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Glycobiology, 2001, Vol. 11, No. 11 957-967
© 2001 Oxford University Press

Genetic basis for expression of the major globotetraose-containing lipopolysaccharide from H. influenzae strain Rd (RM118)

Derek W. Hood1,2, Andrew D. Cox3, Warren W. Wakarchuk3, Melissa Schur3, Elke K.H. Schweda4, Shannon L. Walsh2, Mary E. Deadman2, Adele Martin3, E. Richard Moxon2 and James C. Richards3

2Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DS, UK; 3Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, K1A 0R6 Canada; and 4Clinical Research Centre, Karolinska Institutet and University College of South Stockholm, NOVUM, S-141 86 Huddinge, Sweden.

A genetic basis for the biosynthetic assembly of the globotetraose containing lipopolysaccharide (LPS) of Haemophilus influenzae strain RM118 (Rd) was determined by structural analysis of LPS derived from mutant strains. We have previously shown that the parent strain RM118 elaborates a population of LPS molecules made up of a series of related glycoforms differing in the degree of oligosaccharide chain extension from the distal heptose residue of a conserved phosphorylated inner-core element, L-{alpha}-D-Hepp-(1->2)-L-{alpha}-D-Hepp-(1->3)-[ß-D-Glcp-(1->4)-]-L-{alpha}-D-Hepp-(1->5)-{alpha}-Kdo. The fully extended LPS glycoform expresses the globotetraose structure, ß-D-GalpNAc-(1->3)-{alpha}-D-Galp-(1->4)-ß-D-Galp-(1->4)-ß-D-Glcp. A fingerprinting strategy was employed to establish the structure of LPS from strains mutated in putative glycosyltransferase genes compared to the parent strain. This involved glycose and linkage analysis on intact LPS samples and analysis of O-deacylated LPS samples by electrospray ionization mass spectrometry and 1D 1H-nuclear magnetic resonance spectroscopy. Four genes, lpsA, lic2A, lgtC, and lgtD, were required for sequential addition of the glycoses to the terminal inner-core heptose to give the globotetraose structure. lgtC and lgtD were shown to encode glycosyltransferases by enzymatic assays with synthetic acceptor molecules. This is the first genetic blueprint determined for H. influenzae LPS oligosaccharide biosynthesis, identifying genes involved in the addition of each glycose residue.

1 To whom correspondence should be addressed


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