ArticleInfection and immunity2014
Identification of lysine residues in the Borrelia burgdorferi DbpA adhesin required for murine infection.
Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 30 citations in OpenAlex.
- Characterization ofMicroorganisms · 2026Article
- Characterizing the impact of intracutaneous dissemination on host responses duringFrontiers in immunology · 2026Article
- Navigating infection by pathogenic spirochetes: The host-bacteria interface at the atomic level.Protein science : a publication of the Protein Society · 2025Review
- Germline encoded residues dominate the interaction of a human monoclonal antibody with decorin binding protein A ofFrontiers in immunology · 2025Article
- Choreography of Lyme Disease Spirochete Adhesins To Promote Vascular Escape.Microbiology spectrum · 2023Article
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- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- Lyme Disease in Humans.Current issues in molecular biology · 2021Article
- The BB0345 Hypothetical Protein of Borrelia burgdorferi Is Essential for Mammalian Infection.Infection and immunity · 2020Article
- Strain-specific joint invasion and colonization by Lyme disease spirochetes is promoted by outer surface protein C.PLoS pathogens · 2020Article
- Non-anticoagulant Heparin as a Pre-exposure Prophylaxis Prevents Lyme Disease Infection.ACS infectious diseases · 2020Article
- A joint effort: The interplay between the innate and the adaptive immune system in Lyme arthritis.Immunological reviews · 2020Review
- Leishmaniasis and glycosaminoglycans: a future therapeutic strategy?Parasites & vectors · 2018Review
- Borrelia burgdorferi glycosaminoglycan-binding proteins: a potential target for new therapeutics against Lyme disease.Microbiology (Reading, England) · 2017Review
- Review
- Mechanistic and therapeutic overview of glycosaminoglycans: the unsung heroes of biomolecular signaling.Glycoconjugate journal · 2016Review
- Middle region of the Borrelia burgdorferi surface-located protein 1 (Lmp1) interacts with host chondroitin-6-sulfate and independently facilitates infection.Cellular microbiology · 2016Article
- Structure of decorin binding protein B from Borrelia burgdorferi and its interactions with glycosaminoglycans.Biochimica et biophysica acta · 2015Article
- Host cell heparan sulfate glycosaminoglycans are ligands for OspF-related proteins of the Lyme disease spirochete.Cellular microbiology · 2015Article
- Borrelia burgdorferi RevA Significantly Affects Pathogenicity and Host Response in the Mouse Model of Lyme Disease.Infection and immunity · 2015Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Decorin-binding protein A (DbpA) of Borrelia burgdorferi mediates bacterial adhesion to heparin and dermatan sulfate associated with decorin. Lysines K82, K163, and K170 of DbpA are known to be important for in vitro interaction with decorin, and the DbpA structure, initially solved by nuclear magnetic resonance (NMR) spectroscopy, suggests these lysine residues colocalize in a pocket near the C terminus of the protein. In the current study, we solved the structure of DbpA from B. burgdorferi strain 297 using X-ray crystallography and confirmed the existing NMR structural data. In vitro binding experiments confirmed that recombinant DbpA proteins with mutations in K82, K163, or K170 did not bind decorin, which was due to an inability to interact with dermatan sulfate. Most importantly, we determined that the in vitro binding defect observed upon mutation of K82, K163, or K170 in DbpA also led to a defect during infection. The infectivity of B. burgdorferi expressing individual dbpA lysine point mutants was assessed in mice challenged via needle inoculation. Murine infection studies showed that strains expressing dbpA with mutations in K82, K163, and K170 were significantly attenuated and could not be cultured from any tissue. Proper expression and cellular localization of the mutated DbpA proteins were examined, and NMR spectroscopy determined that the mutant DbpA proteins were structurally similar to wild-type DbpA. Taken together, these data showed that lysines K82, K163, and K170 potentiate the binding of DbpA to dermatan sulfate and that an interaction(s) mediated by these lysines is essential for B. burgdorferi murine infection.
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