Borrelia burgdorferi sensu stricto invasiveness is correlated with OspC–plasminogen affinity

Lagal, Vanessa; Portnoı̈, Denis; Faure, Grazyna; Postić, D.; Baranton, Guy

doi:10.1016/j.micinf.2005.08.017

Cited by 114 publications

(116 citation statements)

References 54 publications

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“…Several plasminogen-binding proteins have been characterized, including Tuf from P. aeruginosa (23), the PE protein of Haemophilus influenzae (59), Lsa20 from Leptospira interrogans (60), enolases from S. pneumoniae and Neisseria meningitidis (61,62), and Gpm1p as well as Pra1 from the invasive yeast C. albicans (26,27). For B. burgdorferi, a number of plasminogen-binding proteins have been reported, including OspA (31) and OspC (32), BPBP (30), and more recently B. burgdorferi enolase (34 -36). Of note, the functionally related but genetically heterologous complement regulator-acquiring surface proteins CspA, CspZ, ErpP, ErpC, and ErpA all bind plasminogen in addition to binding various host-derived complement regulators (28,29,(63)(64)(65)(66).…”

Section: Discussionmentioning

confidence: 99%

“…Several B. burgdorferi plasminogen-binding proteins have been identified, such as the infection-associated surface proteins CspA (complement regulator-acquiring surface protein 1; CRASP-1) and CspZ (CRASP-2) (28), ErpP (CRASP-3), ErpC (CRASP-4), ErpA (CRASP-5) (29), the 70-kDa surface protein BPBP (30), OspA (31), and OspC, which a recent study, employing live cell binding assays, has shown to be a plasminogen receptor on the surface of B. burgdorferi (32,33). Additionally, B. burgdorferi enolase has recently been demonstrated to moonlight on the bacterial outer surface and serve as a plasminogen-binding protein (34 -36).…”

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confidence: 99%

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BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Koenigs

Hammerschmidt

Jutras

et al. 2013

Journal of Biological Chemistry

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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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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Koenigs

Hammerschmidt

Jutras

et al. 2013

Journal of Biological Chemistry

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“…The evolutionary reason for this tick cooperation with its own pathogen is open to question. Newly published data attribute to OspC plasminogen binding activity as was described for OspA above 112 . However, OspC is not the only protein involved in immune evasion.…”

Section: Outer Surface Protein Cmentioning

confidence: 92%

Biological Aspects of Lyme Disease Spirochetes: Unique Bacteria of the Borrelia Burgdorferi Species Group

Křupka¹,

Raška²,

Bĕláková³

et al. 2007

Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub

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Background: Borrelia burgdorferi sensu lato is a group of at least twelve closely related species some of which are responsible for Lyme disease, the most frequent zoonosis in Europe and the USA. Many of the biological features of Borrelia are unique in prokaryotes and very interesting not only from the medical viewpoint but also from the view of molecular biology.Methods: Relevant recent articles were searched using PubMed and Google search tools. Results and Conclusion:This is a review of the biological, genetic and physiological features of the spirochete species group, Borrelia burgdorferi sensu lato. In spite of a lot of recent articles focused on B. burgdorferi sensu lato, many features of Borrelia biology remain obscure. It is one of the main reasons for persisting problems with prevention, diagnosis and therapy of Lyme disease. The aim of the review is to summarize ongoing current knowledge into a lucid and comprehensible form.

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“…Some studies have found a correlation between OspC type and wild rodent host specificity [129], but others found no such link [130]. The OspC types of human clinical isolates have also been correlated with invasive and non-invasive phenotypes [128,131]. However, similar studies demonstrated greater diversity among invasive types than previously recognized, calling into question any causative effect of OspC sequence on invasion [130,132].…”

Section: B Burgdorferi Products Required For Mammalian Infectionmentioning

confidence: 99%

“…Carefully controlling for variables other than OspC has not been possible in such studies, since additional genome components of these isolates also differ. Recently, the invasive OspC protein types were shown to bind plasminogen [131], a trait shared with other B. burgdorferi proteins [133,134] that was suggested to facilitate B. burgdorferi infection of mammals and ticks [135].…”

Section: B Burgdorferi Products Required For Mammalian Infectionmentioning

confidence: 99%

Biology of Infection with Borrelia burgdorferi

Tilly

Rosa

Stewart

2008

Infectious Disease Clinics of North America

183

177

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The spirochete Borrelia burgdorferi is a tick-borne obligate parasite whose normal reservoir is a variety of small mammals [1]. Whereas infection of these natural hosts does not lead to disease, infection of humans can result in Lyme disease, as a consequence of the human immunopathological response to B. burgdorferi [2,3]. Consistent with the pathogenesis of Lyme disease, bacterial products that allow B. burgdorferi to replicate and survive, rather than true "virulence factors," appear to be primarily what is required for the bacterium to cause disease in a susceptible host. In support of this idea, the genome sequence of B31, the type strain of B. burgdorferi sensu stricto [4,5], revealed that the bacterium lacks factors common to many bacterial pathogens, such as lipopolysaccharide, toxins, and specialized secretion systems. In this chapter, we will describe the basic biology of B. burgdorferi, and some of the bacterial components required to infect and survive in the mammalian and tick hosts.

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Borrelia burgdorferi sensu stricto invasiveness is correlated with OspC–plasminogen affinity

Cited by 114 publications

References 54 publications

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

BBA70 of Borrelia burgdorferi Is a Novel Plasminogen-binding Protein

Biological Aspects of Lyme Disease Spirochetes: Unique Bacteria of the Borrelia Burgdorferi Species Group

Biology of Infection with Borrelia burgdorferi

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