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Int. J. Mol. Sci. 2017, 18(11), 2256; doi:10.3390/ijms18112256

The Glycosyltransferases of LPS Core: A Review of Four Heptosyltransferase Enzymes in Context

Department of Chemistry, Wesleyan University, Middletown, CT 06459, USA
Author to whom correspondence should be addressed.
Received: 29 September 2017 / Revised: 23 October 2017 / Accepted: 24 October 2017 / Published: 27 October 2017
(This article belongs to the Special Issue Lipopolysaccharides (LPSs))
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Bacterial antibiotic resistance is a rapidly expanding problem in the world today. Functionalization of the outer membrane of Gram-negative bacteria provides protection from extracellular antimicrobials, and serves as an innate resistance mechanism. Lipopolysaccharides (LPS) are a major cell-surface component of Gram-negative bacteria that contribute to protecting the bacterium from extracellular threats. LPS is biosynthesized by the sequential addition of sugar moieties by a number of glycosyltransferases (GTs). Heptosyltransferases catalyze the addition of multiple heptose sugars to form the core region of LPS; there are at most four heptosyltransferases found in all Gram-negative bacteria. The most studied of the four is HepI. Cells deficient in HepI display a truncated LPS on their cell surface, causing them to be more susceptible to hydrophobic antibiotics. HepI–IV are all structurally similar members of the GT-B structural family, a class of enzymes that have been found to be highly dynamic. Understanding conformational changes of heptosyltransferases are important to efficiently inhibiting them, but also contributing to the understanding of all GT-B enzymes. Finding new and smarter methods to inhibit bacterial growth is crucial, and the Heptosyltransferases may provide an important model for how to inhibit many GT-B enzymes. View Full-Text
Keywords: LPS; lipopolysaccharide; heptosyltransferase; protein dynamics; glycosyltransferase; GT-B; inhibitor design LPS; lipopolysaccharide; heptosyltransferase; protein dynamics; glycosyltransferase; GT-B; inhibitor design

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Cote, J.M.; Taylor, E.A. The Glycosyltransferases of LPS Core: A Review of Four Heptosyltransferase Enzymes in Context. Int. J. Mol. Sci. 2017, 18, 2256.

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