The Cell Lysis Activity of the Streptococcus agalactiae Bacteriophage B30 Endolysin Relies on the Cysteine, Histidine-Dependent Amidohydrolase/Peptidase Domain-Reference-Cited by-同舟云学术

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

Published:2006-07 Issue:7 Volume:72 Page:5108-5112
ISSN:0099-2240
Container-title:Applied and Environmental Microbiology
language:en
Short-container-title:Appl Environ Microbiol

Author:

Donovan David M.¹,Foster-Frey Juli¹,Dong Shengli²,Rousseau Geneviève M.³,Moineau Sylvain³,Pritchard David G.²

Affiliation:

1. Biotechnology and Germplasm Laboratory, ANRI, ARS, USDA, Bldg. 230, Room 104, BARC-East, 10300 Baltimore Ave., Beltsville, Maryland 20705-23501

2. Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 552 McCallum Basic Health Sciences Building, 1918 University Boulevard, Birmingham, Alabama 35294-0005

3. 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 7P4

Abstract

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.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Link

https://journals.asm.org/doi/pdf/10.1128/AEM.03065-05

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