Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding

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• 作者：Rie Jø ; nsson^a ; ^b ; ¹ ; Bing Liu^c ; ¹ ; Carsten Struve^b ; Yi Yang^c ; René ; Jø ; rgensen^b ; Yingqi Xu^c ; Hå ; vard Jenssen^a ; Karen A Krogfelt^b ; ^kak@ssi.dk ; Steve Matthews^c ; ^{s.j.matthews@imperial.ac.uk}
• 关键词：EAEC ; Enteroaggregative Escherichia coli ; AAF ; aggregative adherence fimbriae ; NMR ; nuclear magnetic resonance ; ECM ; extracellular matrix ; SPR ; surface plasmon resonance ; SDS-PAGE ; sodium dodecyl sulphate polyacrylamide gel electrophoresis ; Ig ; immunoglobulin ; CU ; chaperone-usher ; RMSD ; root mean square deviation ; ELISA ; enzyme-linked immunosorbent assay ; TOCSY ; total correlation (TOCSY) spectroscopy ; NOE ; nuclear Overhauser effect ; DMEM ; Dulbecco's modified Eagle's medium
• 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
• 出版年：2017
• 出版时间：March 2017
• 年：2017
• 卷：1865
• 期：3
• 页码：304-311
• 全文大小：1470 K
• 卷排序：1865

文摘

AAF/V expressing strain show no specificity to extracellular matrix (ECM) proteins compared to the uncoated wells. Agg5A share structural similarity to the two previously described AAF subunits AggA and AafA. Fibronectin binding is restored by substitution of a single aspartic acid to lysine.