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We have previously reported clinical data to suggest that colonization factor I (CFA/I) fimbriae of enterotoxigenic  Escherichia coli  (ETEC) can bind to Lewis a (Le a ), a glycan epitope ubiquitous in the small intestinal mucosa of young children (<2 years of age), and individuals with a genetic mutation of  FUT2 . To further elucidate the physiological binding properties of this interaction, we engineered Chinese Hamster Ovary (CHO-K1) cells to express Le a  or Le b  determinants on both  N - and  O -glycans. We used our glyco-engineered CHO-K1 cell lines to demonstrate that CfaB, the major subunit of ETEC CFA/I fimbriae, as well as four related ETEC fimbriae, bind more to our CHO-K1 cell-line expressing Le a , compared to cells carrying Le b  or the CHO-K1 wild-type glycan phenotype. Furthermore, using  in-silico  docking analysis, we predict up to three amino acids (Glu 25 , Asn 27 , Thr 29 ) found in the immunoglobulin (Ig)-like groove region of CfaB of CFA/I and related fimbriae, could be important for the preferential and higher affinity binding of CFA/I fimbriae to the potentially structurally flexible Le a  glycan. These findings may lead to a better molecular understanding of ETEC pathogenesis, aiding in the development of vaccines and/or anti-infection therapeutics.

Glyco-engineered cell line and computational docking studies reveals enterotoxigenic Escherichia coli CFA/I fimbriae bind to Lewis a glycans