ArticleInfection and immunity2001
Coiling phagocytosis of Borrelia burgdorferi by primary human macrophages is controlled by CDC42Hs and Rac1 and involves recruitment of Wiskott-Aldrich syndrome protein and Arp2/3 complex.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
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- Molecular Mechanisms ofBiology · 2021Review
- Immune Response toCurrent issues in molecular biology · 2021Article
- A joint effort: The interplay between the innate and the adaptive immune system in Lyme arthritis.Immunological reviews · 2020Review
- Characterization of Stress and Innate Immunity Resistance of Wild-Type and ΔInfection and immunity · 2018Article
- Human neuroglial cells internalize Borrelia burgdorferi by coiling phagocytosis mediated by Daam1.PloS one · 2018Article
- Phagocytic Receptors Activate Syk and Src Signaling during Borrelia burgdorferi Phagocytosis.Infection and immunity · 2017Article
- Outer surface protein OspC is an antiphagocytic factor that protects Borrelia burgdorferi from phagocytosis by macrophages.Infection and immunity · 2015Article
- Mechanisms of Borrelia burgdorferi internalization and intracellular innate immune signaling.Frontiers in cellular and infection microbiology · 2014Review
- Phagosomal TLR signaling upon Borrelia burgdorferi infection.Frontiers in cellular and infection microbiology · 2014Review
- The formins FMNL1 and mDia1 regulate coiling phagocytosis of Borrelia burgdorferi by primary human macrophages.Infection and immunity · 2013Article
- Macrophage phagocytosis: effects of environmental pollutants, alcohol, cigarette smoke, and other external factors.Journal of leukocyte biology · 2011Review
- Downstream signals for MyD88-mediated phagocytosis of Borrelia burgdorferi can be initiated by TRIF and are dependent on PI3K.Journal of immunology (Baltimore, Md. : 1950) · 2009Article
- Activation of human monocytes by live Borrelia burgdorferi generates TLR2-dependent and -independent responses which include induction of IFN-beta.PLoS pathogens · 2009Article
- The origins of phagocytosis and eukaryogenesis.Biology direct · 2009Article
- Lyme arthritis: current concepts and a change in paradigm.Clinical and vaccine immunology : CVI · 2008Review
- Cdc42 and RhoB activation are required for mannose receptor-mediated phagocytosis by human alveolar macrophages.Molecular biology of the cell · 2005Article
- Opsonization modulates Rac-1 activation during cell entry by Leishmania amazonensis.Infection and immunity · 2002Article
- A role for cofilin and LIM kinase in Listeria-induced phagocytosis.The Journal of cell biology · 2001Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lyme borreliosis is a multisystemic disorder primarily affecting the skin, nervous system, and joints. It is caused by the spirochete Borrelia burgdorferi sensu lato and is transmitted via ticks of the Ixodidae family. Persistence of borreliae within macrophages has been implicated in the often chronic history of borreliosis. The uptake of B. burgdorferi by professional phagocytes occurs predominantly by coiling phagocytosis, a host cell-driven process in which single pseudopods wrap around and engulf the spirochetes. In the present study, we investigated the molecular machinery and the signal transduction pathways controlling the formation of these unique uptake structures. We found that the phagocytosis of borreliae by primary human macrophages is accompanied by the formation of f-actin-rich structures, which in their morphological organization correspond well to the earlier described coiling pseudopods. Further experiments revealed that Wiskott-Aldrich Syndrome protein and Arp2/3 complex, major regulators of actin polymerization, are also recruited to these sites of actin accumulation. In addition, inhibition of an upstream regulator of Wiskott-Aldrich Syndrome protein, the Rho-family GTPase CDC42Hs, greatly inhibited the occurrence of borrelia-induced phagocytic uptake structures. Inhibition of Rac1, another Rho family GTPase, had a less-pronounced inhibitory effect, while blocking of Rho activity showed no discernible influence. These results suggest that basic mechanisms of actin polymerization that control other types of phagocytosis are also functional in the formation of the morphologically unique uptake structures in coiling phagocytosis. Our findings should enhance the understanding of the infection process of B. burgdorferi and contribute to devising new strategies for countering Lyme disease.
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