Background: Sri Lankan cassava mosaic virus (SLCMV) is a plant virus causing significant economic losses throughout Southeast Asia. While proteomics has the potential to identify molecular markers that could assist the breeding of virus resistant cultivars, the effects of SLCMV infection in cassava have not been previously explored in detail. Results: Liquid Chromatography-Tandem Mass Spectrometry (LC/MS–MS) was used to identify differentially expressed proteins in SLCMV infected leaves, and qPCR was used to confirm changes at mRNA levels. LC/MS–MS identified 1,813 proteins, including 479 and 408 proteins that were upregulated in SLCMV-infected and healthy cassava plants respectively, while 109 proteins were detected in both samples. Most of the identified proteins were involved in biosynthetic processes (29.8%), cellular processes (20.9%), and metabolism (18.4%). Transport proteins, stress response molecules, and proteins involved in signal transduction, plant defense responses, photosynthesis, and cellular respiration, although present, only represented a relatively small subset of the detected differences. RT-qPCR confirmed the upregulation of WRKY 77 (A0A140H8T1), WRKY 83 (A0A140H8T7), NAC 6 (A0A0M4G3M4), NAC 35 (A0A0M5JAB4), NAC 22 (A0A0M5J8Q6), NAC 54 (A0A0M4FSG8), NAC 70 (A0A0M4FEU9), MYB (A0A2C9VER9 and A0A2C9VME6), bHLH (A0A2C9UNL9 and A0A2C9WBZ1) transcription factors. Additional upregulated transcripts included receptors, such as receptor-like serine/threonine-protein kinase (RSTK) (A0A2C9UPE4), Toll/interleukin-1 receptor (TIR) (A0A2C9V5Q3), leucine rich repeat N-terminal domain (LRRNT_2) (A0A2C9VHG8), and cupin (A0A199UBY6). These molecules participate in innate immunity, plant defense mechanisms, and responses to biotic stress and to phytohormones. Conclusions: We detected 1,813 differentially expressed proteins infected cassava plants, of which 479 were selectively upregulated. These could be classified into three main biological functional groups, with roles in gene regulation, plant defense mechanisms, and stress responses. These results will help identify key proteins affected by SLCMV infection in cassava plants.

Cassava mosaic disease (CMD) is a major disease affecting cassava production in Southeast Asia. This study aimed to perform an integrated proteomics and metabolomics analysis of cassava cv. Kasetsart 50 infected with Sri Lankan cassava mosaic virus (SLCMV). Proteomics analyses revealed that 359 proteins were enriched in the plant–pathogen interaction, plant hormone signal transduction, and MAPK signaling pathways. A total of 79 compounds were identified by metabolomics analysis of the healthy and SLCMV-infected cassava plants. Integrated omics analysis revealed that 9 proteins and 5 metabolites were enriched in 11 KEGG pathways. The metabolic pathways, plant hormone signal transduction, and plant–pathogen interaction pathway terms were specifically investigated. The findings revealed that caffeic acid and chlorogenic acid were associated with the plant–pathogen interaction pathway, histidine (HK3) was involved in plant hormone signal transduction, while citric acid and D-serine were associated with the metabolic pathways. KEGG functional enrichment analysis revealed that plant–pathogen interaction, plant hormone signal transduction, and metabolic pathways were linked via the enriched protein (protein phosphatase 2C) and metabolites (cyclic nucleotide-binding (AT2G20050) and D-serine). The available information and resources for proteomics and metabolomics analyses of cassava can elucidate the mechanism of disease resistance and aid in cassava crop improvement programs.

The overuse and inappropriate use of antibiotics have led to the emergence of several antibiotic resistant bacteria. As a result, there is growing interest in exploring alternative agents as antimicrobial peptides (AMPs), which operate through unique mechanisms to effectively counteract bacterial resistance. In this study, peptides smaller than 3 kDa were isolated by cation exchange chromatography, anion exchange chromatography and reverse-phase chromatography. Subsequently, 12 candidate peptides were selected and chemically synthesized for a comparative study of growth inhibition in pathogenic bacteria. They demonstrated potent antibacterial activity toward A. baumannii, S. epidermidis, S. aureus, and S. enterica. Exposure to the Cur-1 peptide induced changes in bacterial proteins associated with metabolite interconversion and translation. In addition, all peptides derived from turmeric peptic hydrolysate exhibited antioxidant activity as assessed by ABTS, DPPH and FRAP assays. Cur-1 peptide displayed both high antibacterial and antioxidant potential, positioning it as a promising natural option for antibacterial management and applications within food industry.

