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Upon infection, some\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. burgdorferi<\/jats:named-content>\n            proteins containing the von Willebrand factor A (vWFA) domain. In the present study, we characterized the expression and membrane association of the vWFA domain-containing protein BB0172 by using\n            <jats:italic>in vitro<\/jats:italic>\n            transcription\/translation systems in the presence of microsomal membranes and with detergent phase separation assays. Our results showed evidence of BB0172 localization in the outer membrane, the orientation of the vWFA domain to the extracellular environment, and its function as a metal ion-dependent integrin-binding protein. This is the first report of a borrelial adhesin with a metal ion-dependent adhesion site (MIDAS) motif that is similar to those observed in eukaryotic integrins and has a similar function.\n          <\/jats:p>","DOI":"10.1128\/jb.00187-13","type":"journal-article","created":{"date-parts":[[2013,5,18]],"date-time":"2013-05-18T06:08:34Z","timestamp":1368857314000},"page":"3320-3330","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":21,"title":["BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin \u03b1\n            <sub>3<\/sub>\n            \u03b2\n            <sub>1<\/sub>"],"prefix":"10.1128","volume":"195","author":[{"given":"Elaine","family":"Wood","sequence":"first","affiliation":[{"name":"Department of Veterinary Pathobiology, College of Veterinary Medicine and Biomedical Sciences, Texas A&amp;M University, College Station, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia","family":"Tamborero","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Faculty of Biology, Burjassot, Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ismael","family":"Mingarro","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Faculty of Biology, Burjassot, Valencia, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria D.","family":"Esteve-Gassent","sequence":"additional","affiliation":[{"name":"Department of Veterinary Pathobiology, College of Veterinary Medicine and Biomedical Sciences, Texas A&amp;M University, College Station, Texas, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro2714"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.112408.134040"},{"key":"e_1_3_2_4_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1574-695X.2012.00980.x","article-title":"The role of Borrelia burgdorferi outer surface proteins","volume":"66","author":"Kenedy MR","year":"2012","unstructured":"KenedyMRLenhartTRAkinsDR. 2012. 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