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• W1968133795 abstract "Bordetella bronchiseptica PagP (PagP BB ) is a lipid A palmitoyl transferase that is required for resistance to antibody-dependent complement-mediated killing in a murine model of infection. B. parapertussis contains a putative pagP homolog (encoding B. parapertussis PagP [PagP BPa ]), but its role in the biosynthesis of lipid A, the membrane anchor of lipopolysaccharide (LPS), has not been investigated. Mass spectrometry analysis revealed that wild-type B. parapertussis lipid A consists of a heterogeneous mixture of lipid A structures, with penta- and hexa-acylated structures containing one and two palmitates, respectively. Through mutational analysis, we demonstrate that PagP BPa is required for the modification of lipid A with palmitate. While PagP BB transfers a single palmitate to the lipid A C-3′ position, PagP BPa transfers palmitates to the lipid A C-2 and C-3′ positions. The addition of two palmitate acyl chains is unique to B. parapertussis . Mutation of pagP BPa resulted in a mutant strain with increased sensitivity to antimicrobial peptide killing and decreased endotoxicity, as evidenced by reduced proinflammatory responses via Toll-like receptor 4 (TLR4) to the hypoacylated LPS. Therefore, PagP-mediated modification of lipid A regulates outer membrane function and may be a means to modify interactions between the bacterium and its human host during infection." @default.
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• W1968133795 date "2014-11-24" @default.
• W1968133795 modified "2023-09-25" @default.
• W1968133795 title "Bordetella parapertussis PagP Mediates the Addition of Two Palmitates to the Lipopolysaccharide Lipid A" @default.
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• W1968133795 doi "https://doi.org/10.1128/jb.02236-14" @default.
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