Effect of IgG Fc-fusion and KDEL-ER retention signal on prostate-specific antigen expression in plant and its immune in mice

Transient Plant Expression of Recombinant Rabies Virus Glycoprotein: A strategy for Vaccine Production

“…The procedure for protein extraction from both the infiltrated (with Agrobacterium carrying pEAQ-RVGP-FcK) and non-infiltrated N. benthamiana leaves (130 mg) involved grinding each sample with 390 µL of 1X PBS in a 1.5-mL tube using a homogenizer to extract the total soluble proteins. Following homogenization, 96 µL of the homogenized sample was mixed with 24 µL of a 5X protein sample buffer (Shin et al, 2022). All samples were denatured at 122°C for 10 min.…”

Single-cell transcriptome sequencing of plant leaf expressing anti-HER2 VHH–FcK cancer therapeutic protein

“…Plants are considered a heterologous bio-system for the production of valuable recombinant immunotherapeutic antibody proteins as an alternative to mammalian cell-based systems 5 . In plant expression system, the recombinant antibody genes are controlled by the CaMV35S promoter, which is considered a consistent and non-tissue-specific promoter in plant leaf and is mainly used for its stable or transient expression 6 – 8 . The transgene expression by the cauliflower mosaic virus (CaMV) 35S promoter has been investigated in leaf, root, and stem tissues 9 .…”

Fc engineered anti‐virus therapeutic human IgG1 expressed in plants with altered binding to the neonatal Fc receptor

“…Many therapeutic proteins, such as antibodies and vaccines in plants, have been expressed [ 26–31 ] ) Plant systems have several advantages, including the mass production of recombinant proteins and the absence of pathogenic animal contaminants. [ 32 ] However, the differences in the N ‐glycosylation process between plants and humans and the low expression level are not acceptable for producing therapeutic proteins [ 33–35 ] For example, allergic reactions can be caused by the plant‐derived specific N‐glycans containing β(1, 2)‐xylose and α(1, 3)‐fucose that does not exist in mammalian glycans.…”

“…[22] The humanized antilysozyme heavy chain variant with two mutations in the C H 3 domains (H433K and N434F) showed a 16fold increase in binding to human FcRn at acidic pH while retaining a low affinity at neutral pH in human systems but increased binding affinities at both pH 6.0 and pH 7.4 to mouse FcRn in the murine system. [23][24][25] Many therapeutic proteins, such as antibodies and vaccines in plants, have been expressed [26][27][28][29][30][31] ) Plant systems have several advantages, including the mass production of recombinant proteins and the absence of pathogenic animal contaminants. [32] However, the differ-ences in the N-glycosylation process between plants and humans and the low expression level are not acceptable for producing therapeutic proteins [33][34][35] For example, allergic reactions can be caused by the plant-derived specific N-glycans containing β(1, 2)-xylose and α(1,…”