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- W2136333721 abstract "ABSTRACT Lyme disease is a multisystemic disorder caused by Borrelia burgdorferi infection. Upon infection, some B. burgdorferi genes are upregulated, including members of the microbial surface components recognizing adhesive matrix molecule (MSCRAMM) protein family, which facilitate B. burgdorferi adherence to extracellular matrix components of the host. Comparative genome analysis has revealed a new family of B. burgdorferi 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 in vitro 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." @default.
- W2136333721 created "2016-06-24" @default.
- W2136333721 creator A5021137999 @default.
- W2136333721 creator A5026194186 @default.
- W2136333721 creator A5055695025 @default.
- W2136333721 creator A5082168636 @default.
- W2136333721 date "2013-08-01" @default.
- W2136333721 modified "2023-10-15" @default.
- W2136333721 title "BB0172, a Borrelia burgdorferi Outer Membrane Protein That Binds Integrin α <sub>3</sub> β <sub>1</sub>" @default.
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- W2136333721 doi "https://doi.org/10.1128/jb.00187-13" @default.
- W2136333721 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3719542" @default.
- W2136333721 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23687274" @default.
- W2136333721 hasPublicationYear "2013" @default.
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