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(Received for publication, April 4, 1996, and in revised form, May 21, 1996)
From the The biosynthetic function of the
lgtABE genetic locus of Neisseria meningitidis
was determined by structural analysis of lipopolysaccharide (LPS)
derived from mutant strains and enzymic assay for glycosyltransferase
activity. LPS was obtained from mutants generated by insertion of
antibiotic resistance cassets in each of the three genes
lgtA, lgtB, lgtE of the N. meningitidis immunotype L3 strain
Volume 271, Number 32,
Issue of August 9, 1996
pp. 19166-19173
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Institute for Biological Sciences, National
Research Council of Canada, Ottawa, Ontario, K1A 0R6, Canada and the
§ Molecular Infectious Diseases Group and Department of
Paediatrics, Institute for Molecular Medicine, John Radcliffe Hospital,
Headington, Oxford, OX3 3DU, United Kingdom
3 MC58. LPS from the parent
strain expresses the terminal lacto-N-neotetraose
structure, Gal
1
4GlcNAc13Gal14Glc. Mild
hydrazine treatment of the LPS afforded O-deacylated
samples that were analyzed directly by electrospray ionization mass
spectrometry (ESI-MS) in the negative ion mode. In conjunction with
results from sugar analysis, ESI-MS revealed successive loss of the
sugars Gal, GlcNAc, and Gal in lgt B, lgt A,
and lgt E LPS, respectively. The structure of a sample of
O- and N-deacylated LPS derived by aqueous KOH
treatment of lgt B LPS was determined in detail by
two-dimensional homo- and heteronuclear NMR methods. Using a synthetic
-GlcNAc acceptor and a -lactose acceptor, the glycosyltransferase
activities encoded by the lgtB and lgtA genes
were unambiguously established. These data provide the first definitive
evidence that the three genes encode the respective
glycosyltransferases required for biosynthesis of the terminal
trisaccharide moiety of the lacto-N-neotetraose structure
in Neisseria LPS. From ESI-MS data, it was also determined
that the Gal-deficient LPS expressed by the lgt E mutant is
identical to that of the major component expressed by immunotype L3
galE-deficient strains. The galE gene which
encodes for UDP-glucose-4-epimerase plays an essential role in the
incorporation of Gal into meningococcal LPS.
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