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Gene Review:

waaP - LPS biosynthesis rpteon

Escherichia coli O157:H7 str. EDL933

Yethon, J.A. et al., Yethon, J.A. et al., Yethon, J.A. et al.

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Disease relevance of waaP

The purified enzyme catalyzes the incorporation of 33P from [gamma-33P]ATP into acceptor LPS purified from a defined E. coli waaP mutant [1].
In Escherichia coli, Salmonella enterica, and Pseudomonas aeruginosa, the waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region [1].
Only mutation of waaP resulted in hypersensitivity to novobiocin and sodium dodecyl sulfate, a characteristic of deep-rough mutations [2].

High impact information on waaP

The waaY, waaQ, and waaP genes are located in the central operon of the waa (formerly rfa) locus on the chromosome of Escherichia coli [2].
Mutation of waaP resulted in loss of phosphoryl substituents on HepI and obviated WaaQ and WaaY activity [2].
Salmonella enterica serovar typhimurium waaP mutants show increased susceptibility to polymyxin and loss of virulence In vivo [3].

Biological context of waaP

In this study, the waaY, waaQ, and waaP genes were independently mutated by insertion of a non-polar antibiotic resistance cassette, and the structures of the resulting mutant core oligosaccharides were determined by chemical analyses and phosphorus-nuclear magnetic resonance spectroscopy [2].

Associations of waaP with chemical compounds

The waaP mutant was significantly more sensitive to polymyxin in both wild-type and polymyxin-resistant backgrounds, despite the decreased negative charge of the mutant LPSs [3].

References

Purification and characterization of WaaP from Escherichia coli, a lipopolysaccharide kinase essential for outer membrane stability. Yethon, J.A., Whitfield, C. J. Biol. Chem. (2001) [Pubmed]
Involvement of waaY, waaQ, and waaP in the modification of Escherichia coli lipopolysaccharide and their role in the formation of a stable outer membrane. Yethon, J.A., Heinrichs, D.E., Monteiro, M.A., Perry, M.B., Whitfield, C. J. Biol. Chem. (1998) [Pubmed]
Salmonella enterica serovar typhimurium waaP mutants show increased susceptibility to polymyxin and loss of virulence In vivo. Yethon, J.A., Gunn, J.S., Ernst, R.K., Miller, S.I., Laroche, L., Malo, D., Whitfield, C. Infect. Immun. (2000) [Pubmed]

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