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Journal of Bacteriology, October 2004, p. 6970-6982, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6970-6982.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

lpt6, a Gene Required for Addition of Phosphoethanolamine to Inner-Core Lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzae

J. Claire Wright,1* Derek W. Hood,1 Gaynor A. Randle,1 Katherine Makepeace,1 Andrew D. Cox,2 Jianjun Li,2 Ronald Chalmers,3 James C. Richards,2 and E. Richard Moxon1

Molecular Infectious Diseases Group, Department of Paediatrics, Weatherall Institute for Molecular Medicine, John Radcliffe Hospital,1 Department of Biochemistry, University of Oxford, Oxford, United Kingdom,3 Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada2

Received 31 March 2004/ Accepted 14 July 2004

We previously described a gene, lpt3, required for the addition of phosphoethanolamine (PEtn) at the 3 position on the ß-chain heptose (HepII) of the inner-core Neisseria meningitidis lipopolysaccharide (LPS), but it has long been recognized that the inner-core LPS of some strains possesses PEtn at the 6 position (PEtn-6) on HepII. We have now identified a gene, lpt6 (NMA0408), that is required for the addition of PEtn-6 on HepII. The lpt6 gene is located in a region previously identified as Lgt-3 and is associated with other LPS biosynthetic genes. We screened 113 strains, representing all serogroups and including disease and carriage strains, for the lpt3 and lpt6 genes and showed that 36% contained both genes, while 50% possessed lpt3 only and 12% possessed lpt6 only. The translated amino acid sequence of lpt6 has a homologue (72.5% similarity) in a product of the Haemophilus influenzae Rd genome sequence. Previous structural studies have shown that all H. influenzae strains investigated have PEtn-6 on HepII. Consistent with this, we found that, among 70 strains representing all capsular serotypes and nonencapsulated H. influenzae strains, the lpt6 homologue was invariably present. Structural analysis of LPS from H. influenzae and N. meningitidis strains where lpt6 had been insertionally inactivated revealed that PEtn-6 on HepII could not be detected. The translated amino acid sequences from the N. meningitidis and H. influenzae lpt6 genes have conserved residues across their lengths and are part of a family of proven or putative PEtn transferases present in a wide range of gram-negative bacteria.

* Corresponding author. Mailing address: Molecular Infectious Diseases Group, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom. Phone: 44 1865 222347. Fax: 44 1865 222626. E-mail: claire.wright{at}paediatrics.ox.ac.uk.

Journal of Bacteriology, October 2004, p. 6970-6982, Vol. 186, No. 20
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.20.6970-6982.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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