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Distinct Glycan Structures Of Uroplakins Ia And Ib, Bo Xie, Ge Zhou, Shiu-Yung Chan, Ellen Shapiro, Xiant-Peng Kong, Xue-Ru Wu, Tung-Tien Sun, Catherine E. Costello
Distinct Glycan Structures Of Uroplakins Ia And Ib, Bo Xie, Ge Zhou, Shiu-Yung Chan, Ellen Shapiro, Xiant-Peng Kong, Xue-Ru Wu, Tung-Tien Sun, Catherine E. Costello
Bo Xie
Although it has been shown that mouse uroplakin (UP) Ia, a major glycoprotein of urothelial apical surface, can serve as the receptor for the FimH lectin adhesin of type 1-fimbriated Escherichia coli, the organism that causes a great majority of urinary tract infections, the glycan structure of this native receptor was unknown. Using a sensitive approach that combines in-gel glycosidase and protease digestions, permethylation of released glycans, and mass spectrometry, we have elucidated for the first time the native glycoform structures of the mouse UPIa receptor and those of its non-binding homolog, UPIb, and have determined the glycosylation site occupancy. …