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Journal of Bacteriology, May 2005, p. 2939-2947, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.2939-2947.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of a Cluster of Three Glycosyltransferase Enzymes Essential for Moraxella catarrhalis Lipooligosaccharide Assembly

Katie J. Edwards,1,2 Simon Allen,3 Bradford W. Gibson,3,4 and Anthony A. Campagnari1,2,5*

Department of Microbiology and Immunology,1 Witebsky Center for Microbial Pathogenesis and Immunology,2 the Department of Medicine, State University of New York at Buffalo, Buffalo, New York 14214,5 The Buck Institute for Age Research, Novato, California 94945,3 the Department of Pharmaceutical Chemistry, University of California, San Francisco, California 941434

Received 25 October 2004/ Accepted 14 January 2005

Moraxella catarrhalis isolates express lipooligosaccharide (LOS) molecules on their surface, which share epitopes similar to that of the Neisseria and Haemophilus species. These common LOS epitopes have been implicated in various steps of pathogenesis for the different organisms. In this study, a cluster of three LOS glycosyltransferase genes (lgt) were identified in M. catarrhalis 7169, a strain that produces a serotype B LOS. Mutants in these glycosyltransferase genes were constructed, and the resulting LOS phenotypes were consistent with varying degrees of truncation compared to wild-type LOS. The LOS structures of each lgt mutant were no longer detected by a monoclonal antibody (MAb 4G5) specific to a highly conserved terminal epitope nor by a monoclonal antibody (MAb 3F7) specific to the serotype B LOS side chain. Mass spectrometry of the LOS glycoforms assembled by two of these lgt mutants indicated that lgt1 encodes an {alpha}(1-2) glucosyltransferase and the lgt2 encodes a ß(1-4) galactosyltransferase. However, these structural studies could not delineate the function for lgt3. Therefore, M. catarrhalis lgt3 was introduced into a defined ß(1-4) glucosyltransferase Haemophilus ducreyi 35000glu– mutant in trans, and monoclonal antibody analysis confirmed that Lgt3 complemented the LOS defect. These data suggest that lgt3 encodes a glucosyltransferase involved in the addition of a ß(1-4)-linked glucose to the inner core. Furthermore, we conclude that this enzymatic step is essential for the assembly of the complete LOS glycoform expressed by M. catarrhalis 7169.

* Corresponding author. Mailing address: Department of Microbiology, University at Buffalo, Biomedical Research Bldg. Rm. 143, 3435 Main St., Buffalo, NY 14214. Phone: (716) 829-2673. Fax: (716) 829-3889. E-mail: aac{at}buffalo.edu.

Journal of Bacteriology, May 2005, p. 2939-2947, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.2939-2947.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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