Generation of multi-layered protein bodies in for the encapsulation of vaccine antigens.

The ability of plants to assemble particulate structures such as virus-like particles and protein storage organelles allows the direct bioencapsulation of recombinant proteins during the manufacturing process, which holds promise for the development of new drug delivery vehicles. Storage organelles found in plants such as protein bodies (PBs) have been successfully used as tools for accumulation and encapsulation of recombinant proteins. The fusion of sequences derived from 27-kDa-γ-zein, a major storage protein of maize, with a protein of interest leads to the incorporation of the chimeric protein into the stable and protected environment inside newly induced PBs.

Corrigendum: 3D Electron Microscopy Gives a Clue: Maize Zein Bodies Bud From Central Areas of ER Sheets.

[This corrects the article DOI: 10.3389/fpls.2020.

3D Electron Microscopy Gives a Clue: Maize Zein Bodies Bud From Central Areas of ER Sheets.

Zeins are the main storage proteins in maize seed endosperm, and the onset of zein synthesis in young seeds challenges the endomembrane system and results in the formation of storage organelles. Even though zeins lack a conventional endoplasmic reticulum (ER) retention signal, they accumulate within the ER and assemble in conspicuous ER-derived protein bodies (PBs) stabilized by disulfide bridge formation and hydrophobic interaction between zein chains. Zein body formation during seed development has been extensively studied, as well as the mechanisms that lead to the initiation of PBs.

Involvement of the eIF2α Kinase GCN2 in UV-B Responses.

() is a serine/threonine-protein kinase that regulates translation in response to stressors such as amino acid and purin deprivation, cold shock, wounding, cadmium, and UV-C exposure. Activated phosphorylates the α-subunit of the eukaryotic initiation factor 2 (eIF2) leading to a drastic inhibition of protein synthesis and shifting translation to specific mRNAs. To investigate the role of in responses to UV-B radiation its activity was analyzed through eIF2α phosphorylation assays in mutants of the specific UV-B and stress signaling pathways of .