title: Molecular aspects of Bordetella pertussis pathogenesis.
abstract: The molecular mechanisms of Bordetella virulence are now well understood, and many virulence factors have been identified and characterized at the molecular level. These virulence factors can be grouped into two major categories: adhesins, such as filamentous hemagglutinin, pertactin and fimbriae, and toxins, such as pertussis toxin, adenylate cyclase, dermonecrotic toxin and tracheal cytotoxin. The production of most virulence factors is coordinately regulated by a two-component signal transduction system composed of the regulator BvgA and the sensor protein BvgS. The adhesins and toxins act in concert to establish infection. Some adhesins exert their effects synergically or are redundant functioning only in the absence of another adhesin, illustrating the importance of adhesion in infection. Most virulence factors are secreted into the culture supernatant or exposed at the surface of the bacterial cell. A notable exception is dermonecrotic toxin, which remains in the cytoplasmic compartment of bacterial cells. Most virulence factors are produced by all of the three major Bordetella species, B. pertussis, B. parapertussis and B. bronchiseptica. However, some, such as pertussis toxin and the tracheal colonization factor, are only produced by B. pertussis. Our understanding of Bordetella virulence at the molecular level has led to the development of new acellular vaccines against whooping cough, and of genetically attenuated B. pertussis strains to be used as recombinant live bacterial vaccine vectors for homologous and heterologous protection.
authors.affiliation: Laboratoire de Microbiologie Génétique et Moléculaire, INSERM, Institut Pasteur de Lille, France. camille.locht@pasteur-lille.fr
authors.forename: C
authors.initials: C
authors.lastname: Locht
mesh_terms: D037361:Adenylate Cyclase Toxin; D000262:Adenylyl Cyclases / Q000378:metabolism; D018829:Adhesins, Bacterial / Q000502:physiology; D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology; D001426:Bacterial Proteins / Q000502:physiology; D001427:Bacterial Toxins / Q000378:metabolism; D001886:Bordetella pertussis / Q000235:genetics / Q000472:pathogenicity*; D010861:Fimbriae, Bacterial / Q000502:physiology; D006388:Hemagglutinins / Q000502:physiology; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism; D051379:Mice; D010457:Peptidoglycan / Q000378:metabolism; D037342:Pertussis Toxin; D010567:Pertussis Vaccine; D015398:Signal Transduction; D014157:Transcription Factors / Q000502:physiology; D011503:Transglutaminases; D014613:Vaccines, Attenuated; D014774:Virulence / Q000235:genetics; D010566:Virulence Factors, Bordetella / Q000378:metabolism; D014917:Whooping Cough / Q000382:microbiology
chemical_list: D037361:Adenylate Cyclase Toxin; D018829:Adhesins, Bacterial; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; C065601:BvgA protein, Bacteria; D006388:Hemagglutinins; D008070:Lipopolysaccharides; D010457:Peptidoglycan; D010567:Pertussis Vaccine; D014157:Transcription Factors; D014613:Vaccines, Attenuated; D010566:Virulence Factors, Bordetella; C080662:bvgS protein, Bordetella pertussis; C060969:dermonecrotic toxin, Bordetella; C065273:filamentous hemagglutinin adhesin, Bordetella pertussis; C059708:tracheal cytotoxin, Bordetella pertussis; C068929:pertactin; D011503:Transglutaminases; D037342:Pertussis Toxin; D000262:Adenylyl Cyclases