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Two\u2010dimensional electrophoresis analysis of <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content>. <jats:italic>burgdorferi<\/jats:italic>\u2005<jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>31<jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>3 and a strain that overexpresses <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> (<jats:styled-content style=\"fixed-case\">A3HtrAOE<\/jats:styled-content>) identified a downregulated protein in <jats:styled-content style=\"fixed-case\">A3HtrAOE<\/jats:styled-content> with a mass, pI and <jats:styled-content style=\"fixed-case\">MALDI\u2010TOF<\/jats:styled-content> spectrum consistent with outer membrane protein p66. <jats:styled-content style=\"fixed-case\">P<\/jats:styled-content>66 and <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> from cellular lysates partitioned into detergent\u2010resistant membranes, which contain cholesterol\u2010glycolipid\u2010rich membrane regions known as lipid rafts, suggesting that <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> and p66 may reside together in lipid rafts also. This agrees with previous work from our laboratory, which showed that <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> and p66 are constituents of <jats:styled-content style=\"fixed-case\"><jats:italic>B<\/jats:italic><\/jats:styled-content>. <jats:italic>burgdorferi<\/jats:italic> outer membrane vesicles. <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> degraded p66 <jats:italic>in vitro<\/jats:italic> and <jats:styled-content style=\"fixed-case\">A3HtrAOE<\/jats:styled-content> expressed reduced levels of p66 <jats:italic>in vivo<\/jats:italic>. Fluorescence confocal microscopy revealed that <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> and p66 colocalize in the membrane. The association of <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content> and p66 establishes that they could interact efficiently and their protease\/substrate relationship provides functional relevance to this interaction. <jats:styled-content style=\"fixed-case\">A3HtrAOE<\/jats:styled-content> also showed reduced levels of p66 transcript in comparison with wild\u2010type <jats:styled-content style=\"fixed-case\">B<\/jats:styled-content>31<jats:styled-content style=\"fixed-case\">A<\/jats:styled-content>3, indicating that <jats:styled-content style=\"fixed-case\">HtrA<\/jats:styled-content>\u2010mediated regulation of p66 may occur at multiple levels.<\/jats:p>","DOI":"10.1111\/mmi.13221","type":"journal-article","created":{"date-parts":[[2015,9,15]],"date-time":"2015-09-15T08:30:50Z","timestamp":1442305850000},"page":"135-150","source":"Crossref","is-referenced-by-count":21,"title":["<scp><i>B<\/i><\/scp><i>orrelia burgdorferi<\/i>\u2005<scp>HtrA<\/scp>: evidence for 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