Currently, the detection of pathogens such as through instrumental alternatives with fast response and excellent sensitivity and selectivity are being studied. Biosensors are systems consisting of nanomaterials and biomolecules that exhibit remarkable properties such as simplicity, portable, affordable, user‑friendly, and deliverable to end‑users. For this, in this work we report for the first time, to our knowledge, the bioinformatic design of a new peptide based on TIR protein, a receptor of Intimin membrane protein which is characteristic of . This peptide (named PEPTIR‑1.0) was used as recognition element in a biosensor based on AuNPs‑modified screen‑printed electrodes for the detection of . The morphological and electrochemical characteristics of the biosensor obtained were studied. Results show that the biosensor can detect the bacteria with limits of detection and quantification of 2 and 6 CFU/mL, respectively. Moreover, the selectivity of the system is statistically significant towards the detection of the pathogen in the presence of other microorganisms such as and . This makes this new PEPTIR‑1.0 based biosensor can be used in the rapid, sensitive, and selective detection of in aqueous matrices.
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http://dx.doi.org/10.3390/molecules26092559 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, QLD 4072, Australia.
Innate immunity relies on Toll-like receptors (TLRs) to detect pathogen-associated molecular patterns. The TIR (Toll/interleukin-1 receptor) domain-containing TLR adaptors TRIF (TIR domain-containing adaptor-inducing interferon-β) and TRAM (TRIF-related adaptor molecule) are essential for MyD88-independent TLR signaling. However, the structural basis of TRIF and TRAM TIR domain-based signaling remains unclear.
View Article and Find Full Text PDFSci Rep
December 2024
Division of Genetics, Indian Agricultural Research Institute, New Delhi, 110012, India.
The mungbean yellow mosaic India virus (MYMIV, Begomovirus vignaradiataindiaense) causes Yellow Mosaic Disease (YMD) in mungbean (Vigna radiata L.). The biochemical assays including total phenol content (TPC), total flavonoid content (TFC), ascorbic acid (AA), DPPH (2,2-diphenyl-1-picrylhydrazyl), and FRAP (Ferric Reducing Antioxidant Power) were used to study the mungbean plants defense response to MYMIV infection.
View Article and Find Full Text PDFComp Biochem Physiol B Biochem Mol Biol
December 2024
State Key Laboratory of Mariculture Breeding, Fisheries College, Jimei University, Xiamen 361021, China. Electronic address:
Toll-like receptor 5 (TLR5) plays a crucial role in the immune response through recognizing bacterial flagellin. Some teleosts possess two forms of TLR5, including a canonical membrane TLR5 (TLR5M) ortholog and a piscine soluble TLR5 (TLR5S). In this report, the full-length cDNA sequences of Larimichthys crocea TLR5M (LcTLR5M) and TLR5S (LcTLR5S) were identified.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
College of Fisheries and Life Science, Dalian Ocean University, Dalian 116023, China; Engineering Research Center of Shellfish Culture and Breeding in Liaoning Province, Dalian 116023, China. Electronic address:
Toll-like receptor 4 (TLR4) is a pattern recognition receptor that activates innate immunity in response to pathogen infection. However, the role of TLR4 in pathogen-induced apoptosis and host immunity in mollusks remains largely unknown. In this study, the TLR4 of the Manila clam Ruditapes philippinarum (RpTLR4) was cloned.
View Article and Find Full Text PDFPlant Mol Biol
December 2024
State Key Laboratory of Cotton Biology, Zhengzhou Research Base, Zhengzhou University, Zhengzhou, 450001, China.
In the past decades, cyclic nucleotide-gated ion channels (CNGCs) have been extensively studied in diploid species Arabidopsis thaliana. However, the functional diversification of CNGCs in crop plants, mostly polyploid, remains poorly understood. In allotetraploid Upland cotton (Gossypium hirsutum), GhCNGC31 is one of the multiple orthologs of AtCNGC2, being present in the plasma membrane, capable of interacting with itself and binding to calmodulins and cyclic nucleotides.
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