2013
DOI: 10.1074/jbc.m112.413872
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BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Abstract: Background: Recruitment of plasminogen is important for efficient dissemination of Borrelia burgdorferi. Results: BBA70 of B. burgdorferi binds plasminogen, and following activation, bound plasmin can cleave fibrinogen and inactivate the key complement components C3b and C5. Conclusion: BBA70 is a potent plasminogen-binding protein.Significance: Investigation suggests that binding of plasminogen may aid in pathogen dissemination and inhibit bacteriolytic effects of the host complement system.

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Cited by 58 publications
(69 citation statements)
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References 90 publications
(90 reference statements)
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“…It was previously shown that plasminogen bound at the surface of cells of the respiratory pathogen H. influenzae degrades C3b (27). In parallel, Borrelia burgdorferi recruits plasminogen and inactivates C3b as well as C5 to escape the innate immune system (25). Similar to those findings, we observed that M. catarrhalis with plasmin at the bacterial surface also degrades C3b and C5, which most likely contributes to increased resistance against serum-mediated killing.…”
Section: Discussionsupporting
confidence: 78%
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“…It was previously shown that plasminogen bound at the surface of cells of the respiratory pathogen H. influenzae degrades C3b (27). In parallel, Borrelia burgdorferi recruits plasminogen and inactivates C3b as well as C5 to escape the innate immune system (25). Similar to those findings, we observed that M. catarrhalis with plasmin at the bacterial surface also degrades C3b and C5, which most likely contributes to increased resistance against serum-mediated killing.…”
Section: Discussionsupporting
confidence: 78%
“…Another approach used by microbes to degrade the ECM is to attract the zymogen plasminogen. It has been reported that when plasminogen is bound to pathogens, it contributes to adherence to host tissues (29), degradation of ECM proteins resulting in increased invasion (30), and, finally, degradation of complement (25). Interestingly, our present results also suggest that M. catarrhalis utilizes host plasminogen to escape from the innate host defense.…”
Section: Discussionsupporting
confidence: 74%
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“…Plasminogen not only binds complement proteins such as C3 and C5, but has also been shown to cleave C3b and C5 upon activation to active plasmin (40). Interestingly, many pathogenic microorganisms acquire these inhibitors (including but not limited to C4BP and plasminogen) to establish an infection and evade the constant attack of complement (27,29,(41)(42)(43)(44).…”
Section: C4bp-plasminogen Interactionmentioning
confidence: 99%