ArticleJournal of bacteriology2013
BB0172, a Borrelia burgdorferi outer membrane protein that binds integrin α3β1.
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 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2023Review
- LIC12254 Is a Leptospiral Protein That Interacts with Integrins via the RGD Motif.Tropical medicine and infectious disease · 2023Article
- TheInfection and immunity · 2023Article
- Identification of a novel transport system in Borrelia burgdorferi that links the inner and outer membranes.Pathogens and disease · 2023Article
- Generation of multi-layered protein bodies inFrontiers in plant science · 2023Article
- Human and Veterinary Vaccines for Lyme Disease.Current issues in molecular biology · 2021Article
- Lyme Disease Pathogenesis.Current issues in molecular biology · 2021Review
- Leptospira interrogans Bat proteins impair host hemostasis by fibrinogen cleavage and platelet aggregation inhibition.Medical microbiology and immunology · 2020Article
- The Borrelia burgdorferi VlsE Lipoprotein Prevents Antibody Binding to an Arthritis-Related Surface Antigen.Cell reports · 2020Article
- Borrelia burgdorferi protein interactions critical for microbial persistence in mammals.Cellular microbiology · 2019Review
- A bite so sweet: the glycobiology interface of tick-host-pathogen interactions.Parasites & vectors · 2018Review
- Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018Review
- Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi.BMC microbiology · 2017Article
- Outer Membrane Proteins BB0405 and BB0406 Are Immunogenic, but Only BB0405 Is Required for Borrelia burgdorferi Infection.Infection and immunity · 2017Article
- Consensus computational network analysis for identifying candidate outer membrane proteins from Borrelia spirochetes.BMC microbiology · 2016Article
- Characterization of the β-barrel assembly machine accessory lipoproteins from Borrelia burgdorferi.BMC microbiology · 2015Article
- Immunization with a Borrelia burgdorferi BB0172-derived peptide protects mice against lyme disease.PloS one · 2014Article
- That's my story, and I'm sticking to it--an update on B. burgdorferi adhesins.Frontiers in cellular and infection microbiology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using in vitro transcription/translation systems in the presence of microsomal membranes and with detergent phase separation assays. Our results showed evidence of BB0172 localization in the outer membrane, the orientation of the vWFA domain to the extracellular environment, and its function as a metal ion-dependent integrin-binding protein. This is the first report of a borrelial adhesin with a metal ion-dependent adhesion site (MIDAS) motif that is similar to those observed in eukaryotic integrins and has a similar function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.