Gedvilaite A, Aleksaite E, Staniulis J, Ulrich R, Sasnauskas K
Institute of Biotechnology, Vilnius, Lithuania.
Arch Virol. 2006 Sep;151(9):1811-25. doi: 10.1007/s00705-006-0745-8. Epub 2006 Mar 30.
The hamster polyomavirus major capsid protein VP1 was modified in its carboxy-terminal region by consecutive truncations and single amino acid exchanges. The ability of yeast-expressed VP1 variants to form virus-like particles (VLPs) strongly depended on the size and position of the truncation. VP1 variants lacking 21, 69, and 79 amino acid (aa) residues in their carboxy-terminal region efficiently formed VLPs similar to those formed by the unmodified VP1 (diameter 40-45 nm). In contrast, VP1 derivatives with carboxy-terminal truncations of 35 to 56 aa residues failed to form VLPs. VP1 mutants with a single A336G aa exchange or internal deletions of aa 335 to aa 346 and aa 335 to aa 363 resulted in the formation of VLPs of a smaller size (diameter 20 nm). These data indicate that certain parts of the carboxy-terminal region of VP1 are not essential for pentamer-pentamer interactions in the capsid, at least in the yeast expression system used.
仓鼠多瘤病毒主要衣壳蛋白VP1在其羧基末端区域通过连续截短和单个氨基酸交换进行了修饰。酵母表达的VP1变体形成病毒样颗粒（VLP）的能力强烈依赖于截短的大小和位置。在其羧基末端区域缺少21、69和79个氨基酸（aa）残基的VP1变体有效地形成了与未修饰的VP1形成的颗粒相似的VLP（直径40 - 45纳米）。相反，羧基末端截短35至56个aa残基的VP1衍生物未能形成VLP。具有单个A336G氨基酸交换或aa 335至aa 346以及aa 335至aa 363内部缺失的VP1突变体导致形成较小尺寸（直径20纳米）的VLP。这些数据表明，至少在所使用的酵母表达系统中，VP1羧基末端区域的某些部分对于衣壳中五聚体 - 五聚体相互作用不是必需的。
