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Applied and Environmental Microbiology, July 2006, p. 5108-5112, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.03065-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

The Cell Lysis Activity of the Streptococcus agalactiae Bacteriophage B30 Endolysin Relies on the Cysteine, Histidine-Dependent Amidohydrolase/Peptidase Domain

David M. Donovan,1* Juli Foster-Frey,1 Shengli Dong,2 Geneviève M. Rousseau,3 Sylvain Moineau,3 and David G. Pritchard2

Biotechnology and Germplasm Laboratory, ANRI, ARS, USDA, Bldg. 230, Room 104, BARC-East, 10300 Baltimore Ave., Beltsville, Maryland 20705-23501,1 Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 552 McCallum Basic Health Sciences Building, 1918 University Boulevard, Birmingham, Alabama 35294-0005,2 Département de Biochimie et de Microbiologie, Faculté des Sciences et de Génie, Groupe de Recherche en Écologie Buccale (GREB), Faculté de Médecine Dentaire, Félix d'Hérelle Reference Center for Bacterial Viruses, Université Laval, Québec City, Québec, Canada G1K 7P43

Received 29 December 2005/ Accepted 9 April 2006

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.

* Corresponding author. Mailing address: Biotechnology and Germplasm Laboratory, ANRI, ARS, USDA, Bldg. 230, Room 104, BARC-East, 10300 Baltimore Ave., Beltsville, MD 20705-23501. Phone: (301) 504-9150. Fax: (301) 504-8571. E-mail: ddonovan{at}anri.barc.usda.gov.

Applied and Environmental Microbiology, July 2006, p. 5108-5112, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.03065-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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