ArticleTicks and tick-borne diseases2020
A soft tick Ornithodoros moubata salivary protein OmCI is a potent inhibitor to prevent avian complement activation.
Article in Ticks and tick-borne diseases, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Ticks' tricks: immunomodulatory effects of ixodid tick saliva at the cutaneous tick-host interface.Frontiers in immunology · 2025Review
- Structural evolution of an immune evasion determinant shapes pathogen host tropism.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Phylogenomic Diversity Elucidates Mechanistic Insights into Lyme Borreliae-Host Association.mSystems · 2022Article
- Utilizing Two Borrelia bavariensis Isolates Naturally Lacking the PFam54 Gene Array To Elucidate the Roles of PFam54-Encoded Proteins.Applied and environmental microbiology · 2022Article
- Bactericidal activity of avian complement: a contribution to understand avian-host tropism of Lyme borreliae.Parasites & vectors · 2021Article
- Host tropism determination by convergent evolution of immunological evasion in the Lyme disease system.PLoS pathogens · 2021Article
- Immunomodulatory Proteins in Tick Saliva From a Structural Perspective.Frontiers in cellular and infection microbiology · 2021Review
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Authors and funding
8 authors at 6 institutions in 3 countries.
Funding
Abstract
Complement is a key first line innate host defense system in the blood of vertebrates. Upon activation, this powerful defense mechanism can elicit inflammatory responses, lyse non-self-cells, or mark them for opsonophagocytic removal. Blood-feeding arthropods thus require the ability to block host complement activation in the bloodmeal to prevent undesired cell or tissue damage during feeding. The soft tick Ornithodoros moubata produces a complement inhibitory protein, OmCI. This protein binds to a mammalian complement protein C5 and blocks further activation of complement cascades, which results in the prevention of complement-mediated bacterial killing through membrane attack complex. Interestingly, the amino acids involved in OmCI binding are highly conserved among mammalian and avian C5, but the ability of this protein to inhibit the complement from birds remains unclear. Here we demonstrated that OmCI is capable of preventing quail complement-mediated erythrocyte lysis, inhibiting the capability of this animal's complement to eliminate a serum-sensitive Lyme disease bacterial strain. We also found that the ability of OmCI to inhibit quail complement-mediated killing of Lyme disease bacteria can be extended to different domestic and wild birds. Our results illustrate the utility of OmCI to block bird complement. These results provide the foundation for further use of this protein as a tool to study the molecular basis of avian complement and pathogen evasion to such a defense mechanism.
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