The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain |
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| Authors: | Donovan David M Foster-Frey Juli Dong Shengli Rousseau Geneviève M Moineau Sylvain Pritchard David G |
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| Institution: | Biotechnology and Germplasm Laboratory, ANRI, ARS, USDA, Bldg. 230, Room 104, BARC-East, 10300 Baltimore Ave., Beltsville, MD 20705-23501, USA. ddonovan@anri.barc.usda.gov |
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| Abstract: | The Streptococcus agalactiae bacteriophage B30 endolysin contains three domains: cysteine, histidine-dependent amidohydrolase/peptidase (CHAP), Acm glycosidase, and the SH3b cell wall binding domain. Truncations and point mutations indicated that the Acm domain requires the SH3b domain for activity, while the CHAP domain is responsible for nearly all the cell lysis activity. |
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