Role of pagL and lpxO in Bordetella bronchiseptica lipid A biosynthesis

I MacArthur, J W Jones, D R Goodlett, R K Ernst, Andrew Preston

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

PagL and LpxO are enzymes that modify lipid A. PagL is a 3-O deacylase that removes the primary acyl chain from the 3 position, and LpxO is an oxygenase that 2-hydroxylates specific acyl chains in the lipid A. pagL and lpxO homologues have been identified in the genome of Bordetella bronchiseptica, but in the current structure for B. bronchiseptica lipid A the 3 position is acylated and 2-OH acylation is not reported. We have investigated the role of B. bronchiseptica pagL and lpxO in lipid A biosynthesis. We report a different structure for wild-type (WT) B. bronchiseptica lipid A, including the presence of 2-OH-myristate, the presence of which is dependent on lpxO. We also demonstrate that the 3 position is not acylated in the major WT lipid A structures but that mutation of pagL results in the presence of 3-OH-decanoic acid at this position, suggesting that lipid A containing this acylation is synthesized but that PagL removes most of it from the mature lipid A. These data refine the structure of B. bronchiseptica lipid A and demonstrate that pagL and lpxO are involved in its biosynthesis.
Original languageEnglish
Pages (from-to)4726-4735
Number of pages10
JournalJournal of Bacteriology
Volume193
Issue number18
Early online date14 Jul 2011
DOIs
Publication statusPublished - Sep 2011

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Bordetella bronchiseptica
Lipid A
Acylation
Oxygenases
Myristic Acid
Genome

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Role of pagL and lpxO in Bordetella bronchiseptica lipid A biosynthesis. / MacArthur, I; Jones, J W; Goodlett, D R; Ernst, R K; Preston, Andrew.

In: Journal of Bacteriology, Vol. 193, No. 18, 09.2011, p. 4726-4735.

Research output: Contribution to journalArticle

MacArthur, I ; Jones, J W ; Goodlett, D R ; Ernst, R K ; Preston, Andrew. / Role of pagL and lpxO in Bordetella bronchiseptica lipid A biosynthesis. In: Journal of Bacteriology. 2011 ; Vol. 193, No. 18. pp. 4726-4735.
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