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Journal of Bacteriology, January 2002, p. 104-110, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.104-110.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Lytic Enzyme of Bacteriophage PRD1 Is Associated with the Viral Membrane

Pia S. Rydman and Dennis H. Bamford*

Department of Biosciences and Institute of Biotechnology, Viikki Biocenter, University of Helsinki, 00014 University of Helsinki, Finland

Received 23 July 2001/ Accepted 26 September 2001

Bacteriophage PRD1 encodes two proteins (P7 and P15) that are associated with a muralytic activity. Protein P15 is a soluble ß-1,4-N-acetylmuramidase that causes phage-induced host cell lysis. We demonstrate here that P15 is also a structural component of the PRD1 virion and that it is connected to the phage membrane. Small viral membrane proteins P20 and P22 modulate incorporation of P15 into the virion and may connect it to the phage membrane. The principal muralytic protein involved in PRD1 DNA entry seems to be the putative lytic transglycosylase protein P7, as the absence of protein P15 did not delay initiation of phage DNA replication in the virus-host system used. The incorporation of two different lytic enzymes into virions may reflect the broad host range of bacteriophage PRD1.

* Corresponding author. Mailing address: Viikki Biocenter, P.O. Box 56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland. Phone: 358-9-19159100. Fax: 358-9-19159098. E-mail: dennis.bamford{at}helsinki.fi.

Journal of Bacteriology, January 2002, p. 104-110, Vol. 184, No. 1
0021-9193/01/$04.00+0     DOI: 10.1128/JB.184.1.104-110.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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