Characterization of the protease domain of Rice tungro bacilliform virus responsible for the processing of the capsid protein from the polyprotein

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• 作者：Philippe Marmey (1)
  Ana Rojas-Mendoza (2)
  Alexandre de Kochko (1)
  Roger N Beachy (3)
  Claude M Fauquet (3)
  
• 刊名：Virology Journal
• 出版年：2005
• 出版时间：December 2005
• 年：2005
• 卷：2
• 期：1
• 全文大小：1589KB
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• 作者单位：Philippe Marmey (1)
  Ana Rojas-Mendoza (2)
  Alexandre de Kochko (1)
  Roger N Beachy (3)
  Claude M Fauquet (3)
  
  1. IRD, UMR 芦DGPC禄, B.P. 64501, 34394, Montpellier cedex 5, France
  2. Protein Design Group, Centro Nacional de Biotecnologia, Campus Universidad Autonoma Cantoblanco, 28049, Madrid, Spain
  3. Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, MO, 63132, USA
  
• ISSN：1743-422X

文摘

Background Rice tungro bacilliform virus (RTBV) is a pararetrovirus, and a member of the family Caulimoviridae in the genus Badnavirus. RTBV has a long open reading frame that encodes a large polyprotein (P3). Pararetroviruses show similarities with retroviruses in molecular organization and replication. P3 contains a putative movement protein (MP), the capsid protein (CP), the aspartate protease (PR) and the reverse transcriptase (RT) with a ribonuclease H activity. PR is a member of the cluster of retroviral proteases and serves to proteolytically process P3. Previous work established the N- and C-terminal amino acid sequences of CP and RT, processing of RT by PR, and estimated the molecular mass of PR by western blot assays. Results A molecular mass of a protein that was associated with virions was determined by in-line HPLC electrospray ionization mass spectral analysis. Comparison with retroviral proteases amino acid sequences allowed the characterization of a putative protease domain in this protein. Structural modelling revealed strong resemblance with retroviral proteases, with overall folds surrounding the active site being well conserved. Expression in E. coli of putative domain was affected by the presence or absence of the active site in the construct. Analysis of processing of CP by PR, using pulse chase labelling experiments, demonstrated that the 37 kDa capsid protein was dependent on the presence of the protease in the constructs. Conclusion The findings suggest the characterization of the RTBV protease domain. Sequence analysis, structural modelling, in vitro expression studies are evidence to consider the putative domain as being the protease domain. Analysis of expression of different peptides corresponding to various domains of P3 suggests a processing of CP by PR. This work clarifies the organization of the RTBV polyprotein, and its processing by the RTBV protease.