ArticleJournal of bacteriology2013
D-alanine modification of a protease-susceptible outer membrane component by the Bordetella pertussis dra locus promotes resistance to antimicrobial peptides and polymorphonuclear leukocyte-mediated killing.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Avirulent phenotype promotesEmerging microbes & infections · 2023Article
- Mechanism of D-alanine transfer to teichoic acids shows how bacteria acylate cell envelope polymers.Nature microbiology · 2023Article
- Bacterial resistance to antibacterial agents: Mechanisms, control strategies, and implications for global health.The Science of the total environment · 2023Review
- 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
- Genome Analysis ofApplied and environmental microbiology · 2022Article
- Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities.Biophysical reviews · 2021Review
- Comparative NanoUPLC-MSScientific reports · 2017Article
- Antimicrobial Peptide Resistance Genes in the Plant Pathogen Dickeya dadantii.Applied and environmental microbiology · 2016Article
- Bacterial strategies of resistance to antimicrobial peptides.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Review
- Daptomycin Tolerance in the Staphylococcus aureus pitA6 Mutant Is Due to Upregulation of the dlt Operon.Antimicrobial agents and chemotherapy · 2016Article
- Host Antimicrobial Peptides in Bacterial Homeostasis and Pathogenesis of Disease.Antibiotics (Basel, Switzerland) · 2014Article
- Bordetella pertussis lipid A glucosamine modification confers resistance to cationic antimicrobial peptides and increases resistance to outer membrane perturbation.Antimicrobial agents and chemotherapy · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Bordetella pertussis is the causative agent of pertussis, a highly contagious disease of the human respiratory tract. Despite very high vaccine coverage, pertussis has reemerged as a serious threat in the United States and many developing countries. Thus, it is important to pursue research to discover unknown pathogenic mechanisms of B. pertussis. We have investigated a previously uncharacterized locus in B. pertussis, the dra locus, which is homologous to the dlt operons of Gram-positive bacteria. The absence of the dra locus resulted in increased sensitivity to the killing action of antimicrobial peptides (AMPs) and human phagocytes. Compared to the wild-type cells, the mutant cells bound higher levels of cationic proteins and peptides, suggesting that dra contributes to AMP resistance by decreasing the electronegativity of the cell surface. The presence of dra led to the incorporation of d-alanine into an outer membrane component that is susceptible to proteinase K cleavage. We conclude that dra encodes a virulence-associated determinant and contributes to the immune resistance of B. pertussis. With these findings, we have identified a new mechanism of surface modification in B. pertussis which may also be relevant in other Gram-negative pathogens.
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Registered trials
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