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Archives of Virology

, Volume 149, Issue 5, pp 997–1005 | Cite as

Regions on nucleocapsid protein of Newcastle disease virus that interact with its phosphoprotein

  • C. L. Kho
  • W. S. Tan
  • B. T. Tey
  • K. Yusoff
Brief Report

Summary.

The nucleocapsid (NP) and phospho-(P) proteins of paramyxoviruses are involved in transcription and replication of the viral genome. An in vitro protein binding assay was used to investigate the regions on NP protein that interact with the P protein of Newcastle disease virus (NDV). Truncated NP mutants were first immobilised on a solid phase and then interacted with radio-labelled [35S]-P protein synthesised in rabbit reticulocyte. The interaction affinity was quantitated by measuring the radioactivity that was retained on the solid phase. Using this approach, a highly interactive region was identified to be resided at the first 25 amino acids of NP N-terminus. The interaction between these two proteins remained strong even with the removal of 114 amino acids from the C-terminal end of NP. However, it is possible that the 49 amino acids at the C-terminal end might have another contact region for P protein, which is not as critical as the N-terminal end. The interaction regions mapped in this study are significantly different from the other two paramyxoviruses: Sendai and measles viruses in which the C-termini of their NP proteins play an important role in binding to the P.

Keywords

Measle Disease Virus Phospho Binding Assay Viral Genome 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag/Wien 2004

Authors and Affiliations

  • C. L. Kho
    • 1
  • W. S. Tan
    • 1
    • 2
  • B. T. Tey
    • 3
  • K. Yusoff
    • 1
    • 2
  1. 1.Department of Biochemistry and Microbiology, Faculty of Science and Environmental StudiesUniversiti Putra MalaysiaSerdangMalaysia
  2. 2.Institute of Bioscience, Universiti Putra MalaysiaSerdangMalaysia
  3. 3.Department of Chemical and Environmental Engineering, Faculty of EngineeringUniversiti Putra MalaysiaSerdangMalaysia

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