ArticleMolecular microbiology2009
Borrelia burgdorferi small lipoprotein Lp6.6 is a member of multiple protein complexes in the outer membrane and facilitates pathogen transmission from ticks to mice.
Article in Molecular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 53 citations in OpenAlex.
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- Targeting of interaction between BB0323-BB0238 informs new paradigms in Lyme disease therapeutics.PLoS pathogens · 2026Article
- Analysis of the BadR regulon in Borrelia burgdorferi.BMC microbiology · 2025Article
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- Recent Advances in Tick Antigen Discovery and Anti-Tick Vaccine Development.International journal of molecular sciences · 2023Review
- Dome1-JAK-STAT signaling between parasite and host integrates vector immunity and development.Science (New York, N.Y.) · 2023Article
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- Antibodies against EGF-like domains in Ixodes scapularis BM86 orthologs impact tick feeding and survival of Borrelia burgdorferi.Scientific reports · 2021Article
- DksA Controls the Response of the Lyme Disease SpirocheteJournal of bacteriology · 2019Article
- The RpoS Gatekeeper inFrontiers in microbiology · 2019Article
- Assessing the Contribution of an HtrA Family Serine Protease DuringFrontiers in cellular and infection microbiology · 2019Article
- Identification of Lyme borreliae proteins promoting vertebrate host blood-specific spirochete survival in Ixodes scapularis nymphs using artificial feeding chambers.Ticks and tick-borne diseases · 2018Article
- Polymorphic factor H-binding activity of CspA protects Lyme borreliae from the host complement in feeding ticks to facilitate tick-to-host transmission.PLoS pathogens · 2018Article
- Plasticity in early immune evasion strategies of a bacterial pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Comprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial Surface.Journal of bacteriology · 2017Article
- Global Tn-seq analysis of carbohydrate utilization and vertebrate infectivity of Borrelia burgdorferi.Molecular microbiology · 2016Article
- Interaction of the Lyme disease spirochete with its tick vector.Cellular microbiology · 2016Review
- Cyclic di-GMP modulates gene expression in Lyme disease spirochetes at the tick-mammal interface to promote spirochete survival during the blood meal and tick-to-mammal transmission.Infection and immunity · 2015Article
- BB0323 and novel virulence determinant BB0238: Borrelia burgdorferi proteins that interact with and stabilize each other and are critical for infectivity.The Journal of infectious diseases · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Borrelia burgdorferi lipoprotein Lp6.6 is a differentially produced spirochete antigen. An assessment of lp6.6 expression covering representative stages of the infectious cycle of spirochetes demonstrates that the gene is solely expressed during pathogen persistence in ticks. Deletion of lp6.6 in infectious B. burgdorferi did not influence in vitro growth, or its ability to persist and induce inflammation in mice, migrate to larval or nymphal ticks or survive through the larval-nymphal molt. However, Lp6.6-deficient spirochetes displayed significant impairment in their ability to transmit from infected ticks to naïve mice, which was restored upon genetic complementation of the mutant with a wild-type copy of lp6.6, establishing that Lp6.6 plays a role in pathogen transmission from ticks to mammals. Lp6.6 is a subsurface, yet highly abundant, outer membrane antigen. Two-dimensional blue native/SDS-PAGE coupled with liquid chromatography-mass spectrometry (LC-MS/MS) analysis and protein cross-linking studies independently shows that Lp6.6 exists in multiple protein complexes in the outer membrane. We speculate that the function of Lp6.6 is connected to the physiological processes of these membrane complexes. Further characterization of differentially produced membrane antigens and associated protein complexes will likely aid in our understanding of the molecular details of B. burgdorferi persistence and transmission through a complex enzootic cycle.
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