ArticleCellular microbiology2014
The Bordetella pertussis Bps polysaccharide enhances lung colonization by conferring protection from complement-mediated killing.
Article in Cellular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 31 citations in OpenAlex.
- Mechanisms of natural and vaccine-induced immunity to Bordetella pertussis.PLoS pathogens · 2026Review
- Bordetellae colonization oligosaccharide (b-Cool), a glycan crucial for nasal colonization.Science advances · 2025Article
- Highlights of the 14th InternationalmSphere · 2025Article
- Architecture and matrix assembly determinants of Bordetella pertussis biofilms on primary human airway epithelium.PLoS pathogens · 2023Article
- Development of carbohydrate based next-generation anti-pertussis vaccines.Bioorganic & medicinal chemistry · 2022Review
- Bps polysaccharide of Bordetella pertussis resists antimicrobial peptides by functioning as a dual surface shield and decoy and converts Escherichia coli into a respiratory pathogen.PLoS pathogens · 2022Article
- The staphylococcal exopolysaccharide PIA - Biosynthesis and role in biofilm formation, colonization, and infection.Computational and structural biotechnology journal · 2020Review
- Acellular Pertussis Vaccines Induce Anti-pertactin Bactericidal Antibodies Which Drives the Emergence of Pertactin-Negative Strains.Frontiers in microbiology · 2020Article
- Structural mechanism for regulation of DNA binding of BpsR, a Bordetella regulator of biofilm formation, by 6-hydroxynicotinic acid.PloS one · 2019Article
- Deacetylated microbial biofilm exopolysaccharides: It pays to be positive.PLoS pathogens · 2018Review
- Structural Analysis of Bordetella pertussis Biofilms by Confocal Laser Scanning MicroscopyBio-protocol · 2018Article
- Kingella kingae Surface Polysaccharides Promote Resistance to Human Serum and Virulence in a Juvenile Rat Model.Infection and immunity · 2018Article
- PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms.PLoS pathogens · 2018Article
- Hyperbiofilm Formation by Bordetella pertussis Strains Correlates with Enhanced Virulence Traits.Infection and immunity · 2017Article
- The Bordetella Bps Polysaccharide Is Required for Biofilm Formation and Enhances Survival in the Lower Respiratory Tract of Swine.Infection and immunity · 2017Article
- The History of Bordetella pertussis Genome Evolution Includes Structural Rearrangement.Journal of bacteriology · 2017Article
- Bordetella biofilms: a lifestyle leading to persistent infections.Pathogens and disease · 2016Review
- The protein BpsB is a poly-β-1,6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in Bordetella bronchiseptica.The Journal of biological chemistry · 2015Article
- Complement evasion by Bordetella pertussis: implications for improving current vaccines.Journal of molecular medicine (Berlin, Germany) · 2015Review
- Continuous nondestructive monitoring of Bordetella pertussis biofilms by Fourier transform infrared spectroscopy and other corroborative techniques.Analytical and bioanalytical chemistry · 2007Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Bordetella pertussis is a human-restricted Gram-negative bacterial pathogen that causes whooping cough or pertussis. Pertussis is the leading vaccine preventable disease that is resurging in the USA and other parts of the developed world. There is an incomplete understanding of the mechanisms by which B. pertussis evades killing and clearance by the complement system, a first line of host innate immune defence. The present study examined the role of the Bps polysaccharide to resist complement activity in vitro and in the mouse respiratory tract. The isogenic bps mutant strain containing a large non-polar in-frame deletion of the bpsA-D locus was more sensitive to serum and complement mediated killing than the WT strain. As determined by Western blotting, flow cytometry and electron microscopic studies, the heightened sensitivity of the mutant strain was due to enhanced deposition of complement proteins and the formation of membrane attack complex, the end-product of complement activation. Bps was sufficient to confer complement resistance as evidenced by a Bps-expressing Escherichia coli being protected by serum killing. Additionally, Western blotting and flow cytometry assays revealed that Bps inhibited the deposition of complement proteins independent of other B. pertussis factors. The bps mutant strain colonized the lungs of complement-deficient mice at higher levels than that observed in C57Bl/6 mice. These results reveal a previously unknown interaction between Bps and the complement system in controlling B. pertussis colonization of the respiratory tract. These findings also make Bps a potential target for the prevention and therapy of whooping cough.
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Registered trials
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