TY - JOUR
T1 - BpaB and EbfC DNA-binding proteins regulate production of the Lyme disease spirochete's infection-associated Erp surface proteins
AU - Jutras, Brandon L.
AU - Verma, Ashutosh
AU - Adams, Claire A.
AU - Brissette, Catherine A.
AU - Burns, Logan H.
AU - Whetstine, Christine R.
AU - Bowman, Amy
AU - Chenail, Alicia M.
AU - Zückert, Wolfram R.
AU - Stevenson, Brian
PY - 2012/2
Y1 - 2012/2
N2 - Vector-borne pathogens regulate their protein expression profiles, producing factors during host infection that differ from those produced during vector colonization. The Lyme disease agent, Borrelia burgdorferi, produces Erp surface proteins throughout mammalian infection and represses their synthesis during colonization of vector ticks. Known functions of Erp proteins include binding of host laminin, plasmin(ogen), and regulators of complement activation. A DNA region immediately 5' of erp operons, the erp operator, is required for transcriptional regulation. The B. burgdorferi BpaB and EbfC proteins exhibit high in vitro affinities for erp operator DNA. In the present studies, chromatin immunoprecipitation (ChIP) demonstrated that both proteins bind erp operator DNA in vivo. Additionally, a combination of in vivo and in vitro methods demonstrated that BpaB functions as a repressor of erp transcription, while EbfC functions as an antirepressor.
AB - Vector-borne pathogens regulate their protein expression profiles, producing factors during host infection that differ from those produced during vector colonization. The Lyme disease agent, Borrelia burgdorferi, produces Erp surface proteins throughout mammalian infection and represses their synthesis during colonization of vector ticks. Known functions of Erp proteins include binding of host laminin, plasmin(ogen), and regulators of complement activation. A DNA region immediately 5' of erp operons, the erp operator, is required for transcriptional regulation. The B. burgdorferi BpaB and EbfC proteins exhibit high in vitro affinities for erp operator DNA. In the present studies, chromatin immunoprecipitation (ChIP) demonstrated that both proteins bind erp operator DNA in vivo. Additionally, a combination of in vivo and in vitro methods demonstrated that BpaB functions as a repressor of erp transcription, while EbfC functions as an antirepressor.
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U2 - 10.1128/JB.06394-11
DO - 10.1128/JB.06394-11
M3 - Article
C2 - 22155777
AN - SCOPUS:84855863354
SN - 0021-9193
VL - 194
SP - 778
EP - 786
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 4
ER -