Pertussis toxin gene: nucleotide sequence and genetic organization

Author(s): Locht C, Keith JM


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.

Similar Articles

Bacterial meningitis in the United States in 1995

Author(s): Schuchat A, Robinson K, Wenger JD, Harrison LH, Farley M, et al.

Arginine-specific mono ADP-ribosylation in vitro of antimicrobial peptides by ADP-ribosylating toxins

Author(s): Castagnini M,Picchianti M, Talluri E, Biagini M, Del Vecchio M, et al.

In silico identification of novel bacterial ADP-ribosyltransferases

Author(s): Masignani V,Balducci E, Serruto D, Veggi D, Aricò B, et al.

NarE: a novel ADP-ribosyltransferase from Neisseria meningitidis

Author(s): Masignani V,Balducci E, Di Marcello F, Savino S, Serruto D, et al.

Auto ADP-ribosylation of NarE, a Neisseria meningitidis ADP-ribosyltransferase, regulates its catalytic activities

Author(s): Picchianti M, Del Vecchio M, Di Marcello F, Biagini M, Veggi D, et al.

A fluorescent analog of nicotinamide adenine dinucleotide

Author(s): Barrio JR, Secrist JA 3rd, Leonard NJ

The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse

Author(s): Glowacki G,Braren R, Firner K, Nissen M, Kühl M, et al.

Activation of choleragen by thiol: protein disulfideoxidoreductase

Author(s): Moss J, Stanley SJ, Morin JE, Dixon JE

Iron transport systems in Neisseria meningitidis

Author(s): Perkins-Balding D, Ratliff-Griffin M, Stojiljkovic I