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Borrelia burgdorferi regulates expression of complement regulator-acquiring surface protein 1 during the mammal-tick infection cycle

During the natural mammal-tick infection cycle, the Lyme disease spirochete Borrelia burgdorferi comes into contact with components of the alternative complement pathway. B. burgdorferi, like many other human pathogens, has evolved the immune evasion strategy of binding two host-derived fluid-phase...

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Main Authors: Lackum, Kate von (Author) , Miller, Jennifer C. (Author) , Bykowski, Tomasz (Author) , Riley, Sean P. (Author) , Woodman, Michael E. (Author) , Brade, Volker (Author) , Kraiczy, Peter (Author) , Stevenson, Brian (Author) , Wallich, Reinhard (Author)
Format: Article (Journal)
Language:English
Published: 2005
In: Infection and immunity
Year: 2005, Volume: 73, Issue: 11, Pages: 7398-7405
ISSN:1098-5522
DOI:10.1128/IAI.73.11.7398-7405.2005
Online Access:Verlag, lizenzpflichtig, Volltext: https://dx.doi.org/10.1128/IAI.73.11.7398-7405.2005
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Author Notes:Kate von Lackum, Jennifer C. Miller, Tomasz Bykowski, Sean P. Riley, Michael E. Woodman, Volker Brade, Peter Kraiczy, Brian Stevenson, and Reinhard Wallich

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520 |a During the natural mammal-tick infection cycle, the Lyme disease spirochete Borrelia burgdorferi comes into contact with components of the alternative complement pathway. B. burgdorferi, like many other human pathogens, has evolved the immune evasion strategy of binding two host-derived fluid-phase regulators of complement, factor H and factor H-like protein 1 (FHL-1). The borrelial complement regulator-acquiring surface protein 1 (CRASP-1) is a surface-exposed lipoprotein that binds both factor H and FHL-1. Analysis of CRASP-1 expression during the mammal-tick infectious cycle indicated that B. burgdorferi expresses this protein during mammalian infection, supporting the hypothesized role for CRASP-1 in immune evasion. However, CRASP-1 synthesis was repressed in bacteria during colonization of vector ticks. Analysis of cultured bacteria indicated that CRASP-1 is differentially expressed in response to changes in pH. Comparisons of CRASP-1 expression patterns with those of other infection-associated B. burgdorferi proteins, including the OspC, OspA, and Erp proteins, indicated that each protein is regulated through a unique mechanism. 
650 4 |a Animals 
650 4 |a Bacterial Proteins 
650 4 |a Blood Proteins 
650 4 |a Borrelia burgdorferi 
650 4 |a Complement C3b Inactivator Proteins 
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650 4 |a Evolution, Molecular 
650 4 |a Female 
650 4 |a Gene Expression Regulation, Bacterial 
650 4 |a Hydrogen-Ion Concentration 
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650 4 |a Mammals 
650 4 |a Membrane Proteins 
650 4 |a Mice 
650 4 |a Mice, Inbred BALB C 
650 4 |a Nymph 
650 4 |a Rabbits 
650 4 |a Ticks 
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