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Current Pharmaceutical Design

Editor-in-Chief

ISSN (Print): 1381-6128
ISSN (Online): 1873-4286

Lipid A Biosynthesis of Multidrug-Resistant Pathogens - A Novel Drug Target

Author(s): Chang-Ro Lee, Jung Hun Lee, Byeong Chul Jeong and Sang Hee Lee

Volume 19, Issue 36, 2013

Page: [6534 - 6550] Pages: 17

DOI: 10.2174/13816128113199990494

Price: $65

Abstract

The rapid increase of human infections by multidrug-resistant (MDR) Gram-negative pathogens poses a serious health threat and demands the identification of new strategies, molecular targets, and agents for the treatment of Gram-negative bacterial infections. The biosynthesis of lipid A, the membrane-anchoring portion of lipopolysaccharide (LPS), is one promising target for novel antibiotic design because lipid A is essential for LPS assembly in most Gram-negative bacteria. The first three enzymes in the biosynthesis of lipid A, UDP-N-acetylglucosamine acyltransferase (LpxA), UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase (LpxC) and UDP- 3-O-(R-3-hydroxyacyl)glucosamine N-acyltransferase (LpxD), have emerged as an attractive Gram-negative antibacterial molecular target. In this article, we review recent advances in the studies on the structures and the structure-based drug designs of the three enzymes.

Keywords: Multidrug-resistant pathogens, lipid A biosynthesis, acyltransferase, deacetylase, chemotherapy.


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