کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
3427480 | 1227399 | 2007 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles Enzymatic treatment of duck hepatitis B virus: Topology of the surface proteins for virions and noninfectious subviral particles](/preview/png/3427480.png)
The large surface antigen L of duck hepatitis B virus exhibits a mixed topology with the preS domains of the protein alternatively exposed to the particles' interior or exterior. After separating virions from subviral particles (SVPs), we compared their L topologies and showed that both particle types exhibit the same amount of L with the following differences: 1—preS of intact virions was enzymatically digested with chymotrypsin, whereas in SVPs only half of preS was accessible, 2—phosphorylation of L at S118 was completely removed by phosphatase treatment only in virions, 3—iodine-125 labeling disclosed a higher ratio of exposed preS to S domains in virions compared to SVPs. These data point towards different surface architectures of virions and SVPs. Because the preS domain acts in binding to a cellular receptor of hepatocytes, our findings implicate the exclusion of SVPs as competitors for the receptor binding and entry of virions.
Journal: Virology - Volume 359, Issue 1, 1 March 2007, Pages 126–136