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Glycobiology Advance Access published online on December 1, 2004
Glycobiology, doi:10.1093/glycob/cwi018
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Received October 5, 2004
Revised November 25, 2004
Accepted November 28, 2004

Article

Inner core assembly and structure of the lipooligosaccharide of Neisseria meningitidis: capacity of strain NMB to express all known immunotype epitopes

Charlene M. Kahler 1*, Anup Datta 2, Yih-ling Tzeng 3, Russell Carlson 2, and David Stephens 3

1 Department of Microbiology, Monash University, Australia,
2 Complex Carbohydrate Research Center, University of Georgia, Athens, GA,
3 Departments of Medicine and Microbiology and Immunology and Laboratories of Microbial Pathogenesis, Emory University School of Medicine and VA Medical Center, Atlanta, GA

* To whom correspondence should be addressed.
Charlene M. Kahler, E-mail: Charlene.Kahler{at}med.monash.edu.au


  Abstract

Neisseria meningitidis expresses a heterogeneous population of lipooligosaccharide 3 (LOS) inner cores variously substituted with {alpha}1-3 linked glucose and O-3, O-6, and O-7 linked phosphoethanolamine (PEA), as well as glycine, attached to HepII. Combinations of these attachments to the LOS inner core represent immunodominant epitopes that are being exploited as future vaccine candidates. Historically, each LOS immunotype was structurally assessed and prescribed a certain unique inner core epitope. We report that a single isolate, strain NMB, possesses the capacity to produce all of the known neisserial LOS inner core immunotype structures. Analysis of the inner cores from parental LOS revealed the presence or absence of {alpha}1,3 linked glucose, O-6 and/or O-7 linked PEA, in addition to glycine attached at the 7 position of the HepII inner core. Identification and inactivation of lpt-6 in strain NMB resulted in the loss of both O-6 and O-7 linked PEA groups from the LOS inner core, suggesting that Lpt-6 of strain NMB may have bifunctional transferase activities or that the O-6 linked PEA groups once attached to the inner core undergo non-enzymatic transfer to the O-7 position of HepII. Although O-3 linked PEA was not detected in parental LOS inner cores devoid of {alpha}1-3 linked glucose residues, LOS glycoforms bearing O-3 PEA groups accumulated in a truncated mutant, NMBlgtK (Hep2Kdo2-lipidA). Since these structures disappeared upon inactivation of the lpt-3 locus, strain NMB expresses a functional O-3 PEA transferase. The LOS glycoforms expressed by NMBlgtK were also devoid of glycine attachments, indicating that glycine was added to the inner core after the completion of the {gamma}-chain by LgtK. In conclusion, strain NMB has the capability to express all known inner core structures, but in in vitro culture L2 and L4 immunotype structures are predominantly expressed.

Keywords: Neisseria meningitidis, lipooligosaccharide, heptose PEA transferase, phosphoethanolamine, immunotype.
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