Bacteriophage PRD1 encodes two proteins (P7 and P15) that are associated with a muralytic activity. Protein P15 is a soluble β-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.
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机译：噬菌体PRD1编码与村寨活动有关的两个蛋白质（P7和P15）。 P15蛋白是一种可溶的β-1,4- N -乙酰基村酰胺酶，可引起噬菌体诱导的宿主细胞裂解。我们在这里证明，P15也是PRD1病毒体的结构成分，并且它与噬菌体膜连接。小型病毒膜蛋白P20和P22调节P15掺入病毒粒子，并可能将其连接至噬菌体膜。参与PRD1 DNA进入的主要Muralytic蛋白似乎是推定的裂解性转糖基转移酶蛋白P7，因为不存在P15蛋白不会延迟所用病毒宿主系统中噬菌体DNA复制的启动。两种不同的裂解酶掺入病毒粒子可能反映了噬菌体PRD1的广泛宿主范围。
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