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J. Biol. Chem., Vol. 276, Issue 1, 139-146, January 5, 2001
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From the Several species of streptococci produce
extracellular polysaccharides in the form of secreted
exopolysaccharides or cell-associated capsules. Although the biological
properties and repeating unit structures of these polysaccharides are
diverse, sequence analysis of the genes required for their production
has revealed a surprising degree of conservation among five genes found
in the capsule gene cluster of each of several polysaccharide-producing
streptococci. To determine the function of these conserved genes, we
characterized a series of isogenic mutants derived from a wild-type
strain of type Ia group B Streptococcus by selectively
inactivating each gene. Inactivation of cpsIaE resulted in
an acapsular phenotype, consistent with previous work that identified
the cpsIaE product as the glycosyltransferase that
initiates synthesis of the polysaccharide repeating unit. Mutants in
cpsIaA, cpsIaB, cpsIaC, or
cpsIaD produced type Ia capsular polysaccharide, but in
reduced amounts compared with the wild type. Analysis of the mutant
polysaccharides and of capsule gene transcription in the mutant strains
provided evidence that cpsIaA encodes a transcriptional
activator that regulates expression of the capsule gene operon. Mutants
in cpsIaC or cpsIaD produced polysaccharide of
reduced molecular size but with an identical repeating unit structure
as the wild-type strain. We conclude that CpsA to -D are not required
for polysaccharide repeating unit biosynthesis but rather that they
direct the coordinated polymerization and export of high molecular
weight polysaccharide.
Functional Analysis in Type Ia Group B Streptococcus
of a Cluster of Genes Involved in Extracellular Polysaccharide
Production by Diverse Species of Streptococci*
§,¶,, and
**
Channing Laboratory and Division of
Infectious Diseases, Brigham and Women's Hospital, and
¶ Department of Microbiology and Molecular Genetics, Harvard
Medical School, Boston, Massachusetts 02115
*
This work was supported in part by NIAID, National
Institutes of Health (NIH), Grant AI42940.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 © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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