Microbial pathogenesis, 2017-11, Vol.112, p.111-116
2017
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Details
- Autor(en) / Beteiligte
- Titel
- eEF1G interaction with foot-and-mouth disease virus nonstructural protein 2B: Identification by yeast two-hybrid system
- Ist Teil von
- Microbial pathogenesis, 2017-11, Vol.112, p.111-116
- Ort / Verlag
- England: Elsevier Ltd
- Erscheinungsjahr
- 2017
- Quelle
- Access via ScienceDirect (Elsevier)
- Beschreibungen/Notizen
- Foot-and-mouth disease virus (FMDV) is a picornavirus that causes an economically significant disease in cattle and swine. Replication of FMDV is dependent on both viral proteins and cellular factors. Nonstructural protein 2B of FMDV plays multiple roles during viral infection and replication. We investigated the roles of 2B in virus–host interactions by constructing a cDNA library obtained from FMDV-infected swine tissues, and used a split-ubiquitin-based yeast two-hybrid system to identify host proteins that interacted with 2B. We found that 2B interacted with amino acids 208–437 in the C-terminal region of the eEF1G subunit of eukaryotic elongation factor 1, which is essential for protein synthesis. The 2B–eEF1G interaction was confirmed by co-immunoprecipitation of 2B and eEF1G in HEK293T cells. Collectively, our results suggest that eEF1G interacts with the 2B protein of FMDV. The identified 2B interaction partner may help to elucidate the mechanisms of FMDV infection and replication.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0882-4010eISSN: 1096-1208DOI: 10.1016/j.micpath.2017.09.039Titel-ID: cdi_proquest_miscellaneous_1942698374
- Format
- –
- Schlagworte
- Animals, Disease Models, Animal, Eukaryotic translation elongation factor 1 gamma, Foot-and-Mouth Disease, Foot-and-mouth disease virus, Foot-and-Mouth Disease Virus - metabolism, Foot-and-Mouth Disease Virus - pathogenicity, HEK293 Cells, Host-Pathogen Interactions, Humans, Immunoprecipitation - methods, Peptide Elongation Factor 1 - metabolism, Protein Binding, Protein Interaction Domains and Motifs, Swine, Two-Hybrid System Techniques, Viral Nonstructural Proteins - isolation & purification, Viral Proteins, Viral Regulatory and Accessory Proteins - metabolism, Virus Replication, Virus–host interactions