Journal ArticleDOI
The concept of pertussis as a toxin-mediated disease.
TLDR
Pertussis (whooping cough), a two-stage process of disease (respiratory colonization and toxin-mediated disease) is caused by B. pertussis, a pathogenic parasite with habitat only in human beings.About:
This article is published in Pediatric Infectious Disease.The article was published on 1984-09-01. It has received 244 citations till now. The article focuses on the topics: Pertussis toxin & Immunity.read more
Citations
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Journal ArticleDOI
Molecular Pathogenesis, Epidemiology, and Clinical Manifestations of Respiratory Infections Due to Bordetella pertussis and Other Bordetella Subspecies
Seema Mattoo,Jonathan D. Cherry +1 more
TL;DR: DTaP vaccines, which are less reactogenic than DTP vaccines, are now in general use in many developed countries, and it is expected that the expansion of their use to adolescents and adults will have a significant impact on reducing pertussis and perhaps decrease the circulation of B. pertussedis.
Journal ArticleDOI
Adjuvants--a balance between toxicity and adjuvanticity.
Rajesh Gupta,Edgar H. Relyveld,Erik B. Lindblad,Bernard Bizzini,Shlomo Ben-Efraim,Chander Kanta Gupta +5 more
TL;DR: The most common adjuvants for human use today are still aluminium hydroxide, aluminium phosphate and calcium phosphate although oil emulsions, products from bacteria and their synthetic derivatives as well as liposomes have also been tested or used in humans.
Journal ArticleDOI
Recognition of a bacterial adhesion by an integrin: macrophage CR3 (alpha M beta 2, CD11b/CD18) binds filamentous hemagglutinin of Bordetella pertussis.
David A. Relman,Elaine Tuomanen,Stanley Falkow,Douglas T. Golenbock,Kirsi Saukkonen,Samuel D. Wright +5 more
TL;DR: It is demonstrated that bacterial adherence can be based on the interaction of aacterial adhesin RGD sequence with an integrin and that bacterial adhesins can have multiple binding sites characteristic of eukaryotic extracellular matrix proteins.
Journal ArticleDOI
The crystal structure of pertussis toxin.
Penelope E. Stein,Amechand Boodhoo,Glen D. Armstrong,Stephen A. Cockle,Michel H. Klein,Randy J. Read +5 more
TL;DR: The structure provides insight into the pathogenic mechanisms of pertussis toxin and the evolution of bacterial toxins, and knowledge of the tertiary structure of the active site forms a rational basis for elimination of catalytic activity in recombinant molecules for vaccine use.
Journal ArticleDOI
Pertussis: Microbiology, Disease, Treatment, and Prevention
TL;DR: Ongoing research using newer tools for molecular analysis holds promise for improved understanding of pertussis epidemiology, bacterial pathogenesis, bioinformatics, and immunology, which provide a foundation for the development of new-generation diagnostics, therapeutics, and vaccines.
Related Papers (5)
Pertussis toxin gene: nucleotide sequence and genetic organization
Camille Locht,Jerry M. Keith +1 more