Engineered self-assembly of plant proteins into α-ketoglutarate-loaded nanoplatforms for osteoarthritis treatment.

Glycosylphosphatidylinositol (GPI)-anchored proteins play critical roles in plant development, reproduction, and environmental responses. However, their biochemical characterization in plants remains limited. LORELEI, a putative GPI-anchored protein involved in pollen tube reception and early seed development in Arabidopsis (Arabidopsis thaliana), has lacked direct biochemical evidence confirming its GPI anchoring. This study employed biochemical approaches to validate LORELEI as a GPI-anchored protein. We demonstrate that ectopic expression of wild-type LORELEI fused to a reporter protein in vegetative tissues associates with a detergent-resistant membrane fraction and is sensitive to GPI-specific cleavage enzymes, thereby confirming that it is a GPI-anchored protein. Moreover, we show that mutations in the ω-sites or the GPI attachment signal of LORELEI disrupt its membrane localization, highlighting the necessity of these structural elements for proper GPI anchoring. Analysis of a reporter-fused LORELEI protein in the loss-of-function mutant of GPI8, which encodes the catalytic subunit of the GPI transamidase complex involved in GPI anchor addition, results in the appearance of prominent higher molecular weight bands, further supporting its role in GPI anchoring of the LORELEI protein. This study provides direct biochemical evidence confirming LORELEI as a GPI-anchored protein and sheds light on the structural determinants required for its GPI anchoring. Additionally, our study demonstrates that heterologous ectopic expression of LORELEI in vegetative tissues provides a viable alternative for the biochemical characterization of GPI-anchored proteins predominantly expressed in hard-to-access and small-sized female gametophytes. Our findings underscore the role of GPI anchoring in membrane localization and biosynthesis of GPI-anchored proteins in plants.

Understanding and overcoming protein production bottlenecks in plants.

While consumption of plant proteins providing nutritional, social and climate solutions to feed a growing population in a healthy and sustainable manner is unquestionable, astringency remains a persistent yet underestimated organoleptic challenge. This longstanding issue, contributing to a sensation of dryness, serves as a major bottleneck in the development of plant-based foods with broad consumer acceptance. Here, we investigate experimentally the origin of astringency in plant proteins probing sensory, neural, and cellular responses. Strikingly, by combining sensory profiling with functional near-infrared spectroscopy (fNIRS) and saliva and mucin-coated oral epithelium-mimicking cell lines, we identify that plant protein astringency demonstrates a distinct prefrontal cortex neural response and is associated with salivary mucin-binding, drawing parallels to tannin-like responses. Our mechanistic dissection fuelled by in vitro, in vivo, and ex vivo experimental studies pinpoints direct quantitative evidence uncovering previously uncharacterised astringency of plant proteins, paving the way for solving the sensorial challenges in the era of transitioning towards eco-friendly plant protein-based foods.

M. Chow-shi-yée, M. Grondin, D. A. Averill-Bates, and F. Ouellet, "Plant Protein 2-Cys Peroxiredoxin TaBAS1 Alleviates Oxidative and Nitrosative Stresses Incurred During Cryopreservation of Mammalian Cells," Biotechnology and Bioengineering 113, no. 7 (2016): 1511-1521, https://doi.org/10.1002/bit.25921. The above article, published online on 1 January 2016 in Wiley Online Library (wileyonlinelibrary.com), has been retracted by agreement between the journal Editor-in-Chief, Douglas S. Clark; and Wiley Periodicals LLC. The retraction has been agreed due to concerns raised by third parties. Specifically, Figure 4A was found to contain repetitive elements (i.e., cells) suggesting inappropriate image processing. Investigation by the publisher has confirmed the validity of the concerns. The authors were unable to retrieve the raw data underlying Figure 4A due to the time elapsed since original publication. They also stated that the images presented in Figure 4A were acquired as original images and have not been altered in any form. The authors conducted an independent analysis of the magnified published images, highlighting that the cells identified as duplicated exhibit differences. According to the authors, the observed similarities are characteristic of cells within a homogeneous population (i.e., hepatocytes) and are therefore to be expected, thereby refuting allegations of inappropriate image editing. However, the editors have deemed the clarification from the authors as insufficient to resolve their concerns. The similarities detected in Figure 4A were found to outweigh the differences highlighted by the authors and were considered unlikely to result solely from morphological resemblance within a homogeneous population of primary isolated hepatocytes. The editors have determined that the new experimental data generated by the authors to replace the images in Figure 4A were unsuitable for direct comparison with the originally published data, due to the substantial time gap between the two experimental sets. Therefore, the concerns of the editors were not addressed acceptably and accordingly, the article must be retracted. The authors disagree with the retraction decision.

