Role of<i>Bordetella pertussis</i>Virulence Factors in Adherence to Epithelial Cell Lines Derived from the Human Respiratory Tract

Berg, Bernard M. van den; Beekhuizen, Henry; Willems, Rob J. L.; Mooi, Frits R.; Furth, R. van

doi:10.1128/iai.67.3.1056-1062.1999

Cited by 83 publications

(26 citation statements)

References 54 publications

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“…B. pertussis colonises the respiratory tract and is thought to preferentially adhere to ciliated epithelial cells [18] and also possibly to alveolar macrophages [11,19,20]. BapC and BrkA reveal presence of integrin binding RGD motifs as well as glycosaminoglycan-binding motif SGXG (Fig.…”

Section: Discussionmentioning

confidence: 99%

BapC autotransporter protein of Bordetella pertussis is an adhesion factor

Bokhari

Bilal

Zafar

2011

J. Basic Microbiol.

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Bordetella pertussis, the causative agent of whooping cough, attaches to mucosal surfaces in upper respiratory tract, where it produces, a variety of surface-associated and secreted molecules. Among various secreted products, some of the proteins belonging to autotransporter family; pertactin (Prn), bordetella resistance to killing (BrkA) and a newly identified member, bordetella autotransporter protein-C (BapC), are investigated in this study for their adherence potential to various respiratory and non-respiratory tract specific cell lines. Our results reveal that BapC and Prn mutants adhere significantly less (p < 0.0001 and p < 0.05) respectively to human non-respiratory (HeLa-229) and murine macrophages (P-388 D-1) cells compared to their wild-type strains. Prn, BrkA and BapC share no homology in their passenger domains except existence of common motifs arginine-glycine-asparctic (RGD) and glycosaminoglycan binding site (SGXG). We have shown that RGD and SGXG motifs are present in the coiled region in Prn and BrkA proteins with the exception in BapC where R (463) of RGD and S (597) of SGXG motif were observed in beta sheet of the modeled protein structures. Therefore, there is possibility that such arrangement of motifs can confer greater probability of BapC in better selective adherence to binding sites on the HeLa-229 and P-388 D-1 cell lines.

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Section: Discussionmentioning

confidence: 99%

BapC autotransporter protein of Bordetella pertussis is an adhesion factor

Bokhari

Bilal

Zafar

2011

J. Basic Microbiol.

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“…To date, antigenic divergence between vaccine strains and clinical isolates has been observed with regard to two virulence factors: pertactin (Prn) and pertussis toxin (PT); and it has been suggested that these changes may have contributed to current pertussis epidemics [4]. Recently we described a role for the bacterial virulence factor ®lamentous haemagglutinin (FHA) as a major factor in colonization of the entire respiratory tract [5]. The existence of antigenic variation in this molecule, however, awaits to be con®rmed.…”

Section: Introductionmentioning

confidence: 99%

Binding of Murine Antibodies Against Whole‐Cell Pertussis Vaccine or Filamentous Haemagglutinin by Bordetella pertussis from Patients with Whooping Cough

et al. 2000

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In 1996 an unexpected rise in the incidence of whooping cough occurred in the Netherlands, and antigenic divergence between vaccine strains and clinical isolates has been suggested as a cause for this phenomenon. To investigate this assumption, the binding of murine antibodies against the whole-cell pertussis vaccine or filamentous haemagglutinin, an important protective antigen, to a limited number of Bordetella pertussis strains isolated during different time-periods (1991-92, 1994 and 1996) was assessed. The results showed that all strains were recognized equally well by these antisera, indicating that filamentous haemagglutinin was unchanged during the time-periods examined. Although over the years changes have occurred in at least two surface proteins of B. pertussis, these changes are too subtle to be recognized by the antibodies raised in mice. Further research is required to assess whether antigenic variation of B. pertussis has an effect on protective immunity.

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“…PRN belongs to the type V autotransporter protein family and, similar to FHA, contains an RGD domain as well (18). Several in vitro studies have demonstrated PRN to function as an adhesin (19,32,36,71); however, an exact host receptor has not been identified. The role of PRN as a protective immunogen is more clearly defined.…”

mentioning

confidence: 99%

Contribution of Bordetella bronchiseptica Filamentous Hemagglutinin and Pertactin to Respiratory Disease in Swine

2009

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Bordetella bronchiseptica is pervasive in swine populations and plays multiple roles in respiratory disease. Most studies addressing virulence factors of B. bronchiseptica are based on isolates derived from hosts other than pigs. Two well-studied virulence factors implicated in the adhesion process are filamentous hemagglutinin (FHA) and pertactin (PRN). We hypothesized that both FHA and PRN would serve critical roles in the adhesion process and be necessary for colonization of the swine respiratory tract. To investigate the role of FHA and PRN in Bordetella pathogenesis in swine, we constructed mutants containing an in-frame deletion of the FHA or the PRN structural gene in a virulent B. bronchiseptica swine isolate. Both mutants were compared to the wild-type swine isolate for their ability to colonize and cause disease in swine. Colonization of the FHA mutant was lower than that of the wild type at all respiratory tract sites and time points examined and caused limited to no disease. In contrast, the PRN mutant caused similar disease severity relative to the wild type; however, colonization of the PRN mutant was reduced relative to the wild type during early and late infection and induced higher anti-Bordetella antibody titers. Together, our results indicate that despite inducing different pathologies and antibody responses, both FHA and PRN are necessary for optimal colonization of the swine respiratory tract.

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Role ofBordetella pertussisVirulence Factors in Adherence to Epithelial Cell Lines Derived from the Human Respiratory Tract

Cited by 83 publications

References 54 publications

BapC autotransporter protein of Bordetella pertussis is an adhesion factor

BapC autotransporter protein of Bordetella pertussis is an adhesion factor

Binding of Murine Antibodies Against Whole‐Cell Pertussis Vaccine or Filamentous Haemagglutinin by Bordetella pertussis from Patients with Whooping Cough

Contribution of Bordetella bronchiseptica Filamentous Hemagglutinin and Pertactin to Respiratory Disease in Swine

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