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Infection and Immunity, October 1999, p. 5417-5426, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Conservation and Accessibility of an Inner Core Lipopolysaccharide Epitope of Neisseria meningitidis

Joyce S. Plested,1,2,* Katherine Makepeace,1 Michael P. Jennings,3 Margaret Anne J. Gidney,4 Suzanne Lacelle,4 J.-R. Brisson,4 Andrew D. Cox,4 Adele Martin,4 A. Graham Bird,2 Christoph M. Tang,1 Fiona M. Mackinnon,1 James C. Richards,4 and E. Richard Moxon1

Molecular Infectious Disease Group, Oxford University Department of Paediatrics, John Radcliffe Hospital, Oxford OX3 9DU,1 and Department of Clinical Immunology, Churchill Hospital, Headington, Oxford OX3 7LJ,2 United Kingdom; Department of Microbiology, University of Queensland, St. Lucia, Brisbane, QLD 4072, Australia3; and the Institute for Biological Sciences, National Research Council, Ottawa, Canada K1A OR64

Received 29 March 1999/Returned for modification 17 May 1999/Accepted 23 June 1999

We investigated the conservation and antibody accessibility of inner core epitopes of Neisseria meningitidis lipopolysaccharide (LPS) because of their potential as vaccine candidates. An immunoglobulin G3 murine monoclonal antibody (MAb), designated MAb B5, was obtained by immunizing mice with a galE mutant of N. meningitidis H44/76 (B.15.P1.7,16 immunotype L3). We have shown that MAb B5 can bind to the core LPS of wild-type encapsulated MC58 (B.15.P1.7,16 immunotype L3) organisms in vitro and ex vivo. An inner core structure recognized by MAb B5 is conserved and accessible in 26 of 34 (76%) of group B and 78 of 112 (70%) of groups A, C, W, X, Y, and Z strains. N. meningitidis strains which possess this epitope are immunotypes in which phosphoethanolamine (PEtn) is linked to the 3-position of the beta -chain heptose (HepII) of the inner core. In contrast, N. meningitidis strains lacking reactivity with MAb B5 have an alternative core structure in which PEtn is linked to an exocyclic position (i.e., position 6 or 7) of HepII (immunotypes L2, L4, and L6) or is absent (immunotype L5). We conclude that MAb B5 defines one or more of the major inner core glycoforms of N. meningitidis LPS. These findings support the possibility that immunogens capable of eliciting functional antibodies specific to inner core structures could be the basis of a vaccine against invasive infections caused by N. meningitidis.

* Corresponding author. Mailing address: Department of Clinical Immunology, Churchill Hospital, Oxford OX3 7LJ, United Kingdom. Phone: (01865)-226002. Fax: (01865)-225990. E-mail: Joyce.Plested{at}paediatrics.ox.ac.uk.

Infection and Immunity, October 1999, p. 5417-5426, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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