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Glyco-engineered cell line and computational docking studies reveals enterotoxigenic Escherichia coli CFA/I fimbriae bind to Lewis a glycans
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Glyco-engineered cell line and computational docking studies reveals enterotoxigenic Escherichia coli CFA/I fimbriae bind to Lewis a glycans
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Journal Article
Glyco-engineered cell line and computational docking studies reveals enterotoxigenic Escherichia coli CFA/I fimbriae bind to Lewis a glycans
2018
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
