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Carbohydr Res. 2011 Jul 15;346(10):1262-6. doi: 10.1016/j.carres.2011.04.016. Epub 2011 Apr 13.

The role of lic2B in lipopolysaccharide biosynthesis in Haemophilus influenzae strain Eagan.

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Clinical Research Centre, Karolinska Institutet, Novum, S-141 86 Huddinge, Sweden.


Lipopolysaccharide (LPS) biosynthesis in Haemophilus influenzae involves genes from the lic2 locus that are required for chain extension from the middle heptose (HepII) of the conserved triheptosyl inner-core moiety. Lic2C initiates the process by attaching the first glucose to HepII, but the gene encoding for the enzyme adding the next β-D-Glcp- is uncharacterized. Lic2B is the candidate glucosyltransferase; however, in previous investigations, mutation of lic2B resulted in no hexose extension from HepII, likely due to a polar effect on the lic2C gene. In this study we complemented a lic2B knock-out mutant of H. influenzae strain Eagan with a functional lic2C gene and investigated its LPS by mass spectrometry and 2D NMR spectroscopy. Lic2B was found to encode a glucosyltransferase responsible for the linkage of β-D-Glcp-(1→4)-α-D-Glcp-(1→ extending from O-3 of the central heptose of the triheptosyl inner-core moiety, l-α-D-Hepp-(1→2)-[PEtn→6]-l-α-D-Hepp-(1→3)-l-α-D-Hepp-(1→5)-[PPEtn→4]-α-Kdo-(2→6)-lipid A.

[Indexed for MEDLINE]

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