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Applied and Environmental Microbiology, November 2007, p. 7150-7154, Vol. 73, No. 22
0099-2240/07/$08.00+0     doi:10.1128/AEM.01783-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

LambdaSa1 and LambdaSa2 Prophage Lysins of Streptococcus agalactiae{triangledown}

David G. Pritchard,1* Shengli Dong,1 Marion C. Kirk,2 Robert T. Cartee,3 and John R. Baker1

Department of Biochemistry and Molecular Genetics,1 Comprehensive Cancer Center,2 Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama3

Received 1 August 2007/ Accepted 15 September 2007

Putative N-acetylmuramyl-L-alanine amidase genes from LambdaSa1 and LambdaSa2 prophages of Streptococcus agalactiae were cloned and expressed in Escherichia coli. The purified enzymes lysed the cell walls of Streptococcus agalactiae, Streptococcus pneumoniae, and Staphylococcus aureus. The peptidoglycan digestion products in the cell wall lysates were not consistent with amidase activity. Instead, the structure of the muropeptide digestion fragments indicated that both the LambdaSa1 and LambdaSa2 lysins exhibited {gamma}-D-glutaminyl-L-lysine endopeptidase activity. The endopeptidase cleavage specificity of the lysins was confirmed using a synthetic peptide substrate corresponding to a portion of the stem peptide and cross bridge of Streptococcus agalactiae peptidoglycan. The LambdaSa2 lysin also displayed β-D-N-acetylglucosaminidase activity.

* Corresponding author. Mailing address: Department of Biochemistry & Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave. S., Birmingham, AL 35294-0005. Phone: (205) 934-6023. Fax: (205) 934-6022. E-mail: davidp1{at}uab.edu

{triangledown} Published ahead of print on 28 September 2007.

Applied and Environmental Microbiology, November 2007, p. 7150-7154, Vol. 73, No. 22
0099-2240/07/$08.00+0     doi:10.1128/AEM.01783-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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