The structure and function of the outer coat protein VP9 of Banna virus
The structure and function of the outer coat protein VP9 of Banna virus
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DOI：
10.1016/j.str.2004.10.017
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发表时间：
2005-01-01
期刊：
影响因子：
5.7
通讯作者：
De Lamballerie, X
中科院分区：
文献类型：
--
作者：
Jaafar, FM;Attoui, H;De Lamballerie, X
版纳病毒（BAV：呼肠孤病毒科，Seadornavirus属）具有与轮状病毒和蓝舌病毒相似的双壳形态。通过X射线晶体学在2.6埃分辨率下确定BAV外衣壳蛋白VP 9的结构，揭示了由N-末端螺旋束保持在一起的三聚体分子，使人联想到在融合活性蛋白如HIV gp 41中发现的卷曲螺旋结构。VP 9的主要结构域包含堆叠的P片层，其与轮状病毒的受体结合蛋白VP 8具有显著的结构相似性。抗VP 9抗体中和病毒感染性，并且，显著地，用三聚体VP 9预处理细胞增加病毒感染性，表明VP 9参与病毒附着到细胞表面和随后的内化。BAV VP 10和轮状病毒VP 4的VP 5部分之间也检测到序列相似性，这表明受体结合和内化装置是轮状病毒中蛋白水解激活的单个基因产物，是BAV中两个独立基因组片段的产物。
Banna virus (BAV: genus Seadornavirus, family Reoviridae) has a double-shelled morphology similar to rotavirus and bluetongue virus. The structure of BAV outer-capsid protein VP9 was determined by X-ray crystallography at 2.6 Angstrom resolution, revealing a trimeric molecule, held together by an N-terminal helical bundle, reminiscent of coiled-coil structures found in fusion-active proteins such as HIV gp41. The major domain of VP9 contains stacked P sheets with marked structural similarities to the receptor binding protein VP8 of rotavirus. Anti-VP9 antibodies neutralize viral infectivity, and, remarkably, pretreatment of cells with trimeric VP9 increased viral infectivity, indicating that VP9 is involved in virus attachment to cell surface and subsequent internalization. Sequence similarities were also detected between BAV VP10 and VP5 portion of rotavirus VP4, suggesting that the receptor binding and internalization apparatus, which is a single gene product activated by proteoloysis in rotavirus, is the product of two separate genome segments in BAV.