Virus-like particles (VLPs) are structures of self-assembled virus coat proteins that can be used in a number of fields of research like biology, biotechnology, medicine, bio pharmacy, material science and electronics. We have focused on plant flexible filamentous virus-like particles for applications in biotechnology. We expressed coat protein in fusion with melittin, enhanced yellow fluorescent protein (EYFP) and equinatoxin II, respectively. Our aim was to co-express the fusion protein with the wild type coat protein, which would lead to incorporation of both forms of protein into VLP and would allow surface presentation of larger proteins. As a result, we obtained different lengths of VLPs depending on the chosen method of co-expression. Fibrils in the samples with chimeric proteins did form, but they were in general shorter than wild type VLPs and the length of the fibril was inversely proportional to amount of expressed fusion protein. The conclusion was that the stoichiometry of chimeric and wild type protein is important for VLP assembly. We could also observe the fluorescence of EYFP, meaning that the fusion did not affect protein folding and activity.
B.03 Paper at an international scientific conferenceCOBISS.SI-ID: 6085914
Infection of a plant by a pathogen initiates a complex interaction between both players involved, leading to changes in the complex signalling network, which result in gene activity changes and reprogramming of the cell metabolism. A systems biology approach was adopted for the purpose of modelling complex biological processes in order to understand the mechanisms and dynamics involved in potato plant defense following the infection with potato virus Y (PVY). A qualitative model of potato plant defence signalling network (PDS) was constructed (Miljkovic et al., 2012), describing the biosynthesis and signal transduction pathways for three crucial phytohormones involved in plant defence: salicylic acid (SA), jasmonic acid (JA) and ethylene (ET). The prior knowledge from literature was expanded with information on the viral and plant component interactions, protein-protein interactions and protein-DNA interactions in plant Arabidopsis.
B.04 Guest lectureCOBISS.SI-ID: 3900239