{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T14:53:05Z","timestamp":1781880785714,"version":"3.54.5"},"reference-count":52,"publisher":"American Society for Microbiology","issue":"12","license":[{"start":{"date-parts":[[2014,6,15]],"date-time":"2014-06-15T00:00:00Z","timestamp":1402790400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,6,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Human-pathogenic\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bartonella henselae<\/jats:named-content>\n            causes cat scratch disease and vasculoproliferative disorders. An important pathogenicity factor of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. henselae<\/jats:named-content>\n            is the trimeric autotransporter adhesin (TAA)\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Bartonella<\/jats:named-content>\n            adhesin A (BadA), which is modularly constructed, consisting of a head, a long and repetitive neck-stalk module, and a membrane anchor. BadA is involved in bacterial autoagglutination, binding to extracellular matrix proteins and host cells, and in proangiogenic reprogramming. The slow growth of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. henselae<\/jats:named-content>\n            and limited tools for genetic manipulation are obstacles for detailed examination of BadA and its domains. Here, we established a recombinant expression system for BadA mutants in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>\n            allowing functional analysis of particular BadA domains. Using a BadA mutant lacking 21 neck-stalk repeats (BadA HN23), the BadA HN23 signal sequence was exchanged with that of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            OmpA, and the BadA membrane anchor was additionally replaced with that of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Yersinia<\/jats:named-content>\n            adhesin A (YadA). Constructs were cloned in\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            , and hybrid protein expression was detected by immunoblotting, fluorescence microscopy, and flow cytometry. Functional analysis revealed that BadA hybrid proteins mediate autoagglutination and binding to collagen and endothelial cells.\n            <jats:italic>In vivo<\/jats:italic>\n            , expression of this BadA construct correlated with higher pathogenicity of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">E. coli<\/jats:named-content>\n            in a\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Galleria mellonella<\/jats:named-content>\n            infection model.\n          <\/jats:p>","DOI":"10.1128\/jb.01461-13","type":"journal-article","created":{"date-parts":[[2014,3,29]],"date-time":"2014-03-29T03:28:25Z","timestamp":1396063705000},"page":"2155-2165","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":15,"title":["Heterologous Expression of Bartonella Adhesin A in Escherichia coli by Exchange of Trimeric Autotransporter Adhesin Domains Results in Enhanced Adhesion Properties and a Pathogenic Phenotype"],"prefix":"10.1128","volume":"196","author":[{"given":"Thomas","family":"Schmidgen","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie und Krankenhaushygiene, Klinikum der Goethe-Universit\u00e4t, Frankfurt am Main, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick O.","family":"Kaiser","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie und Krankenhaushygiene, Klinikum der Goethe-Universit\u00e4t, Frankfurt am Main, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wibke","family":"Ballhorn","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie und Krankenhaushygiene, Klinikum der Goethe-Universit\u00e4t, Frankfurt am Main, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bettina","family":"Franz","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie und Krankenhaushygiene, Klinikum der Goethe-Universit\u00e4t, Frankfurt am Main, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephan","family":"G\u00f6ttig","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Mikrobiologie und Krankenhaushygiene, Klinikum der Goethe-Universit\u00e4t, Frankfurt am Main, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk","family":"Linke","sequence":"additional","affiliation":[{"name":"Max-Planck-Institut f\u00fcr Entwicklungsbiologie, Abteilung Proteinevolution, T\u00fcbingen, Germany"},{"name":"Department of Biosciences, University of Oslo, Oslo, Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Volkhard A. 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