitogenicity of Human Peripheral Blood Mononuclear Cells.
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Mutations in the S1 Subunit of Pertussis Toxin That Affect Secretion.
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Polymorphism in the Pertussis Toxin Promoter Region Affecting the DNA-Based Diagnosis of Bordetella Infection.
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Surface Expression of a Protective Recombinant Pertussis Toxin S1 Subunit Fragment in Streptococcus gordonii.
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Infect. Immun. 67, 1511-1516
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F. R. Mooi, H. van Oirschot, K. Heuvelman, H. G. J. van der Heide, W. Gaastra, and R. J. L. Willems (1998)
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Probing the G-protein Regulation of GIRK1 and GIRK4, the Two Subunits of the KACh Channel, Using Functional Homomeric Mutants.
M. Vivaudou, K. W. Chan, J.-L. Sui, L. Y. Jan, E. Reuveny, and D. E. Logothetis (1997)
J. Biol. Chem. 272, 31553-31560
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Evidence for a Ninth Gene, ptlI, in the Locus Encoding the Pertussis Toxin Secretion System of Bordetella pertussis and Formation of a PtlI-PtlF Complex.
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J. Biol. Chem. 271, 31643-31649
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Conservation of a Common Motif in Enzymes Catalyzing ADP-ribose Transfer.
T. Takada, K. Iida, and J. Moss (1995)
J. Biol. Chem. 270, 541-544
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Mutants of pertussis toxin suitable for vaccine development.
M Pizza, A Covacci, A Bartoloni, M Perugini, L Nencioni, M. De Magistris, L Villa, D Nucci, R Manetti, M Bugnoli, et al. (1989)
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Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope.
W. Burnette, W Cieplak, V. Mar, K. Kaljot, H Sato, and J. Keith (1988)
Science 242, 72-74
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ADP-ribosyltransferase activity of pertussis toxin and immunomodulation by Bordetella pertussis.
W. Black, J. Munoz, M. Peacock, P. Schad, J. Cowell, J. Burchall, M Lim, A Kent, L Steinman, and S Falkow (1988)
Science 240, 656-659
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