Given their sessile nature, plants continuously face unfavorable conditions throughout their life cycle, including water scarcity, extreme temperatures and soil pollution. Among all, metal(loid)s are one of the main classes of contaminants worldwide, posing a serious threat to plant growth and development. When in excess, metals which include both essential and non‐essential elements, quickly become phytotoxic, inducing the occurrence of oxidative stress. In this way, in order to ensure food production and safety, attempts to enhance plant tolerance to metal(loid)s are urgently needed. Nitric oxide (NO) is recognized as a signaling molecule, highly involved in multiple physiological events, like the response of plants to abiotic stress. Thus, substantial efforts have been made to assess NO potential in alleviating metal‐induced oxidative stress in plants. In this review, an updated overview of NO‐mediated protection against metal toxicity is provided. After carefully reviewing NO biosynthetic pathways, focus was given to the interaction between NO and the redox homeostasis followed by photosynthetic performance of plants under metal excess.

As described in the literature, Solieria filiformis lectin (SfL) from the marine red alga S. filiformis was found to have antinociceptive and anti-inflammatory effects. In this study, we characterized two SfL variants, SfL-1 and SfL-2, with molecular mass of 27,552Da and 27,985Da, respectively. The primary structures of SfL-1 and SfL-2 consist of four tandem-repeat protein domains with 67 amino acids each. SfL-1 and -2 showed high similarity to OAAH-family lectins. 3D structure prediction revealed that SfL-1 and -2 are composed of two β-barrel-like domains formed by five antiparallel β-strands, which are connected by a short peptide linker. Furthermore, the mixture of isoforms (SfLs) showed anticancer effect against MCF-7 cells. Specifically, SfLs inhibited 50% of viability in MCF-7 cells after treatment at 125μg.mL, while the inhibition of Human Dermal Fibroblasts (HDF) was 34% with the same treatment. Finally, 24h after treatment, 25% of MCF-7 cells were in early apoptosis and 35% in late apoptosis. Evaluation of pro- and anti-apoptotic gene expression of MCF-7 cells revealed that SfLs induced caspase-dependent apoptosis within 24h.

The lectin DLasiL was isolated from seeds of the Dioclea lasiocarpa collected from the northeast coast of Brazil and characterized for the first time by mass spectrometry, DNA sequencing, inductively coupled plasma-mass spectrometry, electron paramagnetic resonance, and fluorescence spectroscopy. The structure of DLasiL lectin obtained by homology modelling suggested strong conservation of the dinuclear Ca/Mn and sugar-binding sites, and dependence of the solvent accessibility of tryptophan-88 on the oligomerisation state of the protein. DLasiL showed highly potent (low nanomolar) antiproliferative activity against several human carcinoma cell lines including A2780 (ovarian), A549 (lung), MCF-7 (breast) and PC3 (prostate), and was as, or more, potent than the lectins ConBr (Canavalia brasiliensis), ConM (Canavalia maritima) and DSclerL (Dioclea sclerocarpa) against A2780 and PC3 cells. Interestingly, DLasiL lectin caused a G2/M arrest in A2780 cells after 24h exposure, activating caspase 9 and delaying the on-set of apoptosis. Confocal microscopy showed that fluorescently-labelled DLasiL localized around the nuclei of A2780 cells at lectin doses of 0.5-2× IC and gave rise to enlarged nuclei and spreading of the cells at high doses. These data reveal the interesting antiproliferative activity of DLasiL lectin, and suggest that further investigations to explore the potential of DLasiL as a new anticancer agent are warranted.

A cowpea class I chitinase (VuChiI) was expressed in the methylotrophic yeast P. pastoris. The recombinant protein was secreted into the culture medium and purified by affinity chromatography on a chitin matrix. The purified chitinase migrated on SDS-polyacrylamide gel electrophoresis as two closely-related bands with apparent molecular masses of 34 and 37 kDa. The identity of these bands as VuChiI was demonstrated by mass spectrometry analysis of tryptic peptides and N-terminal amino acid sequencing. The recombinant chitinase was able to hydrolyze colloidal chitin but did not exhibit enzymatic activity toward synthetic substrates. The highest hydrolytic activity of the cowpea chitinase toward colloidal chitin was observed at pH 5.0. Furthermore, most VuChiI activity (approximately 92%) was retained after heating to 50 °C for 30 min, whereas treatment with 5 mM Cu caused a reduction of 67% in the enzyme's chitinolytic activity. The recombinant protein had antifungal activity as revealed by its ability to inhibit the spore germination and mycelial growth of Penicillium herquei. The three-dimensional structure of VuChiI was resolved at a resolution of 1.55 Å by molecular replacement. The refined model had 245 amino acid residues and 381 water molecules, and the final R-factor and R values were 14.78 and 17.22%, respectively. The catalytic domain of VuChiI adopts an α-helix-rich fold, stabilized by 3 disulfide bridges and possessing a wide catalytic cleft. Analysis of the crystallographic model and molecular docking calculations using chito-oligosaccharides provided evidences about the VuChiI residues involved in sugar binding and catalysis, and a possible mechanism of antifungal action is suggested.

Agricultural soil degradation is occurring at unprecedented rates, not only as an indirect effect of climate change (CC) but also due to intensified agricultural practices which affect soil properties and biodiversity. Therefore, understanding the impacts of CC and soil degradation on plant physiology is crucial for the sustainable development of mitigation strategies to prevent crop productivity losses. The amino acid proline has long been recognized for playing distinct roles in plant cells undergoing osmotic stress. Due to its osmoprotectant and redox-buffering ability, a positive correlation between proline accumulation and plants’ tolerance to abiotic stress has been pointed out in numerous reviews. Indeed, proline quantification is used systematically by plant physiologists as an indicator of the degree of tolerance and a measurement of the antioxidant potential in plants under stressful conditions. Moreover, the exogenous application of proline has been shown to increase resilience to several stress factors, including those related to soil degradation such as salinity and exposure to metals and xenobiotics. However, recent data from several studies often refer to proline accumulation as a signal of stress sensitivity with no clear correlation with improved antioxidant activity or higher stress tolerance, including when proline is used exogenously as a stress reliever. Nevertheless, endogenous proline levels are strongly modified by these stresses, proving its involvement in plant responses. Hence, one main question arises—is proline augmentation always a sign of improved stress resilience? From this perspective, the present review aims to provide a more comprehensive understanding of the implications of proline accumulation in plants under abiotic stress induced by soil degradation factors, reinforcing the idea that proline quantification should not be employed as a sole indicator of stress sensitivity or resilience but rather complemented with further biochemical and physiological endpoints.