Identification and molecular characterization of an <i>N</i>‐acetylmuramyl‐<scp>l</scp>‐alanine amidase Sle1 involved in cell separation of <i>Staphylococcus aureus</i>

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Published
2005-10-14
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  • http://onlinelibrary.wiley.com/termsAndConditions#vor
DOI
  • 10.1111/j.1365-2958.2005.04881.x
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Wiley

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<jats:title>Summary</jats:title><jats:p>We purified a peptidoglycan hydrolase involved in cell separation from a <jats:italic>Staphylococcus aureus atl</jats:italic> null mutant and identified its gene. Characterization of the gene product shows a 32 kDa <jats:italic>N</jats:italic>‐acetylmuramyl‐<jats:sc>l</jats:sc>‐alanine amidase that we designated Sle1. Analysis of peptidoglycan digests showed Sle1 preferentially cleaved <jats:italic>N</jats:italic>‐acetylmuramyl‐<jats:sc>l</jats:sc>‐Ala bonds in dimeric cross‐bridges that interlink the two murein strands in the peptidoglycan. An insertion mutation of <jats:italic>sle1</jats:italic> impaired cell separation and induced <jats:italic>S. aureus</jats:italic> to form clusters suggesting Sle1 is involved in cell separation of <jats:italic>S. aureus</jats:italic>. The Sle1 mutant revealed a significant decrease in pathogenesis using an acute infection mouse model. Atl is the major autolysin of <jats:italic>S. aureus</jats:italic>, which has been implicated in cell separation of <jats:italic>S. aureus</jats:italic>. Generation of an <jats:italic>atl</jats:italic>/<jats:italic>sle1</jats:italic> double mutant revealed that the mutant cell separation was heavily impaired suggesting that <jats:italic>S. aureus</jats:italic> uses two peptidoglycan hydrolases, Atl and Sle1, for cell separation. Unlike Atl, Sle1 is not directly involved in autolysis of <jats:italic>S. aureus</jats:italic>.</jats:p>

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