ArticleBiochemistry2012
Solution structure of decorin-binding protein A from Borrelia burgdorferi.
Article in Biochemistry, 2012. 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, 23 citations in OpenAlex.
- Machine learning-driven identification of virulence determinants in Borrelia burgdorferi associated with human dissemination.PLoS computational biology · 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
- Pathogenicity and virulence ofVirulence · 2023Review
- Article
- A bite so sweet: the glycobiology interface of tick-host-pathogen interactions.Parasites & vectors · 2018Review
- Mechanistic and therapeutic overview of glycosaminoglycans: the unsung heroes of biomolecular signaling.Glycoconjugate journal · 2016Review
- Structure of decorin binding protein B from Borrelia burgdorferi and its interactions with glycosaminoglycans.Biochimica et biophysica acta · 2015Article
- Flexible Linker Modulates Glycosaminoglycan Affinity of Decorin Binding Protein A.Biochemistry · 2015Article
- Identification of lysine residues in the Borrelia burgdorferi DbpA adhesin required for murine infection.Infection and immunity · 2014Article
- Strain-specific variation of the decorin-binding adhesin DbpA influences the tissue tropism of the lyme disease spirochete.PLoS pathogens · 2014Article
- That's my story, and I'm sticking to it--an update on B. burgdorferi adhesins.Frontiers in cellular and infection microbiology · 2014Review
- The novel heparin-binding motif in decorin-binding protein A from strain B31 of Borrelia burgdorferi explains the higher binding affinity.Biochemistry · 2013Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Decorin-binding protein A (DBPA) is an important lipoprotein from the bacterium Borrelia burgdorferi, the causative agent of Lyme disease. The absence of DBPA drastically reduces the pathogenic potential of the bacterium, and biochemical evidence indicates DBPA's interactions with the glycosaminoglycan (GAG) portion of decorin are crucial to its function. We have determined the solution structure of DBPA and studied DBPA's interactions with various forms of GAGs. DBPA is determined to be a helical bundle protein consisting of five helices held together by a strong hydrophobic core. The structure also possesses a basic patch formed by portions of two helices and two flexible linkers. Low-molecular mass heparin-induced chemical shift perturbations for residues in the region as well as increases in signal intensities of select residues in their presence confirm residues in the pocket are perturbed by heparin binding. Dermatan sulfate fragments, the dominant GAG type found on decorin, were shown to have lower affinity than heparin but are still capable of binding DBPA.
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