噬菌体PRD1的整合膜蛋白P16可稳定吸附顶点结构。
Integral membrane protein P16 of bacteriophage PRD1 stabilizes the adsorption vertex structure.
作者信息
Jaatinen Silja T, Viitanen Salla J, Bamford Dennis H, Bamford Jaana K H
机构信息
Viikki Biocenter 2, P.O. Box 56 (Viikinkaari 5), FIN-00014 University of Helsinki, Finland.
出版信息
J Virol. 2004 Sep;78(18):9790-7. doi: 10.1128/JVI.78.18.9790-9797.2004.
The icosahedral membrane-containing double-stranded DNA bacteriophage PRD1 has a labile receptor binding spike complex at the vertices. This complex, which is analogous to that of adenovirus, is formed of the penton protein P31, the spike protein P5, and the receptor binding protein P2. Upon infection, the internal phage membrane transforms into a tubular structure that protrudes through a vertex and penetrates the cell envelope for DNA injection. We describe here a new class of PRD1 mutants lacking virion-associated integral membrane protein P16. P16 links the spike complex to the viral membrane and is necessary for spike stability. We also show that the unique vertex used for DNA packaging is intact in the P16-deficient particle, indicating that the 11 adsorption vertices and the 1 portal vertex are functionally and structurally distinct.
二十面体含膜双链DNA噬菌体PRD1在其顶点处有一个不稳定的受体结合刺突复合体。这个复合体类似于腺病毒的复合体，由五聚体蛋白P31、刺突蛋白P5和受体结合蛋白P2组成。感染时，噬菌体内部膜转化为管状结构，该结构从一个顶点伸出并穿透细胞包膜以进行DNA注射。我们在此描述了一类新的PRD1突变体，它们缺乏与病毒体相关的整合膜蛋白P16。P16将刺突复合体与病毒膜连接起来，是刺突稳定性所必需的。我们还表明，用于DNA包装的独特顶点在缺乏P16的颗粒中是完整的，这表明11个吸附顶点和1个门户顶点在功能和结构上是不同的。
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