Journal: Frontiers in Plant Science

Article Title: Metabolic engineering strategies for optimized lignan production in plants

doi: 10.3389/fpls.2026.1827862

Figure Lengend Snippet: Integrated overview of lignan biosynthesis and “Push-Pull-Release” strategies for plant lignan metabolic engineering. (A) Overview of the phenylpropanoid pathway leading to flavonoids, lignin, and lignan precursors. Sequential enzymatic conversions start from L-phenylalanine and branch into flavonoid biosynthesis and monolignol production for lignin monomer (H-, G-, and S-lignin). The principal enzymes and end products depicted are as follows: PAL, phenylalanine ammonia-lyase; C4H, cinnamate 4-hydroxylase; 4CL, 4-coumarate:CoA ligase; CHS, chalcone synthase; HCT, hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyl transferase; C3’H, p -coumaroyl shikimate 3’-hydroxylase; CSE, caffeoyl shikimate esterase; C3H, coumarate 3-hydroxylase; COMT, caffeic acid O-methyltransferase; F5H, ferulate 5-hydroxylase; CCoA-OMT, caffeoyl-CoA O-methyltransferase; CCR, cinnamoyl-CoA reductase; CAD, cinnamyl alcohol dehydrogenase; LAC, laccase; PRX, peroxidase; H-lignin, hydroxyphenyl-lignin; G-lignin, guaiacyl lignin; S-lignin, syringyl-lignin. The pathway also highlights interconnections leading to lignan biosynthesis. Enzyme names are shown at each reaction step, and the main product classes are indicated at pathway termini. (B) Chemical structures of monolignol precursor (coniferyl alcohol) and representative lignans derived from phenylpropanoid pathway. (C) Biosynthetic pathway from coniferyl alcohol to sesamin and podophyllotoxin derivatives. This panel illustrates the enzymatic conversion steps starting from coniferyl alcohol as the precursor of lignan biosynthesis. Key enzymes and their full names are as follows: DIR, dirigent protein; PLR, pinoresinol-lariciresinol reductase; SDH, secoisolariciresinol dehydrogenase; CYP81Q1, (+)-piperitol/(+)-sesamin synthase; CYP719A23, (–)-pluviatolide synthase; OMT3, (–)-pluviatolide-O-methyltransferase; CYP71CU1, (–)-5’-desmethoxy-yatein hydroxylase; OMT1, (–)-5’-desmethyl-yatein O-methyltransferase; 2-ODD, 2-oxoglutarate/Fe(II)-dependent dioxygenase; CYP82D61, (–)-deoxypodophyllotoxin 4-hydroxylase; CYP71BE54, (–)-4’-desmethyl-deoxypodophyllotoxin hydroxylase. Each step highlights the enzyme responsible for the specific biochemical reaction ( Gasper et al., 2016 ; ; Yao et al., 2021 ). (D) Schematic representation of the “Push-Pull-Release” framework for lignan metabolic engineering. “Push” promotes precursor supply, “Pull” redirects flux by blocking competing pathways, and “Release” removes negative regulators to relieve pathway repression. These strategies are linked with synthetic biology tools for modular assembly, multiplex CRISPR, and spatiotemporal control to support lignan production and plant fitness (See Table 1 for a comparative overview of major engineering strategies and their risks and considerations).

Article Snippet: Caffeoyl-CoA O-methyltransferase ( CCoA-OMT ) downregulation in alfalfa ( Medicago sativa ) redirected flux toward the isoflavonoid pathway, thereby improving resistance to F. oxysporum ( ).

Techniques: Derivative Assay, Blocking Assay, Multiplex Assay, CRISPR, Control

Journal: Food Chemistry: Molecular Sciences

Article Title: Proteomic and in silico identification of potential allergenic proteins in cowpea ( Vigna unguiculata L. Walp) seeds

doi: 10.1016/j.fochms.2026.100360

Figure Lengend Snippet: Multiple regions of potential T-cell allergenic epitopes in endochitinase, endochitinase 1B and 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB). Sequence alignment was performed using Clustal Omega (EMBL-EBI). See full region alignment in , . Multiple regions of potential T-cell allergenic epitopes in endochitinase, endochitinase 1B and 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB). Sequence alignment was performed using Clustal Omega (EMBL-EBI). See full region alignment in Supplementary Fig. S2 and S3.

Article Snippet: Supplementary Figure S2 Supplementary Figure S3 Full region alignment depicts multiple regions of potential T-cell allergenic epitopes in 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB).

Techniques: Sequencing

Journal: Food Chemistry: Molecular Sciences

Article Title: Proteomic and in silico identification of potential allergenic proteins in cowpea ( Vigna unguiculata L. Walp) seeds

doi: 10.1016/j.fochms.2026.100360

Figure Lengend Snippet: B-cell epitope prediction of endochitinase 1B and 5-methyltetrahydropteroyltriglutamate–homocysteine methyltransferase (MetE). Panel A and B represent protein structure of endochitinase 1B and MetE, respectively, predicted by AlphaFold database. The B-cell epitope regions predicted by the Kolaskar & Tongaonkar (KT) algorithm within IEDB are indicated by the dashed red lines and yellow highlight in protein structures. The KT antigenicity maps of endochitinase 1B and MetE are displayed in panels C and D, respectively. The residues in yellow regions indicate potential antigenic areas. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

Article Snippet: Supplementary Figure S2 Supplementary Figure S3 Full region alignment depicts multiple regions of potential T-cell allergenic epitopes in 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB).

