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Department of Biochemistry and Molecular Genetics, MCLM 552, 1530 3rd Ave S, University of Alabama at Birmingham, Birmingham, AL 35294-0005, USA
Correspondence
David G. Pritchard
davidp1{at}uab.edu
A group B streptococcal (GBS) bacteriophage lysin gene was cloned and expressed in Escherichia coli. The purified recombinant enzyme, calculated to have a molecular mass of 49 677 Da, lysed GBS cells. The susceptibility of GBS cells to lysis by the enzyme depended upon the growth stage at which they were harvested, with early exponential phase cells most sensitive. Calcium ions enhanced the activity of the enzyme. The enzyme also lysed other 
-haemolytic streptococci, including groups A, C, E and G streptococci, but not common oral streptococci, including Streptococcus mutans. The generation of both reducing activity and N-terminal alanine residues during lysis indicated that the lysin is a bifunctional enzyme, possessing both glycosidase and endopeptidase activities. This is consistent with the presence of two conserved sequence domains, an Acm (acetylmuramidase) domain associated with lysozyme activity, and a CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain associated with endopeptidase activity. Site-directed mutagenesis of conserved cysteine and histidine residues in the CHAP domain and conserved aspartate and glutamate residues in the Acm domain confirmed their importance for lysozyme and endopeptidase activity respectively.
-N-acetylmuramidase domain; CHAP domain, cysteine histidine-dependent amidohydrolases/peptidases domain; GBS, group B streptococci (Streptococcus agalactiae); TNBS, 2,4,6-trinitrobenzenesulfonic acidThe GenBank accession number for the nucleotide sequence of the GBS phage lysin and flanking regions reported in this paper is AY149214.
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