Role of the Gp16 lytic transglycosylase motif in bacteriophage T7 virions at the initiation of infection
Role of the Gp16 lytic transglycosylase motif in bacteriophage T7 virions at the initiation of infection
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DOI：
10.1046/j.1365-2958.2000.01995.x
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发表时间：
2000-07-01
影响因子：
3.6
通讯作者：
Molineux, IJ
中科院分区：
文献类型：
--
作者：
Moak, M;Molineux, IJ
噬菌体T7 GP16的二糖基化酶活性的预测催化谷氨酸残基对于噬菌体生长不是必不可少的，但在感染e耐神经大肠杆菌细胞期间具有有益于高细胞密度，其中膜蛋白更高度交叉链接。在没有推定的乳糖基酶的情况下，噬菌体基因组的内在化在感染过程中显着延迟。 GP16的裂解糖基化酶基序对于低于20摄氏度的温度下的噬菌体生长至关重要，表明这些生长条件也导致肽聚糖的交联增加。 SLTY，大肠溶性溶解裂解糖基化酶的过表达部分补充了突变噬菌体颗粒感染的缺陷，从而使它们能够在较高的效率下感染。相反，SLTY缺失增加了野生型噬菌体的潜在时期。
The predicted catalytic glutamate residue for transglycosylase activity of bacteriophage T7 gp16 is not essential for phage growth, but is shown to be beneficial during infection of Escherichia coli cells grown to high cell density, conditions in which murein is more highly cross-linked. In the absence of the putative transglycosylase, internalization of the phage genome is significantly delayed during infection. The lytic transglycosylase motif of gp16 is essential for phage growth at temperatures below 20 degrees C, indicating that these growth conditions also lead to increased cross-linking of peptidoglycan. Overexpression of sltY, E. coli soluble lytic transglycosylase, partially complements the defect in infection of mutant phage particles, allowing them to infect at higher efficiencies. Conversely, an sltY deletion increases the latent period of wild-type phage.