Kao S H, McClain W H
J Virol. 1980 Apr;34(1):95-103. doi: 10.1128/JVI.34.1.95-103.1980.
Analyses of a new bacteriophage T4 mutant that permits lysis of infected cells in the absence of e lysozyme showed that the strain carried a suppressor mutation in gene 5, a gene whose polypeptide product (gp5) is an integral component of the virion baseplate. Indirect experiments indicated that cell lysis was caused by the lytic action of mutant gp5. With regard to the physiological role of normal gp5, we speculate that it functions in the initiation of infection by catalyzing local cell wall digestion to facilitate penetration of the tail tube through the cell envelope. The proposed lytic activity of gp5 may also be responsible for the well-known phenomenon of lysis from without observed with T4.
对一种新的噬菌体T4突变体进行分析，该突变体在没有e溶菌酶的情况下也能使受感染的细胞裂解，结果表明该菌株在基因5中携带了一个抑制突变，该基因的多肽产物（gp5）是病毒体基板的一个组成部分。间接实验表明，细胞裂解是由突变型gp5的裂解作用引起的。关于正常gp5的生理作用，我们推测它通过催化局部细胞壁消化来促进尾管穿透细胞包膜，从而在感染起始过程中发挥作用。所提出的gp5的裂解活性也可能是T4所观察到的众所周知的自外裂解现象的原因。
