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The PapG Adhesion of Uropathogenic Escherichia coli Contains Separate Regions for Receptor Binding and for the Incorporation into the Pilus

Scott J. Hultgren, Frederik Lindberg, Goran Magnusson, Jan Kihlberg, Jan M. Tennent and Staffan Normark
Proceedings of the National Academy of Sciences of the United States of America
Vol. 86, No. 12 (Jun. 15, 1989), pp. 4357-4361
Stable URL: http://www.jstor.org/stable/33689
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The PapG Adhesion of Uropathogenic Escherichia coli Contains Separate Regions for Receptor Binding and for the Incorporation into the Pilus
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Abstract

Most uropathogenic strains of Escherichia coli produce heteropolymeric organelles, known as P pili, that bind to the globoseries of glycolipids present in the urinary tract. The formation of a P pilus is the result of a family of related proteins being coordinately assembled into the structure in a defined order with the adhesin located exclusively at the tip. The preassembled digalactoside α -D-galactopyranosyl-(1→ 4)-β -D-galactopyranose-binding adhesin was purified to homogeneity from the periplasmic space in a complex with the periplasmic assembly protein PapD by affinity chromatography to α -D-galactopyranosyl-(1→ 4)-β -D-galactopyranose-Sepharose. A receptor-binding domain was mapped to the amino-terminal half of the adhesin. The interaction of PapD with PapG, which was required for the incorporation of the adhesin into the pilus, was found to protect PapG from proteolytic cleavages and enhanced the processing of the PapG signal peptide. A preassembly domain necessary for forming a complex with PapD was mapped to the carboxyl terminus of PapG.

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