| DOI | Resolve DOI: https://doi.org/10.1093/glycob/cws100 |
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| Author | Search for: Ronholm, Jennifer; Search for: Wang, Linru; Search for: Hayashi, Ikue; Search for: Sugai, Motoyuki; Search for: Zhang, Zhiyi1; Search for: Cao, Xudong; Search for: Lin, Min |
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| Affiliation | - National Research Council of Canada. Information and Communication Technologies
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| Format | Text, Article |
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| Subject | N-acetylglucosaminidase; N-acetylation; IspC; peptidoglycan; Listeria monocytogenes |
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| Abstract | IspC 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. |
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| Publication date | 2012-06-21 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 21270075 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 337d9c05-fff0-4b73-bdc8-51910d53d64c |
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| Record created | 2013-12-19 |
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| Record modified | 2020-04-21 |
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