Interaction of Borrelia burgdorferi Hbb with the p66 promoter
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چکیده
منابع مشابه
Interaction of Borrelia burgdorferi Hbb with the p66 promoter
Borrelia burgdorferi, an agent of Lyme disease, encodes the beta(3)-chain integrin ligand P66. P66 is expressed by B. burgdorferi in the mammal, in laboratory media, and as the bacteria are acquired or transmitted by the tick, but is not expressed by the bacterium in unfed ticks. Attempts to reveal factors influencing expression revealed that P66 was expressed in all in vitro conditions investi...
متن کاملCross-Reactive Epitopes in Borrelia burgdorferi p66.
Epitope mapping of the p66 outer membrane protein of Borrelia burgdorferi revealed that the protein contains numerous cross-reactive linear epitopes recognized by serum antibody in the majority of individuals tested, regardless of Lyme disease history, limiting the usefulness of this antigen in Lyme disease serodiagnostic assays.
متن کاملThe Oms66 (p66) protein is a Borrelia burgdorferi porin.
In this study we report the purification and characterization of a 66-kDa protein, designated Oms66, for outer membrane-spanning 66-kDa protein, that functions as a porin in the outer membrane (OM) of Borrelia burgdorferi. Oms66 was purified by fast-performance liquid chromatography and exhibited an average single-channel conductance of 9.62 +/- 0.37 nS in 1 M KCl, as evidenced by 581 individua...
متن کاملUse of Nonelectrolytes Reveals the Channel Size and Oligomeric Constitution of the Borrelia burgdorferi P66 Porin
In the Lyme disease spirochete Borrelia burgdorferi, the outer membrane protein P66 is capable of pore formation with an atypical high single-channel conductance of 11 nS in 1 M KCl, which suggested that it could have a larger diameter than 'normal' Gram-negative bacterial porins. We studied the diameter of the P66 channel by analyzing its single-channel conductance in black lipid bilayers in t...
متن کاملIntegrin binding by Borrelia burgdorferi P66 facilitates dissemination but is not required for infectivity
P66, a Borrelia burgdorferi surface protein with porin and integrin-binding activities, is essential for murine infection. The role of P66 integrin-binding activity in B. burgdorferi infection was investigated and found to affect transendothelial migration. The role of integrin binding, specifically, was tested by mutation of two amino acids (D205A,D207A) or deletion of seven amino acids (Del20...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2009
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/gkp1027