A single mutation in the carboxy terminus of reovirus outer-capsid protein sigma 3 confers enhanced kinetics of sigma 3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in sigma 3 structure.

@article{Wilson2002ASM,
  title={A single mutation in the carboxy terminus of reovirus outer-capsid protein sigma 3 confers enhanced kinetics of sigma 3 proteolysis, resistance to inhibitors of viral disassembly, and alterations in sigma 3 structure.},
  author={Gregory J. Wilson and Emma L. Nason and Charles S. Hardy and Daniel H. Ebert and Jacqueline Denise Wetzel and B. V. Venkataram Prasad and Terence S Dermody},
  journal={Journal of virology},
  year={2002},
  volume={76 19},
  pages={9832-43}
}
Mammalian reoviruses undergo acid-dependent proteolytic disassembly within endosomes, resulting in formation of infectious subvirion particles (ISVPs). ISVPs are obligate intermediates in reovirus disassembly that mediate viral penetration into the cytoplasm. The initial biochemical event in the reovirus disassembly pathway is the proteolysis of viral outer-capsid protein sigma 3. Mutant reoviruses selected during persistent infection of murine L929 cells (PI viruses) demonstrate enhanced… CONTINUE READING