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J. Biol. Chem., Vol. 280, Issue 27, 25936-25947, July 8, 2005

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Molecular and Functional Characterization of O Antigen Transfer in Vibrio cholerae^*

Stefan Schild, Anna-Karina Lamprecht, and Joachim Reidl

From the Institut für Hygiene und Mikrobiologie, Universität Würzburg, Josef Schneider Strasse 2, E1, Würzburg 97080, Germany

The majority of Gram-negative bacteria transfer O antigen polysaccharides onto the lipid A-core oligosaccharide via the action of surface polymer:lipid A-core ligases (WaaL). Here, we characterize the WaaL proteins of Vibrio cholerae with emphasis on structural and functional characterization of O antigen transfer and core oligosaccharide recognition. We demonstrate that the activity of two distantly related O antigen ligases is dependent on the presence of N-acetylglucosamine, and substitution of an additional sugar, i.e. galactose, alters the site specificity of the core oligosaccharide necessitating discriminative WaaL types. Protein topology analysis and a conserved domain search identified two distinct conserved motifs in the periplasmic domains of WaaL proteins. Site-directed mutagenesis of the two motifs, shown for WaaLs of V. cholerae and Salmonella enterica, caused a loss of O antigen transfer activity. Moreover, analogy of topology and motifs between WaaLs and O polysaccharide polymerases (Wzy) reveals a relationship between the two protein families, suggesting that the catalyzed reactions are related to each other.

Received for publication, February 3, 2005 , and in revised form, May 19, 2005.

^* This work was funded by Deutsche Forschungsgemeinschaft Grant DFG1561/2-1 (to J. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains a supplemental figure.

To whom correspondence should be addressed. Tel.: 49-0-931-201-46159; Fax: 49-0-931-201-46445; E-mail: joachim.reidl{at}mail.uni-wuerzburg.de.

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