ArticleThe Journal of biological chemistry2012
OspC is potent plasminogen receptor on surface of Borrelia burgdorferi.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 2 of them syntheses that pooled it.
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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.
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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.
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Who cites it
71 citing papers in PubMed, 2 syntheses or guidelines pooled it, 115 citations in OpenAlex.
- Cutaneous Lyme borreliosis: Guideline of the German Dermatology Society.German medical science : GMS e-journal · 2025Guideline
- Cutaneous Lyme borreliosis: Guideline of the German Dermatology Society.German medical science : GMS e-journal · 2017Guideline
- Borrelia surface proteins: new horizons in Lyme disease diagnosis.Applied microbiology and biotechnology · 2025Review
- Article
- Characterization and genomic analysis of the Lyme disease spirochete bacteriophage ϕBB-1.PLoS pathogens · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Differential Resistance ofPathogens (Basel, Switzerland) · 2023Article
- Skin microbiota secretomes modulate cutaneous innate immunity against Borrelia burgdorferi s.s.Scientific reports · 2023Article
- Development of an mRNA-lipid nanoparticle vaccine against Lyme disease.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- Whole genome sequencing of human Borrelia burgdorferi isolates reveals linked blocks of accessory genome elements located on plasmids and associated with human dissemination.PLoS pathogens · 2023Article
- Gac Is a Transcriptional Repressor of the Lyme Disease Spirochete's OspC Virulence-Associated Surface Protein.Journal of bacteriology · 2023Article
- Borrelia burgdorferi Outer Surface Protein C Is Not the Sole Determinant of Dissemination in Mammals.Infection and immunity · 2023Article
- Erp and Rev Adhesins of the Lyme Disease Spirochete's Ubiquitous cp32 Prophages Assist the Bacterium during Vertebrate Infection.Infection and immunity · 2023Review
- Immune evasion strategies of major tick-transmitted bacterial pathogens.Trends in microbiology · 2023Review
- Transmission Cycle of Tick-Borne Infections and Co-Infections, Animal Models and Diseases.Pathogens (Basel, Switzerland) · 2022Review
- The Consistent Tick-Vertebrate Infectious Cycle of the Lyme Disease Spirochete Enables Borrelia burgdorferi To Control Protein Expression by Monitoring Its Physiological Status.Journal of bacteriology · 2022Review
- VlsE, the nexus for antigenic variation of the Lyme disease spirochete, also mediates early bacterial attachment to the host microvasculature under shear force.PLoS pathogens · 2022Article
- Subversion of the immune response of human pathogenic spirochetes.Journal of clinical laboratory analysis · 2022Review
- Maximum antigen diversification in a lyme bacterial population and evolutionary strategies to overcome pathogen diversity.The ISME journal · 2022Article
- Beyond cuts and scrapes: plasmin in malaria and other vector-borne diseases.Trends in parasitology · 2022Review
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Host-derived proteases are crucial for the successful infection of vertebrates by several pathogens, including the Lyme disease spirochete bacterium, Borrelia burgdorferi. B. burgdorferi must traverse tissue barriers in the tick vector during transmission to the host and during dissemination within the host, and it must disrupt immune challenges to successfully complete its infectious cycle. It has been proposed that B. burgdorferi can accomplish these tasks without an endogenous extra-cytoplasmic protease by commandeering plasminogen, the highly abundant precursor of the vertebrate protease plasmin. However, the molecular mechanism by which B. burgdorferi immobilizes plasminogen to its surface remains obscure. The data presented here demonstrate that the outer surface protein C (OspC) of B. burgdorferi is a potent plasminogen receptor on the outer membrane of the bacterium. OspC-expressing spirochetes readily bind plasminogen, whereas only background levels of plasminogen are detectable on OspC-deficient strains. Furthermore, plasminogen binding by OspC-expressing spirochetes can be significantly reduced using anti-OspC antibodies. Co-immunofluorescence staining assays demonstrate that wild-type bacteria immobilize plasminogen only if they are actively expressing OspC regardless of the expression of other surface proteins. The co-localization of plasminogen and OspC on OspC-expressing spirochetes further implicates OspC as a biologically relevant plasminogen receptor on the surface of live B. burgdorferi.
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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.