Infection and Immunity, December 2000, p. 6656-6662, Vol. 68, No. 12
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Enteric Diseases Department, Naval Medical Research Center, Silver Spring, Maryland 20910,1 and Department of Microbiology, National University of Ireland, Galway, Ireland2
Received 7 June 2000/Returned for modification 9 August 2000/Accepted 7 September 2000
Three genes involved in biosynthesis of the lipooligosaccharide
(LOS) core of Campylobacter jejuni MSC57360, the type
strain of the HS:1 serotype, whose structure mimics GM2
ganglioside, have been cloned and characterized. Mutation of genes
encoding proteins with homology to a sialyl transferase
(cstII) and a putative N-acetylmannosamine
synthetase (neuC1), part of the biosynthetic pathway of
N-acetylneuraminic acid (NeuNAc), have identical
phenotypes. The LOS cores of these mutants display identical changes in
electrophoretic mobility, loss of reactivity with cholera toxin (CT),
and enhanced immunoreactivity with a hyperimmune polyclonal antiserum
generated against whole cells of C. jejuni MSC57360. Loss
of sialic acid in the core of the neuC1 mutant was
confirmed by fast atom bombardment mass spectrometry. Mutation of a
gene encoding a putative
-1,4-N-acetylgalactosaminyltransferase (Cgt) resulted in
LOS cores intermediate in electrophoretic mobility between that of wild
type and the mutants lacking NeuNAc, loss of reactivity with CT, and a
reduced immunoreactivity with hyperimmune antiserum. Chemical analyses
confirmed the loss of N-acetylgalactosamine (GalNAc) and
the presence of NeuNAc in the cgt mutant. These data suggest that the Cgt enzyme is capable of transferring GalNAc to an
acceptor with or without NeuNAc and that the Cst enzyme is capable of
transferring NeuNAc to an acceptor with or without GalNAc. A mutant
with a nonsialylated LOS core is more sensitive to the bactericidal
effects of human sera than the wild type or the mutant lacking GalNAc.
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