A penicillin-binding protein inhibits selection of colistin-resistant, lipooligosaccharide-deficient Acinetobacter baumannii
Abstract
Antimicrobial drug resistance is a major threat to public health. Gram-negative bacteria are exceptionally resistant to antibiotics because of their outer-membrane barrier. Glycolipids called lipopolysaccharide (LPS) or lipooligosaccharide (LOS) fortify the outer membrane from many antimicrobials and biocides and were thought to be essential for Gram-negative bacterial survival. The last-resort treatment for multidrug-resistant Gram-negative infections is colistin, which targets the lipid A domain of LPS/LOS to disrupt the membrane, but the emerging pathogen Acinetobacter baumannii can develop colistin resistance by inactivating lipid A biosynthesis. This analysis advances our understanding of lipid A/LOS essentiality in A. baumannii and identifies antimicrobial targets.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Sep 28, 2016
- Source ID
- 10.1073/pnas.1611594113
Entities
People
- Alexander A. Crofts
- Bryan W Davies
- Joseph M. Boll
- Katharina Peters
- M Stephen Trent
- Vincent Cattoir
- Waldemar Vollmer
Organizations
- Army Research Office
- Division of Intramural Research, National Institute of Allergy and Infectious Diseases
- National Institute of General Medical Sciences
- Newcastle University
- University of Georgia
- University of Texas at Austin
- Wellcome Trust