The Origin of 8-Amino-3,8-dideoxy-D-manno-octulosonic Acid (Kdo8N) in the Lipopolysaccharide of Shewanella oneidensis
- The Origin of 8-Amino-3,8-dideoxy-D-manno-octulosonic Acid (Kdo8N) in the Lipopolysaccharide of Shewanella oneidensis
- Samuel G. Gattis; 정학숙; M. Stephen Trent; Christian R. H. Raetz
- Kdo8N; Lipopolysaccharide; Shewanella oneidensis
- Issue Date
- The Journal of biological chemistry
- VOL 288, NO 13, 9216-9225
- Lipopolysaccharide (LPS; endotoxin) is an essential component
of the outer monolayer of nearly all Gram-negative bacteria.
LPS is composed of a hydrophobic anchor, known as lipid A,
an inner core oligosaccharide, and a repeating O-antigen polysaccharide.
In nearly all species, the first sugar bridging the
hydrophobic lipid A and the polysaccharide domain is 3-deoxy-
D-manno-octulosonic acid (Kdo), and thus it is critically important
for LPS biosynthesis. Modifications to lipid A have been
shown to be important for resistance to antimicrobial peptides
as well as modulating recognition by the mammalian innate
immune system. Therefore, lipid A derivatives have been used
for development of vaccine strains and vaccine adjuvants. One
derivative that has yet to be studied is 8-amino-3,8-dideoxy-Dmanno-
octulosonic acid (Kdo8N), which is found exclusively in
marine bacteria of the genus Shewanella. Using bioinformatics,
a candidate gene cluster for Kdo8N biosynthesis was identified
in Shewanella oneidensis. Expression of these genes recombinantly
in Escherichia coli resulted in lipid A containing Kdo8N,
and in vitro assays confirmed their proposed enzymatic function.
Both the in vivo and in vitro data were consistent with
direct conversion of Kdo to Kdo8N prior to its incorporation
into the Kdo8N-lipid A domain of LPS by a metal-dependent
oxidase followed by a glutamate-dependent aminotransferase.
To our knowledge, this oxidase is the first enzyme shown to
oxidize an alcohol using a metal and molecular oxygen, not
NAD(P) . Creation of an S. oneidensis in-frame deletion strain
showed increased sensitivity to the cationic antimicrobial peptide
polymyxin as well as bile salts, suggesting a role in outer
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