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: | David M. Donovan, Juli Foster-Frey, Shengli Dong, Genevi ve M. Rousseau, Sylvain Moineau, David G. Pritchard |
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| Affiliation: | David M. Donovan, Juli Foster-Frey, Shengli Dong, Geneviève M. Rousseau, Sylvain Moineau, and David G. Pritchard |
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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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