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Journal of Bacteriology, October 2006, p. 7211-7221, Vol. 188, No. 20
0021-9193/06/$08.00+0     doi:10.1128/JB.00724-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

AmiC Functions as an N-Acetylmuramyl-L-Alanine Amidase Necessary for Cell Separation and Can Promote Autolysis in Neisseria gonorrhoeae

Daniel L. Garcia and Joseph P. Dillard^*

Department of Medical Microbiology and Immunology, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706

Received 19 May 2006/ Accepted 27 July 2006

Neisseria gonorrhoeae is prone to undergo autolysis under many conditions not conducive to growth. The role of autolysis during gonococcal infection is not known, but possible advantages for the bacterial population include provision of nutrients to a starving population, modulation of the host immune response by released cell components, and donation of DNA for natural transformation. Biochemical studies indicated that an N-acetylmuramyl-L-alanine amidase is responsible for cell wall breakdown during autolysis. In order to better understand autolysis and in hopes of creating a nonautolytic mutant, we mutated amiC, the gene for a putative peptidoglycan-degrading amidase in N. gonorrhoeae. Characterization of peptidoglycan fragments released during growth showed that an amiC mutant did not produce free disaccharide, consistent with a role for AmiC as an N-acetylmuramyl-L-alanine amidase. Compared to the wild-type parent, the mutant exhibited altered growth characteristics, including slowed exponential-phase growth, increased turbidity in stationary phase, and increased colony opacity. Thin-section electron micrographs showed that mutant cells did not fully separate but grew as clumps. Complementation of the amiC deletion mutant with wild-type amiC restored wild-type growth characteristics and transparent colony morphology. Overexpression of amiC resulted in increased cell lysis, supporting AmiC's purported function as a gonococcal autolysin. However, amiC mutants still underwent autolysis in stationary phase, indicating that other gonococcal enzymes are also involved in this process.

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* Corresponding author. Mailing address: 1300 University Avenue, 471A MSC, Madison, WI 53706. Phone: (608) 265-2837. Fax: (608) 262-8418. E-mail: jpdillard{at}wisc.edu.

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Journal of Bacteriology, October 2006, p. 7211-7221, Vol. 188, No. 20
0021-9193/06/$08.00+0     doi:10.1128/JB.00724-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

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