The lytic enzyme of bacteriophage PRD1 is associated with the viral membrane.
Bacteriophage PRD1 encodes two proteins (P7 and P15) that are associated with a muralytic activity. Protein P15 is a soluble beta-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.
Rydman
Pia S
PS
Department of Biosciences and Institute of Biotechnology, Viikki Biocenter, University of Helsinki, 00014 University of Helsinki, Finland.
Bamford
Dennis H
DH
D001433:Bacteriolysis; D025622:Bacteriophage PRD1 / Q000201:enzymology* / Q000254:growth & development; D004261:DNA Replication; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000821:virology*; D009113:Muramidase / Q000302:isolation & purification* / Q000378:metabolism; D014763:Viral Matrix Proteins / Q000302:isolation & purification* / Q000378:metabolism; D014764:Viral Proteins
D014763:Viral Matrix Proteins; D014764:Viral Proteins; D006026:Glycoside Hydrolases; C090044:P15 protein, Enterobacteria phage PRD1; C443982:P7 protein, bacteriophage PRD1; D009113:Muramidase