Abstract:
:The lipid A moiety of lipopolysaccharide forms the outer monolayer of the outer membrane of most gram-negative bacteria. Escherichia coli lipid A is synthesized on the cytoplasmic surface of the inner membrane by a conserved pathway of nine constitutive enzymes. Following attachment of the core oligosaccharide, nascent core-lipid A is flipped to the outer surface of the inner membrane by the ABC transporter MsbA, where the O-antigen polymer is attached. Diverse covalent modifications of the lipid A moiety may occur during its transit from the outer surface of the inner membrane to the outer membrane. Lipid A modification enzymes are reporters for lipopolysaccharide trafficking within the bacterial envelope. Modification systems are variable and often regulated by environmental conditions. Although not required for growth, the modification enzymes modulate virulence of some gram-negative pathogens. Heterologous expression of lipid A modification enzymes may enable the development of new vaccines.
journal_name
Annu Rev Biochemjournal_title
Annual review of biochemistryauthors
Raetz CR,Reynolds CM,Trent MS,Bishop REdoi
10.1146/annurev.biochem.76.010307.145803subject
Has Abstractpub_date
2007-01-01 00:00:00pages
295-329eissn
0066-4154issn
1545-4509journal_volume
76pub_type
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