
pmid: 22404610
Identification of structural protein relationships is likely to be important for virus assembly and anti-WSSV strategies. In this paper, VP90 of white spot syndrome virus (WSSV) was characterized. Temporal-transcription analysis showed that VP90 is expressed in the late stage of WSSV infection. Far-western and matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) assay showed that VP90 interacts with VP26 and VP28, two major envelope proteins. Far-western blot with recombinant VP26 (rVP26), N-terminal end of VP28 (rVP28N) and C-terminal end of VP28 (rVP28C) provided further evidence for interaction of rVP90 and rVP26 or rVP28. These results suggest that VP90 is anchored to the envelope through interacting with VP26 and VP28.
Blotting, Far-Western, Recombinant Proteins, White spot syndrome virus 1, Penaeidae, Viral Envelope Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Escherichia coli, Animals, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular, Plasmids, Protein Binding
Blotting, Far-Western, Recombinant Proteins, White spot syndrome virus 1, Penaeidae, Viral Envelope Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Escherichia coli, Animals, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular, Plasmids, Protein Binding
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