The virulence factors of Bordetella pertussis: a matter of control

Smith, Anna Marie

doi:10.1016/s0168-6445(01)00056-0

Cited by 45 publications

(60 citation statements)

References 198 publications

(319 reference statements)

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“…The majority of virulence factors in the bordetellae are regulated by the two-component system BvgAS (34,52). In response to environmental stimuli, the BvgAS system regulates the transcription of several target genes (13).…”

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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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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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“…B. pertussis produces many virulence factors that are responsible for the clinical features of the disease (9,20,26). The virulence factors of B. pertussis are generally divided into two groups, adhesins and toxins.…”

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confidence: 99%

Strain Variation among Bordetella pertussis Isolates in Finland, Where the Whole-Cell Pertussis Vaccine Has Been Used for 50 Years

et al. 2005

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“…Twenty-five years ago, Ofek et al showed that surface-exposed bacterial lectins were required for initiation of infection (44). Since then, several bacterial lectins have been shown to be involved in the attachment of host cell glycoconjugates, such as the P pili and type 1 fimbriae of Escherichia coli (78), the filamentous hemagglutinin of Bordetella pertussis (63), several adhesins of nontypeable Haemophilus influenzae (70), and type IV pili of Pseudomonas aeruginosa (20).…”

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confidence: 99%

A Novel Lectin, DltA, Is Required for Expression of a Full Serum Resistance Phenotype inHaemophilus ducreyi

Leduc¹,

Richards

Davis

et al. 2004

Infect Immun

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Haemophilus ducreyi, the causative agent of chancroid, is highly resistant to the complement-mediated bactericidal activity of normal human serum (NHS). Previously, we identified DsrA (for ducreyi serum resistance A), a major factor required for expression of the serum resistance phenotype in H. ducreyi. We describe here a second outer membrane protein, DltA (for ducreyi lectin A), which also contributes to serum resistance in H. ducreyi. Isogenic dltA mutants, constructed in 35000HP wild-type and FX517 dsrA backgrounds, were more susceptible to the bactericidal effects of NHS than each respective parent, demonstrating the additive effect of the mutations. Furthermore, expression of dltA in H. influenzae strain Rd rendered this highly susceptible strain partially resistant to 5% NHS compared to a vector-control strain. Although primary basic local alignment search tool analysis of the dltA open reading frame revealed no close bacterial homologue, similarity to the ␤-chain of the eukaryotic lectin ricin was noted. DltA shares highly conserved structural motifs with the ricin ␤ chain, such as cysteines and lectin-binding domains. To determine whether dltA was a lectin, ligand blots and affinity chromatography experiments were performed. DltA was affinity purified on immobilized lactose and N-acetylgalactosamine, and N-glycosylated but not glycosidase-treated model glycoproteins bound DltA. These data indicate that DltA is a lectin with specificity for lactose-related carbohydrates (CHO) and is important for H. ducreyi serum resistance.

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The virulence factors of Bordetella pertussis: a matter of control

Cited by 45 publications

References 198 publications

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

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

Strain Variation among Bordetella pertussis Isolates in Finland, Where the Whole-Cell Pertussis Vaccine Has Been Used for 50 Years

A Novel Lectin, DltA, Is Required for Expression of a Full Serum Resistance Phenotype inHaemophilus ducreyi

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