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Papers In Press, published online ahead of print June 23, 2004
J. Biol. Chem, 10.1074/jbc.M401366200
Submitted on February 6, 2004
Revised on June 23, 2004
Accepted on June 23, 2004

Investigation of the structural requirements in the lipopolysaccharide core acceptor for ligation of O antigens in the genus Salmonella: WaaL "ligase" is not the sole determinant of acceptor specificity

Natalia A. Kaniuk, Evgeny Vinogradov, and Chris Whitfield

Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1

Corresponding Author: cwhitfie{at}uoguelph.ca

The ligation of O-antigen polysaccharide to lipid A-core oligosaccharide is a late step in the formation of the complex glycolipid known as lipopolysaccharide. While the process has been localized to the periplasmic face of the inner membrane, details of the ligation mechanism have not been resolved. To date, there is only one gene product (WaaL, often referred to as "ligase") known to be required. There exists a requirement for a specific lipid A-core oligosaccharide acceptor structure for ligation activity and it has been proposed that the WaaL protein imparts this acceptor specificity. Here, the structural requirements in the core oligosaccharide acceptor for O-antigen ligation are investigated in prototype serovars of Salmonella enterica. Complementation experiments in mutants with defined core oligosaccharide structure indicate that the specificity of the ligation reaction for a particular core oligosaccharide structure is not dependent on the WaaL protein alone. The data provide the first indication of a more complicated recognition process involving additional cellular components.


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