Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

pagP - lipid A palmitoyltransferase PagP

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Merighi, M. et al., Raetz, C.R., Bishop, R.E. et al.

Raetz,

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Disease relevance of pagP

Additional pagP homologs are encoded in the genomes of YERSINIA: and BORDETELLA: species [1].
The Salmonella PhoP/PhoQ-activated gene pagP is required for resistance to cationic antimicrobial peptides and for biosynthesis of hepta-acylated lipid A species containing palmitate [2].

High impact information on pagP

Upregulation in cultured J774A.1 macrophages was shown for pmrH, pagP (LPS palmitate addition), and ssaB (pathogenicity island II secretion) but not for prgH (pathogenicity island I secretion) [3].
The observation of pmrH and pagP expression in the intestine refutes the paradigm of PhoP/PhoQ and PmrA/PmrB in vivo expression as solely intracellularly induced and supports previous data demonstrating peroral virulence attenuation of pmrH mutants [3].

Anatomical context of pagP

Bacteria isolated from spleens of orally inoculated mice showed no further induction of prgH but had the highest expression of pmrH, pagP, and ssaB [3].

References

Transfer of palmitate from phospholipids to lipid A in outer membranes of gram-negative bacteria. Bishop, R.E., Gibbons, H.S., Guina, T., Trent, M.S., Miller, S.I., Raetz, C.R. EMBO J. (2000) [Pubmed]
Regulated covalent modifications of lipid A. Raetz, C.R. J. Endotoxin Res. (2001) [Pubmed]
Resolvase-in vivo expression technology analysis of the Salmonella enterica serovar Typhimurium PhoP and PmrA regulons in BALB/c mice. Merighi, M., Ellermeier, C.D., Slauch, J.M., Gunn, J.S. J. Bacteriol. (2005) [Pubmed]

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