کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
6141234 | 1227221 | 2012 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Turnip yellow mosaic virus forms infectious particles without the native beta-annulus structure and flexible coat protein N-terminus Turnip yellow mosaic virus forms infectious particles without the native beta-annulus structure and flexible coat protein N-terminus](/preview/png/6141234.png)
Structural studies have implicated the TYMV N-terminal amino acids of the coat protein (CP) in both static (virion stabilization) and dynamic (RNA encapsidation and disencapsidation) roles. We have deleted residues 2-5, 2-10 and 2-26 from the N-terminus and expressed the mutant CPs in E. coli to assess assembly in the absence of genomic RNA and in plant infections to assess infectivity and virion properties. In E. coli, the deletion constructs formed virus-like particles, but in decreased yield. All mutants were infectious in Chinese cabbage, producing normal symptoms but with a slight delay and decreased viral yields. Virions were progressively less stable with increasing deletion size and also more accessible to small molecules. These results show that the N-terminal 26 amino acids are not essential for viral processes in vivo, although removal of these residues decreases stability and increases porosity, both important factors for virion integrity and survival outside the host.
Journal: Virology - Volume 422, Issue 2, 20 January 2012, Pages 165-173