Mutations that hamper dimerization of foot-and-mouth disease virus 3A protein are detrimental for infectivity.

  title={Mutations that hamper dimerization of foot-and-mouth disease virus 3A protein are detrimental for infectivity.},
  author={M{\'o}nica Gonz{\'a}lez-Magaldi and Ra{\'u}l Postigo and Beatriz G de la Torre and Yuri A. Vieira and Miguel Rodr{\'i}guez-Pulido and Eduardo L{\'o}pez-Vi{\~n}as and Paulino G{\'o}mez-Puertas and David Andreu and Leonor Kremer and Mar{\'i}a Flora Rosas and Francisco Sobrino},
  journal={Journal of virology},
  volume={86 20},
Foot-and-mouth disease virus (FMDV) nonstructural protein 3A plays important roles in virus replication, virulence, and host range. In other picornaviruses, homodimerization of 3A has been shown to be relevant for its biological activity. In this work, FMDV 3A homodimerization was evidenced by an in situ protein fluorescent ligation assay. A molecular model of the FMDV 3A protein, derived from the nuclear magnetic resonance (NMR) structure of the poliovirus 3A protein, predicted a hydrophobic… CONTINUE READING
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