Pertussis vaccine: present status and future prospects

Robinson, A.; Irons, L.I.; Ashworth, L.A.E.

doi:10.1016/0264-410x(85)90004-0

Cited by 121 publications

(79 citation statements)

References 117 publications

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“…It is now generally believed that there are 3 major agglutinogens AGG-1, 2, 3. The strain 134 containing the AGG factor 1 and 3 [14]. Since the presence of AGG-1, 2, 3 in Whole Cell Pertussis Vaccine (WCPV) is believed) to contribute to its protective efficacy, the WHO requirements for pertussis vaccine use a test to verify the presence of component of such agglutinogens in vaccine [15].…”

Section: Abnormal Toxicity Testmentioning

confidence: 99%

Assessment of Toxic Activity of Heat Labile Toxin from Bordetella pertussis Vaccine Strain 134

S¹

2015

Biochem Physiol

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Section: Abnormal Toxicity Testmentioning

confidence: 99%

Assessment of Toxic Activity of Heat Labile Toxin from Bordetella pertussis Vaccine Strain 134

S¹

2015

Biochem Physiol

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“…In addition, several of the systemic disease effects which may result from infection, such as lymphocytosis, enhanced vascular permeability and stimulation of insulin secretion, can be reproduced by PT in experimental models (Ui, 1988). Consequently in order to induce PT-neutralising antibodies, acellular vaccines designed to protect children from whooping cough contain a detoxified form of the protein (Robinson et al, 1985).…”

Section: (Received November 2 1992) -Ejb 92 1550mentioning

confidence: 99%

Localisation of a receptor‐recognition domain on the S3 subunit of pertussis toxin by peptide mapping

Tallett

Seabrook

Irons

et al. 1993

European Journal of Biochemistry

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Overlapping 1 O-amino-acid peptides, which consecutively span the amino acid sequence of the S3 subunit of pertussis toxin, were synthesised on polyethylene pins and screened for their ability to bind the glycoprotein fetuin. Fetuin binding was localised to a single peptide comprising amino acids 46-55. A free peptide, (E)S3c, of longer sequence (S3 amino acids 44-58) was also found to bind a-1 -acid glycoprotein, mixed brain gangliosides and fetuin. (E)S3c also recognised asialofetuin but with a lower apparent affinity relative to fetuin. The single tryptophan residue of the peptide yielded a fluorescence-emission maximum of 355 nm. In the presence of either ganglioside or the phospholipid L-a-lysolecithin, but not N-acetylneuramin-lactose or lactosylceramide, the emission intensity of (E)S3c was enhanced and the emission maximum blue-shifted to 340 nm by ganglioside, or to 345 nm by L-a-lysolecithin. Monosialogangliosides, disialogangliosides, and trisialogangliosides, when fluorescence-titrated, were each found to bind the peptide with a similar dissociation constant of 4.4 2 2.8 pM. These findings demonstrate that region 44-58 of the pertussis-toxin S3 subunit is likely to be involved in the recognition of both glycosylated and phospholipid constituents of target-cell membranes.

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“…Agglutinogens of B. pertussis are surface substances, defined serologically, of which agglutinogens 2 and 3 may have a role in bacterial adhesion (Preston, 1985;Robinson et al, 1985;Cowell et al, 1986). These serotype antigens are thus considered to be candidates for inclusion in acellular vaccines (Carter and Preston, 1984;Robinson et al, 1985;Miller, 1986).…”

Section: Introductionmentioning

confidence: 99%

“…These serotype antigens are thus considered to be candidates for inclusion in acellular vaccines (Carter and Preston, 1984;Robinson et al, 1985;Miller, 1986). Based on epidemiological data, it is recommended that whole-cell vaccines should contain the three major agglutinogens, 1, 2 and 3 (Preston, 1963 ;World Health Organization, 1979).…”

Section: Introductionmentioning

confidence: 99%

Immuno-electronmicroscopy of fimbriae-like structures on Bordetella pertussis serotype 1.3

Fredriksen¹,

Frøholm²

1988

Journal of Medical Microbiology

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Summary.Fimbriae-like filaments were demonstrated on the surface of Bordetella pertussis, serotype 1.3, by negative staining and electronmicroscopy. Immunoelectronmicroscopy with a monoclonal antibody specific for strains possessing agglutinogen 3, and colloidal gold, gave strong labelling of these structures. However, incubation with adsorbed polyclonal anti-agglutinogen 3 serum gave only weak labelling of the distal parts of the filaments and of the bacterial surface. The different binding patterns of the two antisera suggested that the epitopes involved were dissimilar. Thus, agglutinogen 3, as defined by conventional adsorbed sera, appeared to be associated with the fimbriae-like structures but was not necessarily identical to the fimbrial subunit protein. The monoclonal antibody, however, was more likely directed against the subunits of the fimbriae-like structures on serotype 1.3 bacteria.

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Pertussis vaccine: present status and future prospects

Cited by 121 publications

References 117 publications

Assessment of Toxic Activity of Heat Labile Toxin from Bordetella pertussis Vaccine Strain 134

Assessment of Toxic Activity of Heat Labile Toxin from Bordetella pertussis Vaccine Strain 134

Localisation of a receptor‐recognition domain on the S3 subunit of pertussis toxin by peptide mapping

Immuno-electronmicroscopy of fimbriae-like structures on Bordetella pertussis serotype 1.3

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