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Recombinant <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> exhibits proteolytic activity <jats:italic>in vitro<\/jats:italic>, while a mutant (<jats:styled-content style=\"fixed-case\">HtrABbS<\/jats:styled-content>198<jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>) does not. However, <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> and <jats:styled-content style=\"fixed-case\">DegP<\/jats:styled-content> have some important differences as well. Native <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> occurs in both membrane\u2010bound and soluble forms. Despite its homology to <jats:styled-content style=\"fixed-case\">DegP<\/jats:styled-content>, <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> could not complement an <jats:italic><jats:styled-content style=\"fixed-case\">E<\/jats:styled-content>.\u2009coli<\/jats:italic>\u2005<jats:styled-content style=\"fixed-case\">DegP<\/jats:styled-content> deletion mutant. Late stage Lyme disease patients, as well as infected mice and rabbits developed a robust antibody response to <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content>, indicating that it is a <jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>\u2010cell antigen. In co\u2010immunoprecipitation studies, a number of potential binding partners for <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> were identified, as well as two specific proteolytic substrates, basic membrane protein D (<jats:styled-content style=\"fixed-case\">BmpD<\/jats:styled-content>\/<jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0385) and chemotaxis signal transduction phosphatase <jats:styled-content style=\"fixed-case\">CheX<\/jats:styled-content> (<jats:styled-content style=\"fixed-case\">BB<\/jats:styled-content>0671). <jats:styled-content style=\"fixed-case\">HtrABb<\/jats:styled-content> may function in regulating outer membrane lipoproteins and in modulating the chemotactic response of <jats:italic><jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>.\u2009burgdorferi<\/jats:italic>.<\/jats:p>","DOI":"10.1111\/mmi.12213","type":"journal-article","created":{"date-parts":[[2013,4,9]],"date-time":"2013-04-09T07:39:48Z","timestamp":1365493188000},"page":"619-633","source":"Crossref","is-referenced-by-count":51,"title":["The <scp>HtrA<\/scp> protease of <i><scp>B<\/scp>orrelia burgdorferi<\/i> degrades outer membrane protein <scp>BmpD<\/scp> and chemotaxis phosphatase <scp>CheX<\/scp>"],"prefix":"10.1111","volume":"88","author":[{"given":"James L.","family":"Coleman","sequence":"first","affiliation":[{"name":"New York State Department of Health Stony Brook University  Stony Brook NY 11794\u20105120 USA"},{"name":"Department of Molecular Genetics and Microbiology Center for Infectious Diseases Stony Brook University  Stony Brook NY 11794\u20105120 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jameson 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