New insights into the immunoproteome of B. cenocepacia J2315 using serum samples from cystic fibrosis patients

Sousa, Sílvia A.; Soares-Castro, Pedro; Seixas, António M M; Feliciano, Joana R.; Balugas, Bernardo; Barreto, Celeste; Pereira, Luí­sa Álvares; Santos, Pedro M.; Leitão, Jorge H.

doi:10.1016/j.nbt.2019.08.006

Cited by 7 publications

(14 citation statements)

References 37 publications

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“…On the other hand, the BCAL2022 protein was only immunoreactive with one of the serum samples tested ( Figure 5 A) and therefore was not used in ELISA experiments. These results suggest that although the gene encoding the BCAL2022 protein is highly conserved in Bcc [ 19 ], the expression and surface-exposure of the protein is not a common trait of the Bcc bacteria during the infection of CF patients. No reactivity of the tested proteins was observed when using samples of a pool of sera from healthy individuals ( Figure 5 B).…”

Section: Resultsmentioning

confidence: 99%

“…In this context, the development of protective vaccines against Bcc infections becomes highly attractive. To date, no such vaccine is available and only a few studies have been performed envisaging the identification of Bcc immunogenic proteins with the potential to originate a protective and lasting immune response [12][13][14]19,45,46].…”

Section: Discussionmentioning

confidence: 99%

“…The membranes were then probed for 3 h at room temperature with individual serum samples from CF patients (1:1000 dilution) or with a commercial pool of human sera from healthy donors (1:1000 dilution, S7023, Sigma, St. Louis, MO, USA). Serum samples were obtained from blood samples collected from two CF patients with a clinical record of Bcc infection who attended the Santa Maria hospital in Lisbon, Portugal, as previously described [19]. The membranes were washed with PBS-T (PBS containing 0.05 % (v/v) Tween 20) and then incubated for 1 h at room temperature with a secondary antibody horseradish peroxidase (HRP)-conjugated rabbit anti-human IgG (1:5000 dilution, Santa Cruz Biotechnology, Dallas, TX, USA).…”

Section: Cf Patients' Blood Sera's Immunoreactivity Against the Protementioning

confidence: 99%

“…No reactivity of the tested proteins was observed when using samples of a pool of sera from healthy individuals ( Figure 5B). the BCAL2022 protein is highly conserved in Bcc [19], the expression and surface-exposure of the protein is not a common trait of the Bcc bacteria during the infection of CF patients. No reactivity of the tested proteins was observed when using samples of a pool of sera from healthy individuals ( Figure 5B).…”

Section: Bcal2022mentioning

confidence: 99%

“…Therefore, surface-exposed proteins are appealing antigens for the development of new therapeutic strategies for the eradication of bacterial infections [16]. However, a wide range of characteristics including low abundance, hydrophobic natures and low solubility make these proteins difficult to study, especially using first-generation gel-dependent proteomics approaches [17][18][19]. In order to uncover novel surface-exposed antigens to be studied for the development of new therapeutic strategies for the eradication of Bcc infections, a bioinformatics analysis of the surface-exposed proteins of B. cenocepacia J2315 and their immune profile was performed in this work.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of the Burkholderia cenocepacia J2315 Surface-Exposed Immunoproteome

et al. 2020

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Infections by the Burkholderia cepacia complex (Bcc) remain seriously life threatening to cystic fibrosis (CF) patients, and no effective eradication is available. A vaccine to protect patients against Bcc infections is a highly attractive therapeutic option, but none is available. A strategy combining the bioinformatics identification of putative surface-exposed proteins with an experimental approach encompassing the “shaving” of surface-exposed proteins with trypsin followed by peptide identification by liquid chromatography and mass spectrometry is here reported. The methodology allowed the bioinformatics identification of 263 potentially surface-exposed proteins, 16 of them also experimentally identified by the “shaving” approach. Of the proteins identified, 143 have a high probability of containing B-cell epitopes that are surface-exposed. The immunogenicity of three of these proteins was demonstrated using serum samples from Bcc-infected CF patients and Western blotting, validating the usefulness of this methodology in identifying potentially immunogenic surface-exposed proteins that might be used for the development of Bcc-protective vaccines.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Cf Patients' Blood Sera's Immunoreactivity Against the Protementioning

confidence: 99%

Section: Bcal2022mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Characterization of the Burkholderia cenocepacia J2315 Surface-Exposed Immunoproteome

et al. 2020

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Outer Membrane Vesicles as Mediators of Plant–Bacterial Interactions

et al. 2022

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Plants have co-evolved with diverse microorganisms that have developed different mechanisms of direct and indirect interactions with their host. Recently, greater attention has been paid to a direct “message” delivery pathway from bacteria to plants, mediated by the outer membrane vesicles (OMVs). OMVs produced by Gram-negative bacteria play significant roles in multiple interactions with other bacteria within the same community, the environment, and colonized hosts. The combined forces of innovative technologies and experience in the area of plant–bacterial interactions have put pressure on a detailed examination of the OMVs composition, the routes of their delivery to plant cells, and their significance in pathogenesis, protection, and plant growth promotion. This review synthesizes the available knowledge on OMVs in the context of possible mechanisms of interactions between OMVs, bacteria, and plant cells. OMVs are considered to be potential stimulators of the plant immune system, holding potential for application in plant bioprotection.

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A Polyclonal Antibody Raised against the Burkholderia cenocepacia OmpA-like Protein BCAL2645 Impairs the Bacterium Adhesion and Invasion of Human Epithelial Cells In Vitro

et al. 2021

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Respiratory infections by bacteria of the Burkholderia cepacia complex (Bcc) remain a life threat to cystic fibrosis (CF) patients, due to the faster lung function decline and the absence of effective eradication strategies. Immunotherapies are regarded as an attractive alternative to control and reduce the damages caused by these infections. In this work, we report the cloning and functional characterization of the OmpA-like BCAL2645 protein, previously identified and found to be immunoreactive against sera from CF patients with a record of Bcc infections. The BCAL2645 protein is shown to play a role in biofilm formation, adherence to mucins and invasion of human lung epithelial cells. The expression of the BCAL2645 protein was found to be increased in culture medium, mimicking the lungs of CF patients and microaerophilic conditions characteristic of the CF lung. Moreover, a polyclonal antibody raised against BCAL2645 was found to inhibit, by about 75 and 85%, the ability of B. cenocepacia K56-2 to bind and invade in vitro CFBE41o- human bronchial epithelial cells. These results highlight the potential of anti-BCAL2645 antibodies for the development of passive immunization therapies to protect CF patients against Bcc infections.

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New insights into the immunoproteome of B. cenocepacia J2315 using serum samples from cystic fibrosis patients

Cited by 7 publications

References 37 publications

Characterization of the Burkholderia cenocepacia J2315 Surface-Exposed Immunoproteome

Characterization of the Burkholderia cenocepacia J2315 Surface-Exposed Immunoproteome

Outer Membrane Vesicles as Mediators of Plant–Bacterial Interactions

A Polyclonal Antibody Raised against the Burkholderia cenocepacia OmpA-like Protein BCAL2645 Impairs the Bacterium Adhesion and Invasion of Human Epithelial Cells In Vitro

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