Nonedible materials such as agricultural wastes can serve as sources of antimicrobial peptides (AMPs) effective against bacterial plant pathogens. In this study, thirteen agricultural samples were collected and their protein hydrolysates obtained using pepsin. Peptides smaller than 3 kDa were purified by reverse-phase chromatography, cation exchange chromatography, and pI-based fractionation and tested for activity against plant pathogenic bacteria at each step. Active peptides were then analyzed for putative mechanisms using nanoLC–MS/MS and the Mascot program. Ultimately, eight candidate peptides originating from bagasse were selected and chemically synthesized for a comparative study of growth inhibition in plant pathogenic bacteria and plant growth-promoting rhizobacteria (PGPRs). Three synthesized peptides exhibited a potent activity against plant pathogenic bacteria while also supporting the growth of PGPRs. Proteomics analysis revealed the peptides PQLAVF (Pro-Gln-Leu-Ala-Val-Phe) and MDRFL (Met-Asp-Arg-Phe-Leu) to act against Xanthomonas oryzae pv. oryzae via membrane-active mechanisms, while peptide VQLMNSL (Val-Gln-Leu-Met-Asn-Ser-Leu) acted against Pectobacterium carotovorum and Agrobacterium rhizogenes through intracellular-active mechanisms. Further study remains necessary to customize peptides by amino acid substitution not only for a higher effective activity against these and other critical pathogens, but also for a higher stability of peptides in critical condition when applied in industrial processes in the future.

Due to its excellent biocompatibility and ease of biodegradation, jellyfish gelatin has gained attention as a hydrogel. However, hydrogel produced from jellyfish gelatin has not yet been sufficiently characterized. Therefore, this research aims to produce a jellyfish gelatin-based hydrogel. The gelatin produced from desalted jellyfish by-products varied with the part of the specimen and extraction time. Hydrogels with gelatin: glutaraldehyde ratios of 10:0.25, 10:0.50, and 10:1.00 (v/v) were characterized, and their cefazolin release ability was determined. The optimal conditions for gelatin extraction and chosen for the development of jellyfish hydrogels (JGel) included the use of the umbrella part of desalted jellyfish by-products extracted for 24 h (WU24), which yielded the highest gel strength (460.02 g), viscosity (24.45 cP), gelling temperature (12.70 °C), and melting temperature (22.48 °C). The quantities of collagen alpha−1(XXVIII) chain A, collagen alpha−1(XXI) chain, and collagen alpha−2(IX) chain in WU24 may influence its gel properties. Increasing the glutaraldehyde content in JGel increased the gel fraction by decreasing the space between the protein chains and gel swelling, as glutaraldehyde binds with lateral amino acid residues and produces a stronger network. At 8 h, more than 80% of the cefazolin in JGel (10:0.25) was released, which was higher than that released from bovine hydrogel (52.81%) and fish hydrogel (54.04%). This research is the first report focused on the production of JGel using glutaraldehyde as a cross-linking agent.

Urinary extracellular vesicles (uEVs) reflect the biological conditions of the producing cells. The protein profiling of uEVs allow us to better understand cancer progression in several cancers such as bladder cancer, prostate cancer and kidney cancer but has not been reported in breast cancer. We have, herein, aimed at quantifying the concentration and at generating the proteomic profile of uEVs in patients with breast cancer (BC) as compared to that of healthy controls (CT). Urine samples were collected from 29 CT and 47 patients with BC. uEVs were isolated by using differential ultracentrifugation, and were then characterized by Western blotting and transmission electron microscopy. Moreover, a nanoparticle tracking analysis was used in order to measure the concentration and the size distribution of urine particles and uEVs. The proteomic profiling of the uEVs was facilitated through LC-MS/MS. The uEV concentration was not significantly different between the assessed groups. The undertaken proteomic analysis revealed 15,473 and 11,278 proteins in the BC patients’ group and the CT group, respectively. Furthermore, a heat map analysis revealed a differential protein expression, while a principal component analysis highlighted two clusters. The volcano plot indicated 259 differentially expressed proteins (DEPs; 155 up- and 104 down-regulated proteins) in patients with BC compared with CT. The up-regulated proteins from BC-derived uEVs were enriched in pathways related to cancer progression (i.e., cell proliferation, cell survival, cell cycle, cell migration, carbohydrate metabolism, and angiogenesis). Moreover, we verified the expression of the upregulated DEPs using UALCAN for web-based validation. Remarkably, the results indicated that 6 of 155 up-regulated proteins (POSTN, ATAD2, BCAS4, GSK3β, HK1, and Ki-67) were overexpressed in BC compared with normal samples. Since these six proteins often act as markers of cell proliferation and progression, they may be potential biomarkers for BC screening and diagnosis. However, this requires validation in larger cohorts.