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Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin

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Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin. / Deng, Dong Mei; Urch, Jonathan E.; ten Cate, Jacob M.; Rao, Vincenzo A.; van Aalten, Daan M. F.; Crielaard, Wim.

In: Journal of Bacteriology, Vol. 191, No. 1, 01.2009, p. 394-402.

Research output: Contribution to journalArticle

Harvard

Deng, DM, Urch, JE, ten Cate, JM, Rao, VA, van Aalten, DMF & Crielaard, W 2009, 'Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin' Journal of Bacteriology, vol 191, no. 1, pp. 394-402., 10.1128/JB.00838-08

APA

Deng, D. M., Urch, J. E., ten Cate, J. M., Rao, V. A., van Aalten, D. M. F., & Crielaard, W. (2009). Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin. Journal of Bacteriology, 191(1), 394-402. 10.1128/JB.00838-08

Vancouver

Deng DM, Urch JE, ten Cate JM, Rao VA, van Aalten DMF, Crielaard W. Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin. Journal of Bacteriology. 2009 Jan;191(1):394-402. Available from: 10.1128/JB.00838-08

Author

Deng, Dong Mei; Urch, Jonathan E.; ten Cate, Jacob M.; Rao, Vincenzo A.; van Aalten, Daan M. F.; Crielaard, Wim / Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin.

In: Journal of Bacteriology, Vol. 191, No. 1, 01.2009, p. 394-402.

Research output: Contribution to journalArticle

Bibtex - Download

@article{4597caf7ddcf4b27abb893a5d672b763,
title = "Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin",
keywords = "N-acetylglucosamine deacetylase, Biofilm formation, Cryptococcus neoformans, Bacteria binding, Virulence factor, Peptidoglycan, System, Protein, Pathogen, Chitin",
author = "Deng, {Dong Mei} and Urch, {Jonathan E.} and {ten Cate}, {Jacob M.} and Rao, {Vincenzo A.} and {van Aalten}, {Daan M. F.} and Wim Crielaard",
year = "2009",
doi = "10.1128/JB.00838-08",
volume = "191",
number = "1",
pages = "394--402",
journal = "Journal of Bacteriology",
issn = "0021-9193",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Streptococcus mutans SMU.623c codes for a functional, metal-dependent polysaccharide deacetylase that modulates interactions with salivary agglutinin

A1 - Deng,Dong Mei

A1 - Urch,Jonathan E.

A1 - ten Cate,Jacob M.

A1 - Rao,Vincenzo A.

A1 - van Aalten,Daan M. F.

A1 - Crielaard,Wim

AU - Deng,Dong Mei

AU - Urch,Jonathan E.

AU - ten Cate,Jacob M.

AU - Rao,Vincenzo A.

AU - van Aalten,Daan M. F.

AU - Crielaard,Wim

PY - 2009/1

Y1 - 2009/1

N2 - <p>The genome sequence of the oral pathogen Streptococcus mutans predicts the presence of two putative polysaccharide deacetylases. The first, designated PgdA in this paper, shows homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae and Listeria monocytogenes, which are both thought to be involved in the bacterial defense mechanism against human mucosal lysozyme and are part of the CAZY family 4 carbohydrate esterases. S. mutans cells in which the pgdA gene was deleted displayed a different colony texture and a slightly increased cell surface hydrophobicity and yet did not become hypersensitive to lysozyme as shown previously for S. pneumoniae. To understand this apparent lack of activity, the high-resolution X-ray structure of S. mutans PgdA was determined; it showed the typical carbohydrate esterase 4 fold, with metal bound in a His-His-Asp triad. Analysis of the protein surface showed that an extended groove lined with aromatic residues is orientated toward the active-site residues. The protein exhibited metal-dependent de-N-acetylase activity toward a hexamer of N-acetylglucosamine. No activity was observed toward shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. In agreement with the lysozyme data this would suggest that S. mutans PgdA does not act on peptidoglycan but on an as-yet-unidentified polysaccharide within the bacterial cell surface. Strikingly, the pgdA-knockout strain showed a significant increase in aggregation/agglutination by salivary agglutinin, in agreement with this gene acting as a deacetylase of a cell surface glycan.</p>

AB - <p>The genome sequence of the oral pathogen Streptococcus mutans predicts the presence of two putative polysaccharide deacetylases. The first, designated PgdA in this paper, shows homology to the catalytic domains of peptidoglycan deacetylases from Streptococcus pneumoniae and Listeria monocytogenes, which are both thought to be involved in the bacterial defense mechanism against human mucosal lysozyme and are part of the CAZY family 4 carbohydrate esterases. S. mutans cells in which the pgdA gene was deleted displayed a different colony texture and a slightly increased cell surface hydrophobicity and yet did not become hypersensitive to lysozyme as shown previously for S. pneumoniae. To understand this apparent lack of activity, the high-resolution X-ray structure of S. mutans PgdA was determined; it showed the typical carbohydrate esterase 4 fold, with metal bound in a His-His-Asp triad. Analysis of the protein surface showed that an extended groove lined with aromatic residues is orientated toward the active-site residues. The protein exhibited metal-dependent de-N-acetylase activity toward a hexamer of N-acetylglucosamine. No activity was observed toward shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. In agreement with the lysozyme data this would suggest that S. mutans PgdA does not act on peptidoglycan but on an as-yet-unidentified polysaccharide within the bacterial cell surface. Strikingly, the pgdA-knockout strain showed a significant increase in aggregation/agglutination by salivary agglutinin, in agreement with this gene acting as a deacetylase of a cell surface glycan.</p>

KW - N-acetylglucosamine deacetylase

KW - Biofilm formation

KW - Cryptococcus neoformans

KW - Bacteria binding

KW - Virulence factor

KW - Peptidoglycan

KW - System

KW - Protein

KW - Pathogen

KW - Chitin

U2 - 10.1128/JB.00838-08

DO - 10.1128/JB.00838-08

M1 - Article

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 1

VL - 191

SP - 394

EP - 402

ER -

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