A model food mimicking plant-based meat analogues for determination of matrix effects on growth of Listeria monocytogenes.

A desiccation-induced chloroplast DnaJ/HSP40 gene, BhDnaJC6, from the resurrection plant enhances photosynthesis and cotton drought tolerance via interaction with and stabilization of Rieske iron-sulfur protein (PetC) in transgenic cotton plants. Drought stress severely affects cotton productivity and seedling survival. Resurrection plants are known for their unique mechanisms of desiccation tolerance, including the maintenance of photosynthetic proteins during dehydration and rehydration, making their genes valuable for drought-tolerant cotton breeding. Chloroplast DnaJ proteins play roles in protein quality control in plant cells. Here, we report the identification and functional characterization of a chloroplast-localized C-type DnaJ protein-coding gene BhDnaJC6 from the resurrection plant Boea hygrometrica. BhDnaJC6 transcripts accumulate in response to slow desiccation, and rapid desiccation in acclimated (desiccation-tolerant) but not non-acclimated (desiccation-sensitive) B. hygrometrica plants. Microscopic observation confirmed the cellular localization of BhDnaJC6-GFP in chloroplasts in transiently transformed tobacco guard cells, and its interference with Rieske iron-sulfur protein, the PetC subunit of the cytochrome b6/f complex, fused with mCherry. In silico analysis predicted a possible physical interaction between BhDnaJC6 and Rieske iron-sulfur protein, which was experimentally confirmed using bimolecular fluorescence complementation (BiFC) and yeast two-hybrid assays. When overexpressed in cotton, the BhDnaJC6 transgenic lines displayed higher Rieske iron-sulfur protein levels and improved drought tolerance compared to the wild type. The higher levels of Rieske iron-sulfur protein improve photosynthetic performance in transgenic lines under both non-stressed and drought-stressed conditions, increasing the electron transport rates and actual quantum yields of PSII and decreasing the quantum yield of non-regulated energy dissipation. Taken together, our findings unveil a novel component enhancing Rieske iron-sulfur protein stability and improving the drought tolerance of transgenic cotton, offering a valuable genetic resource for drought-tolerant cotton breeding.

Sustainable plant-based protein hydrolysates: Utilization of waste proteins modified by enzymatic hydrolysis in techno-functional applications.

Comparative Analysis of Chloroplast Promoters for Optimized Production of Recombinant Proteins in Plants

Plant-based protein nanofibers: A comprehensive review of fabrication techniques, structural properties, and bifunctional applications.

Optimizing quality and palatability in texture-modified foods: A cross-framework study using sweet potato-based formulations.

Hofmeister and electrostatic modulation of the structure and polymorphism of rice protein fibrils.

Evolutionary and functional characterization of tea plant DELLA proteins.

Plant vs Dairy protein stabilised cappuccino foams: how protein and hydrocolloid conformational changes affect foam stability

Comparative characterization and interaction mechanism of zein-enhanced plant protein blends in a food model with soy, pea, chickpea, rice, and pumpkin seed proteins

Concentration-dependent ion-specific amyloid fibrillation of Phaseolus vulgaris protein for dysphagia-oriented hydrogels.

Plant proteins for human consumption – from local to global opportunities and challenges in a full value chain context

Effects of leguminous plant protein types and amounts on the digestibility of meat protein in emulsion-type sausage.

Dynamic regulation of mung bean globulin amyloid fibrillation by Gallic acid: Structural and functional insights.

Meat analogues: Role of plant protein functionality and processing strategies for quality enhancement