The Listeria monocytogenes serotype 4b autolysin IspC has N-acetylglucosaminidase activity

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DOIResolve DOI: http://doi.org/10.1093/glycob/cws100
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TypeArticle
Journal titleGlycobiology
ISSN0959-6658
Volume22
Issue10
Pages13111320; # of pages: 10
SubjectN-acetylglucosaminidase; N-acetylation; IspC; peptidoglycan; Listeria monocytogenes
AbstractIspC is a novel peptidoglycan (PG) hydrolase that is conserved in Listeria monocytogenes serotype 4b strains and is involved in virulence. The aim of this study was to establish the hydrolytic bond specificity of IspC. Purified L. monocytogenes peptidoglycan was digested by recombinant IspC and the resulting muropeptides were separated by reverse phase high-performance liquid chromatography. The structure of each muropeptide was determined using matrix-assisted laser desorption ionization (MALDI)-time-of-flight mass spectrometry in combination with MALDI-post-source decay mass spectrometry. The structure of muropeptides resulting from IspC-mediated hydrolysis indicated that IspC has N-acetylglucosaminidase activity. These muropeptides also had a high proportion of N-acetylated glucosamine residues. To determine whether IspC is more effective at hydrolysing N-acetylated peptidoglycan than de-N-acetylated peptidoglycan, a peptidoglycan deacetylase (PgdA) in-frame deletion mutant was created. This mutant was shown to have fully N-acetylated peptidoglycan and was more susceptible to hydrolysis by IspC when compared with the partially de-N-acetylated wild-type peptidoglycan. This indicates that IspC is more efficient when hydrolysing a fully N-acetylated peptidoglycan substrate. The finding that IspC acts as an N-acetylglucosaminidase is consistent with its categorization, based on amino acid sequence, as a member of the GH73 family. As with other members of this family, de-N-acetylation seems to be an important mechanism for regulating the activity of IspC. © 2012 The Author.
Publication date
PublisherOxford University Press
LanguageEnglish
AffiliationInformation and Communication Technologies; National Research Council Canada
Peer reviewedYes
NPARC number21270075
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Record identifier337d9c05-fff0-4b73-bdc8-51910d53d64c
Record created2013-12-19
Record modified2016-05-09
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