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Infection and Immunity, June 2005, p. 3512-3520, Vol. 73, No. 6
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.6.3512-3520.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Identification and Characterization of an Autolysin-Encoding Gene of Streptococcus mutans

Yukie Shibata,1 Miki Kawada,1 Yoshio Nakano,1 Kuniaki Toyoshima,2 and Yoshihisa Yamashita1*

Department of Preventive Dentistry, Kyushu University Faculty of Dental Science, Fukuoka 812-8582,1 Department of Oral Anatomy and Neurobiology, Kyushu Dental College, Kitakyushu 803-8580, Japan2

Received 24 December 2004/ Returned for modification 17 January 2005/ Accepted 2 February 2005

We identified a gene (atlA) encoding autolytic activity from Streptococcus mutans Xc. The AtlA protein predicted to be encoded by atlA is composed of 979 amino acids with a molecular weight of 107,279 and has a conserved ß-1,4-N-acetylmuramidase (lysozyme) domain in the C-terminal portion. Sodium dodecyl sulfate extracts of strain Xc showed two major bacteriolytic bands with molecular masses of 107 and 79 kDa, both of which were absent from a mutant with inactivated atlA. Western blot analysis revealed that the 79-kDa band was derived from the 107-kDa peptide by cleavage of its N-terminal portion. The inactivation of atlA resulted in a marked decrease in autolysis and the formation of very long chains of cells compared to the case for the parent strain. Although both the parent and mutant strains formed biofilms in the presence of sucrose, the biofilms formed by the mutant had a sponge-like architecture with large gaps and contained 30% less biomass than those formed by the parent strain. Furthermore, strain Xc formed glucose-dependent, loose biofilms in the absence of sucrose, but the mutant lost this ability. These results suggest that AtlA may play an important role in biofilm formation by S. mutans. The antibody produced against the C-terminal peptide containing the ß-1,4-N-acetylmuramidase domain drastically inhibited the autolytic activity of strain Xc. This inhibition was specific among the oral streptococci to S. mutans. These results indicate that the catalytic domain of AtlA is located at the C terminus, suggesting that further characterization of this domain may provide a means to control cariogenic dental plaque formation.

* Corresponding author. Mailing address: Department of Preventive Dentistry, Kyushu University Faculty of Dental Science, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. Phone: 81-92-642-6350. Fax: 81-92-642-6354. E-mail: yoshi{at}dent.kyushu-u.ac.jp.

Editor: J. T. Barbieri

Infection and Immunity, June 2005, p. 3512-3520, Vol. 73, No. 6
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.6.3512-3520.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ahn, S.-J., Burne, R. A. (2007). Effects of Oxygen on Biofilm Formation and the AtlA Autolysin of Streptococcus mutans. J. Bacteriol. 189: 6293-6302 [Abstract] [Full Text]  
  • Rice, K. C., Mann, E. E., Endres, J. L., Weiss, E. C., Cassat, J. E., Smeltzer, M. S., Bayles, K. W. (2007). The cidA murein hydrolase regulator contributes to DNA release and biofilm development in Staphylococcus aureus. Proc. Natl. Acad. Sci. USA 104: 8113-8118 [Abstract] [Full Text]  
  • Ahn, S.-J., Burne, R. A. (2006). The atlA Operon of Streptococcus mutans: Role in Autolysin Maturation and Cell Surface Biogenesis.. J. Bacteriol. 188: 6877-6888 [Abstract] [Full Text]  
  • Catt, D. M., Gregory, R. L. (2005). Streptococcus mutans Murein Hydrolase. J. Bacteriol. 187: 7863-7865 [Abstract] [Full Text]  


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