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J Biol Chem, Vol. 275, Issue 11, 7497-7504, March 17, 2000
From the The capsular polysaccharide of group B
Streptococcus is a key virulence factor and an important
target for protective immune responses. Until now, the nature of the
attachment between the capsular polysaccharide and the bacterial cell
has been poorly defined. We isolated insoluble cell wall fragments from
lysates of type III group B Streptococcus and showed that
the complexes contained both capsular polysaccharide and group B
carbohydrate covalently bound to peptidoglycan. Treatment with the
endo-N-acetylmuramidase mutanolysin released soluble
complexes of capsular polysaccharide linked to group B carbohydrate by
peptidoglycan fragments. Capsular polysaccharide could be enzymatically
cleaved from group B carbohydrate by treatment of the soluble complexes
with
Characterization of the Linkage between the Type III Capsular
Polysaccharide and the Bacterial Cell Wall of Group B
Streptococcus*
§,,
**
Channing Laboratory and Division of
Infectious Diseases, Brigham and Women's Hospital, Harvard Medical
School, Boston, Massachusetts 02115 and the ¶ Department of
Biochemistry, University of Minnesota, St. Paul, Minnesota 55108
-N-acetylglucosaminidase, which catalyzes
hydrolysis of the
-D-GlcNAc(1
4)-D-MurNAc subunit produced by mutanolysin digestion of peptidoglycan. Evidence from gas
chromatography/mass spectrometry and 31P NMR analysis of
the separated polysaccharides supports a model of the group B
Streptococcus cell surface in which the group B carbohydrate and the capsular polysaccharide are independently linked
to the glycan backbone of cell wall peptidoglycan; group B carbohydrate
is linked to N-acetylmuramic acid, and capsular polysaccharide is linked via a phosphodiester bond and an
oligosaccharide linker to N-acetylglucosamine.
*
This work was supported by NIAID, National Institutes of
Health, Public Health Service Grants AI28040 and AI42940 and Contract AI25152.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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