Article
Mutations that hamper dimerization of foot-and-mouth disease virus 3A protein are detrimental for infectivity.
Journal of virology - 1 Oct 2012
González-Magaldi Mónica, Postigo Raúl, de la Torre Beatriz G, Vieira Yuri A, Rodríguez-Pulido Miguel, López-Viñas Eduardo, Gómez-Puertas Paulino, Andreu David, Kremer Leonor, Rosas María F, Sobrino Francisco
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Cell Line
- Chlorocebus aethiops
- Cricetinae
- Foot-and-Mouth Disease
- Foot-and-Mouth Disease Virus
- Hydrophobic and Hydrophilic Interactions