A comprehensive analysis of Bordetella pertussis surface proteome and identification of new immunogenic proteins

Tefon, Burcu E.; Maaß, Sandra; Özcengīz, Erkan; Becher, Dörte; Hecker, Michael; Özcengiz, Gülay

doi:10.1016/j.vaccine.2011.02.086

Cited by 44 publications

(52 citation statements)

References 54 publications

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“…Immunoproteomics has also been used to identify novel antigens that elicit an immune response, as recently reviewed (5), but when used in isolation, it has limitations, and no efficacious antigens have yet been identified by using this approach. Indeed, the confirmed prophylactic Bordetella pertussis antigen filamentous hemagglutinin (FHA), a component of most licensed acellular whooping cough vaccines, was undetectable in two immunoproteomic studies (6,7).…”

mentioning

confidence: 99%

Linocin and OmpW Are Involved in Attachment of the Cystic Fibrosis-Associated Pathogen Burkholderia cepacia Complex to Lung Epithelial Cells and Protect Mice against Infection

McClean¹,

Healy

Collins³

et al. 2016

Infect Immun

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Members of the Burkholderia cepacia complex (Bcc) cause chronic opportunistic lung infections in people with cystic fibrosis (CF), resulting in a gradual lung function decline and, ultimately, patient death. The Bcc is a complex of 20 species and is rarely eradicated once a patient is colonized; therefore, vaccination may represent a better therapeutic option. We developed a new proteomics approach to identify bacterial proteins that are involved in the attachment of Bcc bacteria to lung epithelial cells. Fourteen proteins were reproducibly identified by two-dimensional gel electrophoresis from four Bcc strains representative of two Bcc species: Burkholderia cenocepacia, the most virulent, and B. multivorans, the most frequently acquired. Seven proteins were identified in both species, but only two were common to all four strains, linocin and OmpW. Both proteins were selected based on previously reported data on these proteins in other species. Escherichia coli strains expressing recombinant linocin and OmpW showed enhanced attachment (4.2-and 3.9-fold) to lung cells compared to the control, confirming that both proteins are involved in host cell attachment. Immunoproteomic analysis using serum from Bcc-colonized CF patients confirmed that both proteins elicit potent humoral responses in vivo. Mice immunized with either recombinant linocin or OmpW were protected from B. cenocepacia and B. multivorans challenge. Both antigens induced potent antigen-specific antibody responses and stimulated strong cytokine responses. In conclusion, our approach identified adhesins that induced excellent protection against two Bcc species and are promising vaccine candidates for a multisubunit vaccine. Furthermore, this study highlights the potential of our proteomics approach to identify potent antigens against other difficult pathogens.

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mentioning

confidence: 99%

Linocin and OmpW Are Involved in Attachment of the Cystic Fibrosis-Associated Pathogen Burkholderia cepacia Complex to Lung Epithelial Cells and Protect Mice against Infection

McClean¹,

Healy

Collins³

et al. 2016

Infect Immun

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“…On the one hand, Finn et al (1995) showed that the absence of OmpQ does not affect the capacity of B. pertussis to colonize mouse lung tissue, discarding the possibility that this protein may play a role in the survival of the bacterium inside the host. On the other hand, recent proteomic studies proposed OmpQ as a novel protective antigen candidate (de Gouw et al, 2014;Packard et al, 2004;Tefon et al, 2011;Williamson et al, 2012;Zhu et al, 2010) and even suggested that OmpQ could play a role in the pathogenesis of Bordetella (Tefon et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

“…In the first studies of OmpQ, Finn et al (1995) reported that the absence of this protein did not affect the ability of B. pertussis 18323 to survive in the mouse respiratory tract. However, more recently, several reports have recognized OmpQ as an immunodominant antigen and, moreover, as a potential novel protective antigen (de Gouw Packard et al, 2004;Tefon et al, 2011;Williamson et al, 2012;Zhu et al, 2010). In addition, it has been proposed that OmpQ should play a role in the pathogenesis of Bordetella, perhaps during the first steps of infection or in the establishment of a carrier state (Tefon et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…However, more recently, several reports have recognized OmpQ as an immunodominant antigen and, moreover, as a potential novel protective antigen (de Gouw Packard et al, 2004;Tefon et al, 2011;Williamson et al, 2012;Zhu et al, 2010). In addition, it has been proposed that OmpQ should play a role in the pathogenesis of Bordetella, perhaps during the first steps of infection or in the establishment of a carrier state (Tefon et al, 2011). Given that OmpQ expression is under the control of the BvgAS system, it seems logical to envisage a role for this porin during the bacterial infection cycle.…”

Section: Introductionmentioning

confidence: 99%

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Outer membrane protein OmpQ of Bordetella bronchiseptica is required for mature biofilm formation

et al. 2016

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Bordetella bronchiseptica, an aerobic Gram-negative bacterium, is capable of colonizing the respiratory tract of diverse animals and chronically persists inside the hosts by forming biofilm. Most known virulence factors in Bordetella species are regulated by the BvgAS two-component transduction system. The Bvg-activated proteins play a critical role during host infection. OmpQ is an outer membrane porin protein which is expressed under BvgAS control. Here, we studied the contribution of OmpQ to the biofilm formation process by B. bronchiseptica. We found that the lack of expression of OmpQ did not affect the growth kinetics and final biomass of B. bronchiseptica under planktonic growth conditions. The DompQ mutant strain displayed no differences in attachment level and in early steps of biofilm formation. However, deletion of the ompQ gene attenuated the ability of B. bronchiseptica to form a mature biofilm. Analysis of ompQ gene expression during the biofilm formation process by B. bronchiseptica showed a dynamic expression pattern, with an increase of biofilm culture at 48 h. Moreover, we demonstrated that the addition of serum anti-OmpQ had the potential to reduce the biofilm biomass formation in a dose-dependent manner. In conclusion, we showed for the first time, to the best of our knowledge, evidence of the contribution of OmpQ to a process of importance for B. bronchiseptica pathobiology. Our results indicate that OmpQ plays a role during the biofilm development process, particularly at later stages of development, and that this porin could be a potential target for strategies of biofilm formation inhibition.

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“…The masses are then compared to protein databases such as Swiss-Prot and GenBank using software that generates lists of the masses of theoretical fragments and matches the experimental and predicted peptides. This is a mature technique and has been applied to immunoproteome mapping of several pathogens, including Bordetella pertussis (whooping cough) [26], Bacillus anthracis (anthrax) [27], and Treponema pallidum (syphilis) [28].…”

Section: D Gel Electrophoresis and Peptide Mass Fingerprintingmentioning

confidence: 99%

Antigen Discovery for Vaccines Using High‐Throughput Proteomic Screening Technologies

Davies¹

2012

Vaccinology

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A comprehensive analysis of Bordetella pertussis surface proteome and identification of new immunogenic proteins

Cited by 44 publications

References 54 publications

Linocin and OmpW Are Involved in Attachment of the Cystic Fibrosis-Associated Pathogen Burkholderia cepacia Complex to Lung Epithelial Cells and Protect Mice against Infection

Linocin and OmpW Are Involved in Attachment of the Cystic Fibrosis-Associated Pathogen Burkholderia cepacia Complex to Lung Epithelial Cells and Protect Mice against Infection

Outer membrane protein OmpQ of Bordetella bronchiseptica is required for mature biofilm formation

Antigen Discovery for Vaccines Using High‐Throughput Proteomic Screening Technologies

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