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Consequences of the expression of lipopolysaccharide-modifying enzymes for the efficacy and reactogenicity of whole-cell pertussis vaccines
- Source :
- Microbes and Infection. 9:1096-1103
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- Lipopolysaccharide is one of the major constituents of the Gram-negative bacterial outer membrane and is, due to its endotoxic activity, responsible for the relatively high reactogenicity of whole-cell vaccines. In addition, lipopolysaccharide has strong immune stimulating properties, which makes it, potentially, an interesting vaccine component. In a previous study, we have shown that expression of two lipopolysaccharide-modifying enzymes, i.e., PagP and PagL, modulates the endotoxic activity of the Gram-negative bacterium Bordetella pertussis, the causative agent of whooping cough. To assess the consequences of PagP and PagL expression on the efficacy and reactogenicity of whole-cell pertussis vaccines, we have immunised mice and challenged them intranasally with wild-type B. pertussis. Vaccine efficacy, B. pertussis-specific antibody responses, and cytokine profiles were evaluated. The results show that expression of PagL, but not of PagP, significantly increases vaccine efficacy without altering vaccine reactogenicity. Therefore, PagL-expressing B. pertussis strains may form a basis for the development of a new and safer whole-cell pertussis vaccine, as higher vaccine efficacies may allow a reduced vaccine dosage. These data show, for the first time, that lipopolysaccharide composition is an important determinant for the efficacy of whole-cell pertussis vaccines.
- Subjects :
- Lipopolysaccharides
Bordetella pertussis
Lipopolysaccharide
Injections, Subcutaneous
Immunology
Biology
Microbiology
Mice
chemistry.chemical_compound
Immune system
medicine
Animals
Lung
Whooping cough
Pertussis Vaccine
Mice, Inbred BALB C
Reactogenicity
medicine.disease
Vaccine efficacy
biology.organism_classification
Antibodies, Bacterial
Infectious Diseases
chemistry
Cytokines
Pertussis vaccine
Female
Bacterial outer membrane
Carboxylic Ester Hydrolases
Acyltransferases
medicine.drug
Subjects
Details
- ISSN :
- 12864579
- Volume :
- 9
- Database :
- OpenAIRE
- Journal :
- Microbes and Infection
- Accession number :
- edsair.doi.dedup.....c59c99b3540a5924b74a31c533f759c6
- Full Text :
- https://doi.org/10.1016/j.micinf.2007.04.015