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J. Biol. Chem., Vol. 275, Issue 27, 20496-20501, July 7, 2000
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From The Rockefeller University, Laboratory of Microbiology,
New York, New York 10021
Analytical work on the fractionation of the
glycan strands of Streptococcus pneumoniae cell wall has
led to the observation that an unusually high proportion of hexosamine
units (over 80% of the glucosamine and 10% of the muramic acid
residues) was not N-acetylated, explaining the resistance
of the peptidoglycan to the hydrolytic action of lysozyme, a muramidase
that cleaves in the glycan backbone. A gene, pgdA, was
identified as encoding for the peptidoglycan
N-acetylglucosamine deacetylase
A with amino acid sequence similarity to fungal chitin
deacetylases and rhizobial NodB chitooligosaccharide deacetylases.
Pneumococci in which pgdA was inactivated by insertion
duplication mutagenesis produced fully N-acetylated glycan
and became hypersensitive to exogenous lysozyme in the stationary phase
of growth. The pgdA gene may contribute to pneumococcal
virulence by providing protection against host lysozyme, which is known
to accumulate in high concentrations at infection sites.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ251472.
The pgdA Gene Encodes for a Peptidoglycan
N-Acetylglucosamine Deacetylase in Streptococcus
pneumoniae*
*
Partial support for this study was provided by National
Institutes of Health Grant AI37275 and by the Irene Diamond Foundation. Sequencing of S. pneumoniae was accomplished with support
from The Institute for Genomic Research, the National Institute of Allergy and Infectious Diseases, and the Merck Genome Research Institute.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.
To whom correspondence should be addressed. Tel.: 212-327-8278;
Fax: 212-327-8688; E-mail: tomasz@rockvax.rockefeller.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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