Production of FMDV virus-like particles by a SUMO fusion protein approach in Escherichia coli.
Virus-like particles (VLPs) are formed by the self-assembly of envelope and/or capsid proteins from many viruses. Some VLPs have been proven successful as vaccines, and others have recently found applications as carriers for foreign antigens or as scaffolds in nanoparticle biotechnology. However, production of VLP was usually impeded due to low water-solubility of recombinant virus capsid proteins. Previous studies revealed that virus capsid and envelope proteins were often posttranslationally modified by SUMO in vivo, leading into a hypothesis that SUMO modification might be a common mechanism for virus proteins to retain water-solubility or prevent improper self-aggregation before virus assembly. We then propose a simple approach to produce VLPs of viruses, e.g., foot-and-mouth disease virus (FMDV). An improved SUMO fusion protein system we developed recently was applied to the simultaneous expression of three capsid proteins of FMDV in E. coli. The three SUMO fusion proteins formed a stable heterotrimeric complex. Proteolytic removal of SUMO moieties from the ternary complexes resulted in VLPs with size and shape resembling the authentic FMDV. The method described here can also apply to produce capsid/envelope protein complexes or VLPs of other disease-causing viruses.
Lee
Chien-Der
CD
Institute of Molecular Biology, Academia Sinica, Taipei 11529, Taiwan, Republic of China. cdlee@gate.sinica.edu.tw
Yan
Yao-Pei
YP
Liang
Shu-Mei
SM
Wang
Ting-Fang
TF
D002213:Capsid / Q000648:ultrastructure*; D036022:Capsid Proteins / Q000737:chemistry* / Q000648:ultrastructure; D004926:Escherichia coli; D029544:Foot-and-Mouth Disease Virus / Q000737:chemistry* / Q000648:ultrastructure; D008854:Microscopy, Electron; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D011499:Protein Processing, Post-Translational; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D012995:Solubility; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000648:ultrastructure; D014867:Water
D036022:Capsid Proteins; D046912:Multiprotein Complexes; D011993:Recombinant Fusion Proteins; C099362:SMT3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D025841:Small Ubiquitin-Related Modifier Proteins; C442501:VP1 protein, Foot-and-mouth disease virus; C442460:VP3 protein, Foot-and-mouth disease virus; D015678:Viral Structural Proteins; D014867:Water