Biochemical and Immunological Comparison of Lipopolysaccharides from Bordetella Species

Amano, Ken‐ichi; Fukushi, Kazue; Watanabe, Mitsuru

doi:10.1099/00221287-136-3-481

Cited by 42 publications

(28 citation statements)

References 23 publications

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“…bronchiseptica LPS induces greater inflammatory responses in vitro than LPSs from B. pertussis and B. parapertussis. Previous studies have reported differences in the biological and immunological properties of LPSs of the three Bordetella species (1,48,49), and the results of our infection experiments suggest that B. bronchiseptica induces a greater inflammatory response via TLR4 than B. pertussis or B. parapertussis. These results suggest that there may be differences in the ability of each LPS to induce TLR4-dependent responses.…”

Section: Resultssupporting

confidence: 58%

Comparative Toll-Like Receptor 4-Mediated Innate Host Defense toBordetellaInfection

et al. 2005

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Bordetella pertussis, B. parapertussis, and B. bronchiseptica are closely related species associated with respiratory disease in humans and other mammals. While B. bronchiseptica has a wide host range, B. pertussis and B. parapertussis evolved separately from a B. bronchiseptica-like progenitor to naturally infect only humans. Despite very different doubling times in vitro, all three establish similar levels of infection in the mouse lung within 72 h. Recent work has revealed separate roles for Toll-like receptor 4 (TLR4) in immunity to B. pertussis and B. bronchiseptica, while no role for TLR4 during B. parapertussis infection has been described. Here we compared the requirement for TLR4 in innate host defense to these organisms using the same mouse infection model. While B. bronchiseptica causes lethal disease in TLR4-deficient mice, B. pertussis and B. parapertussis do not. Correspondingly, TLR4 is critical in limiting B. bronchiseptica but not B. pertussis or B. parapertussis bacterial numbers during the first 72 h. Interestingly, B. bronchiseptica induces a TLR4-dependent cytokine response that is considerably larger than that induced by B. pertussis or B. parapertussis. Analysis of their endotoxins using RAW cells suggests that B. bronchiseptica lipopolysaccharide (LPS) is 10-and 100-fold more stimulatory than B. pertussis or B. parapertussis LPS, respectively. The difference in LPS stimulus is more pronounced when using HEK293 cells expressing human TLR4. Thus, it appears that in adapting to infect humans, B. pertussis and B. parapertussis independently modified their LPS to reduce TLR4-mediated responses, which may compensate for slower growth rates and facilitate host colonization.

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Section: Resultssupporting

confidence: 58%

Comparative Toll-Like Receptor 4-Mediated Innate Host Defense toBordetellaInfection

et al. 2005

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“…The presence of the correct mutation in the bvgS gene on the chromosome was confirmed by nucleotide sequencing in both directions after obtaining the gene by PCR. The correct phenotype was confirmed by testing colonies for hemolytic activity on Bordet-Gengou agar supplemented with 15% defibrinated sheep blood and 50 mM MgSO 4 . Neisseria meningitidis was grown at 37°C on GC agar plates (Oxoid) supplemented with Vitox (Oxoid).…”

Section: Methodsmentioning

confidence: 99%

“…It has been shown that Bordetella LPS is highly immunogenic, acts as an immunological adjuvant, and exhibits the properties that are expected of an endotoxin (4,12,61). Furthermore, Bordetella LPS and its recognition by the TLR4/ MD-2 complex have been shown to be important determinants for the course of infection in mice (6,32,33).…”

mentioning

confidence: 99%

Expression of the Lipopolysaccharide-Modifying Enzymes PagP and PagL Modulates the Endotoxic Activity ofBordetella pertussis

Geurtsen¹,

Steeghs

Hamstra³

et al. 2006

Infect Immun

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Lipopolysaccharide (LPS) is one of the major constituents of the gram-negative bacterial cell envelope. Its endotoxic activity causes the relatively high reactogenicity of whole-cell vaccines. Several bacteria harbor LPS-modifying enzymes that modulate the endotoxic activity of the LPS. Here we evaluated whether two such enzymes, i.e., PagP and PagL, could be useful tools for the development of an improved and less reactogenic whole-cell pertussis vaccine. We showed that expression of PagP and PagL in Bordetella pertussis leads to increased and decreased endotoxic activity of the LPS, respectively. As expected, PagP activity also resulted in increased endotoxic activity of whole bacterial cells. However, more unexpectedly, this was also the case for PagL. This paradoxical result may be explained, in part, by an increased release of LPS, which we observed in the PagL-expressing cells.

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“…Its endotoxin, an immunomodulator of the bacterial surface, has been antigenically defined and the structures of the constituent lipopolysaccharides (LPS) established (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11). B. parapertussis, the other agent of whooping cough is not a strictly human pathogen and can often be isolated from late-stage pertussis patients as well as from infected sheep (6,9,12,13).…”

mentioning

confidence: 99%

Structural characterization of Bordetella parapertussis lipid A

Hamidi¹,

Новиков²,

Karibian³

et al. 2009

Journal of Lipid Research

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Bordetella parapertussis like B. pertussis, is a causal agent of whooping cough but is not a strictly human pathogen. Because its endotoxin, a major structural component of the Gram-negative outer membrane, is an important virulence factor, we have analyzed the structure of its toxic lipid domain, in one rough and two smooth bacterial strains. Chemical analyses and mass spectra obtained before and after recently developed mild-alkali treatments revealed that the lipids A have the common bisphosphorylated b-(1→6)-linked D-glucosamine disaccharide with hydroxytetradecanoic acid in amide linkages. All three strains have two major molecular species: a tetraacyl and a pentaacyl species. The rough strain is richer in a minor hexaacyl species. Acylation at the C-2, C-3, and C-3′ positions was different from that of the B. pertussis lipid A. The C-2 position carries a secondary hexadecanoic acid, the C-3 position is free, and the C-3′ position is substituted with hydroxydecanoic acid (not at C-3 as in B. pertussis), and the rough strain hexaacyl species carries a second secondary hexadecanoic acid. Like the lipid A of B. pertussis, the hydroxytetradecanoic acid at the C-2′ position was substituted by tetradecanoic

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Biochemical and Immunological Comparison of Lipopolysaccharides from Bordetella Species

Cited by 42 publications

References 23 publications

Comparative Toll-Like Receptor 4-Mediated Innate Host Defense toBordetellaInfection

Comparative Toll-Like Receptor 4-Mediated Innate Host Defense toBordetellaInfection

Expression of the Lipopolysaccharide-Modifying Enzymes PagP and PagL Modulates the Endotoxic Activity ofBordetella pertussis

Structural characterization of Bordetella parapertussis lipid A

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