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Papers In Press, published online ahead of print April 25, 2000
Laboratory of Microbiology, The Rockefeller University, New York, NY 10021
Corresponding Author: tomasz{at}rockvax.rockefeller.edu
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 - were 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 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.
J. Biol. Chem, 10.1074/jbc.M910189199
Submitted on December 20, 1999
Revised on March 7, 2000
Accepted on April 25, 2000
The pgdA gene encodes for a peptidoglycan GlcNAc deacetylase in streptococcus pneumoniae
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