Identification of the mucin-binding adhesin of Pseudomonas cepacia isolated from patients with cystic fibrosis

Sajjan, S. Umadevi; Forstner, Janet F.

doi:10.1128/iai.60.4.1434-1440.1992

Cited by 68 publications

(25 citation statements)

References 24 publications

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“…[73][74][75][76] Mucin glycoproteins have been shown to interact with several respiratory pathogens including Pseudomonas aeruginosa, Staphylococcus aureus, Heamophilus influenzae, Streptococcus pneumonia, Burkholderia cenocepacia, influenza virus, adenovirus, and coronavirus. [77][78][79][80][81][82][83] The bound pathogens which are cleared under normal conditions may persist in the airway lumen when the mucociliary clearance is impaired, and initiate an inflammatory response which can damage the airway epithelium. However, the impact of the interaction of mucin glycoproteins with pathogens in vivo is yet to be established.…”

Section: Mucociliary Function Of the Airway Epitheliummentioning

confidence: 99%

Barrier function of airway tract epithelium

Ganesan¹,

2013

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Airway epithelium contributes significantly to the barrier function of airway tract. Mucociliary escalator, intercellular apical junctional complexes which regulate paracellular permeability and antimicrobial peptides secreted by the airway epithelial cells are the three primary components of barrier function of airway tract. These three components act cooperatively to clear inhaled pathogens, allergens and particulate matter without inducing inflammation and maintain tissue homeostasis. Therefore impairment of one or more of these essential components of barrier function may increase susceptibility to infection and promote exaggerated and prolonged innate immune responses to environmental factors including allergens and pathogens resulting in chronic inflammation. Here we review the regulation of components of barrier function with respect to chronic airways diseases.

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Section: Mucociliary Function Of the Airway Epitheliummentioning

confidence: 99%

Barrier function of airway tract epithelium

Ganesan¹,

2013

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“…Isolates of this clonal lineage carry the cblA gene (which encodes the major cable pilin subunit) and the ‘epidemic’ DNA marker called BCESM (Sajjan et al , 1995; Sun et al , 1995; Mahenthiralingam et al , 1997). We have demonstrated previously that selected isolates from this lineage express cable pili and a 22 kDa adhesin that mediates binding to mucin glycoproteins, epithelial cells and lung sections of CF patients (Sajjan and Forstner, 1992; 1993; Sajjan et al , 2000a). The major receptor for the adhesin on epithelial cells was identified as cytokeratin 13 (CK13) (Sajjan et al , 2000b), the expression of which is increased in CF lungs (Sajjan et al , 2000a).…”

Section: Introductionmentioning

confidence: 99%

Interaction of cblA/adhesin-positive Burkholderia cepacia with squamous epithelium

Sajjan¹,

Ackerley

Forstner³

2002

Cell Microbiol

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Summary A highly transmissible strain of Burkholderia cepacia from genomovar III carries the cable pilin gene, expresses the 22 kDa adhesin (cblA+ve/Adh +ve), binds to cytokeratin 13 (CK13) and is invasive. CK13 is expressed abundantly in the airway epithelia of cystic fibrosis (CF) patients. We have now investigated whether binding of cblA+ve/Adh +ve B. cepacia to CK13 potentiates bacterial invasion and epithelial damage using bronchial epithelial cell cultures differentiated into either squamous (CK13‐enriched) or mucociliary (CK13‐deficient) epithelia. Three different B. cepacia isolates (cblA+ve/Adh +ve, cblA+ve/Adh –ve and cblA–ve/Adh –ve) showed minimal binding to mucociliary cultures, and did not invade or cause cell damage. In contrast, the cblA+ve/Adh +ve isolate, but not others, bound to CK13‐expressing cells in squamous cultures, caused cytotoxicity and stimulated IL‐8 release within 2 h. By 24 h, this isolate invaded and migrated across the squamous culture, causing moderate to severe epithelial damage. A specific antiadhesin antibody, which blocked the initial binding of the cblA+ve/Adh +ve isolate to CK13, significantly inhibited all the pathologic effects. Transmission electron microscopy of squamous cultures incubated with the cblA+ve/Adh +ve isolate, revealed bacteria on the surface surrounded by filopodia by 2 h, and within the cells in membrane‐bound vesicles by 24 h. Bacteria were also observed free in the cytoplasm, surrounded by intermediate filaments containing CK13. These findings suggest that binding of B. cepacia to CK13 is an important initial event and that it promotes bacterial invasion and epithelial damage.

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“…(2), fimbriae (16) and mucin-binding adhesin (27,28). We have reported the production of extracellular products of about 120 strains of clinically isolated P. cepacia.…”

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confidence: 99%

Characterization of Hemolytic and Antifungal Substance, Cepalycin, from Pseudomonas cepacia

Abe

Nakazawa

1994

Microbiology and Immunology

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Hemolytic and antifungal substances, cepalycin I and cepalycin II, have been isolated from Pseudomonas cepacia JN106. A large amount of cepalycins were produced by growing the cells on 1% glycerin‐nutrient agar medium covered with a cellophane membrane. The cell‐washed supernatant was applied to an Amberlite XAD2 column, and cepalycins were eluted with 70% ethanol containing 1mM HCl. Cepalycins were separated by reverse phase HPLC in two fractions which were designated as cepalycin I and cepalycin II. The two cepalycins have indistinguishable UV absorption spectra but have different levels of hemolytic activity relative to the UV absorption. From the inhibition of hemolytic activity of cepalycin by sterols, both cepalycins were suggested to interact with cholesterol in erythrocyte membrane. Such an interaction may contribute to their hemolytic and antifungal activities.

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Identification of the mucin-binding adhesin of Pseudomonas cepacia isolated from patients with cystic fibrosis

Abstract: In previous experiments, we have shown that isolates of Pseudomonas cepacia from sputa of patients with cystic fibrosis (CF), particularly those with severe lung infection, exhibited specific binding to purified respiratory or intestinal mucins (U.

Cited by 68 publications

References 24 publications

Barrier function of airway tract epithelium

Barrier function of airway tract epithelium

Interaction of cblA/adhesin-positive Burkholderia cepacia with squamous epithelium

Characterization of Hemolytic and Antifungal Substance, Cepalycin, from Pseudomonas cepacia

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