Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer.

@article{Lawton1997ThreedimensionalSA,
  title={Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal-deleted VP2: implications for the architecture of the VP2 capsid layer.},
  author={Jeffrey A. Lawton and Carl Q-Y Zeng and Sharmila K. Mukherjee and Jean Cohen and Mary K. Estes and B. V. Venkataram Prasad},
  journal={Journal of virology},
  year={1997},
  volume={71 10},
  pages={
          7353-60
        }
}
Rotaviruses are the leading cause of severe infantile gastroenteritis worldwide. These viruses are large, complex icosahedral particles consisting of three concentric capsid layers enclosing a genome of eleven segments of double-stranded RNA (dsRNA). The amino terminus of the innermost capsid protein VP2 possesses a nonspecific single-stranded RNA and dsRNA binding activity, and the amino terminus is also essential for the incorporation of the polymerase enzyme VP1 and guanylyltransferase VP3… CONTINUE READING

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