Techniques:

Journal: Food Chemistry: Molecular Sciences

Article Title: Proteomic and in silico identification of potential allergenic proteins in cowpea ( Vigna unguiculata L. Walp) seeds

doi: 10.1016/j.fochms.2026.100360

Figure Lengend Snippet: Full region alignment depicts multiple regions of potential T-cell allergenic epitopes in 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB). Sequence alignment was performed using Clustal Omega (EMBL-EBI).

Article Snippet: Supplementary Figure S2 Supplementary Figure S3 Full region alignment depicts multiple regions of potential T-cell allergenic epitopes in 5-methyltetrahydropteroyltriglutamate—homocysteine methyltransferase (MetE) predicted by Immune Epitope Database (IEDB).

Techniques: Sequencing

Journal: Oncology Letters

Article Title: RNA methyltransferase NSUN2 enhances vasculogenic mimicry and malignant progression of cervical cancer through upregulation of MMP-9

doi: 10.3892/ol.2026.15518

Figure Lengend Snippet: m 5 C RNA methyltransferase NUSN2 is significantly upregulated in CC and its gene expression is associated with poor prognosis. (A) The level of m 5 C modification of RNA in CC cells was analyzed using a dot blot assay. Methylene blue staining served as an internal reference. (B) Semi-quantitative analysis of dot blot results in HeLa cells. (C) Semi-quantitative analysis of dot blot results in SiHa cells. (D) Expression levels of genes encoding m 5 C methyltransferases was analyzed within a CC database of TCGA. (E) HeLa and SiHa cells were incubated under hypoxia (0.1% O 2 ) and proteins collected at 24, 48 and 72 h were analyzed for NSUN2, TRDMT1 and GAPDH by western blotting. ImageJ was used to quantify western blotting signals from (F) HeLa and (G) SiHa cells. GAPDH served as an internal reference. (H) mRNA expression level of NSUN2 in 44 pairs of CC and paracancerous tissues were quantified using RT-qPCR. Gene expression in cancer tissues is expressed compared with expression in normal tissues. (I) Comparison of the average expression level of NSUN2 mRNA in CC tissues compared with paracancerous tissues. (J) Panoramic scans after IHC detection of NSUN2 and H&E staining in CC and paracancerous tissues. Scale bar, 50 µm. Magnification, ×20. (K) Protein levels of NSUN2 in 20 paired CC and paracancerous tissues, with the NSUN2 level in CC tissue expressed compared with that in the paired normal tissue. (L) Level of NSUN2 expression in CC was associated with a poor prognosis in the form of biochemical progression-free survival (P=0.018; log-rank test). *P<0.05, **P<0.01 and ***P<0.001. MMP9, matrix metalloproteinase 9; VM, vasculogenic mimicry; CC, cervical cancer; IHC, immunohistochemistry; NSUN2, NOP2/Sun RNA methyltransferase 2; m 5 C, 5-methylcytidine; TRDMT1, transfer RNA aspartic acid methyltransferase 1; TCGA, The Cancer Genome Atlas; RT-qPCR, reverse transcription-quantitative PCR; IHC, immunohistochemistry.

Article Snippet: The membranes were blocked with 5% milk at 20±5°C for 1 h. The blocked membranes were incubated at 4°C overnight with the following antibodies: A rabbit monoclonal anti-NSUN2 antibody (1:1,000; cat. no. AB259941; Abcam), a rabbit monoclonal anti-transfer RNA aspartic acid methyltransferase 1 (TRDMT1) antibody (1:1,000; cat. no. 19221-1-AP; Proteintech Group, Inc.; Wuhan Sanying Biotechnology), a rabbit polyclonal anti-MMP-9 antibody (1:1,000; cat. no. 10375-2-AP; Proteintech Group, Inc.; Wuhan Sanying Biotechnology), a rabbit polyclonal anti-aldehyde dehydrogenase 1 (ALDH1) antibody (1:1,000; cat. no. 15910-1-AP; Proteintech Group, Inc.; Wuhan Sanying Biotechnology), a rabbit polyclonal anti-ephrin type-A receptor 2 (EPHA2) antibody (1:1,000; cat. no. AF5 238; Affinity Biosciences) and a rabbit polyclonal anti-GAPDH antibody (1:1,000; TA309157 OriGene Technologies, Inc.).

Techniques: Gene Expression, Modification, Dot Blot, Staining, Quantitative Dot Blot, Expressing, Incubation, Western Blot, Quantitative RT-PCR, Comparison, Immunohistochemistry, Reverse Transcription, Real-time Polymerase Chain Reaction