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Immunoassays are complementary diagnostic tools in human cystic echinococcosis (CE) despite sensitivity/specificity limitations, and synthetic peptides have been suggested to potentially overcome disadvantages reported for traditional antigens. Herein, a systematic study comparing the immunodiagnostic performance of AgB1 versus synthetic peptides derived from its sequence was carried out. Thus, a eukaryotic-expressed recombinant AgB1 was assessed, together with a reported synthetic peptide (p176, N-terminal portion of AgB1) and two new peptides within p176 (namely pB1a and pB1b) corresponding to predicted linear B-cell epitopes. Immunodiagnostic performances were evaluated by ELISA using a large collection of human sera from CE patients, healthy donors, and individuals with other parasitoses; assessing the sensitivity, specificity, indeterminacy, cross-reactivity, and diagnostic efficiency of the assay according to each antigen. Results suggest that peptides retaining most of the original protein sequence and 3D-structure display better overall diagnostic efficiencies (IgG values for rAgB1, p176, pB1a, and pB1b were 66.1%, 60.4%, 54.7%, and 49.0%, respectively), with a small N-terminal portion of AgB1 being immunodominant. Additionally, detection of specific IgG antibodies significantly reduced cross-reactivity, while improving sensitivity (IgG-IgG values for rAgB1, p176, and pB1a were 37.5%-42.7%, 24.0%-29.2%, and 11.5%-24.0%, respectively). Valuable information was obtained for rationally design novel peptide-based assays for CE immunodiagnosis.
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http://dx.doi.org/10.1080/15321819.2025.2556426 | DOI Listing |
Angew Chem Int Ed Engl
September 2025
Department of Biology and Chemistry, Paul Scherrer Institute, Forschungsstrasse 111, Villigen, PSI, 5232, Switzerland.
LL-37 and its variants with amphiphilic structure can modulate amyloid-β (Aβ) fibril formation, but the detailed mechanism behind it is still unclear. By using four different peptides (LL-37, LL-37, LL-37, LL-37), we found these peptides affect Aβ40 aggregation differently. Nanoscale analysis showed that all LL-37 peptides form hetero-oligomers and nanoclusters with Aβ40, but LL-37 and LL-37, which exhibit the strongest inhibition of Aβ fibrillation, form more hetero-oligomers and smaller nanoclusters.
View Article and Find Full Text PDFMicrob Pathog
September 2025
Central Research Laboratory and Molecular Diagnostics, School of Allied Health Sciences, Datta Meghe Institute of Higher Education and Research, Sawangi (Meghe), Postal code 442001, Wardha, Maharashtra, India.
Concerningly, multidrug-resistant bacteria have emerged as a prime worldwide trouble, obstructing the treatment of infectious diseases and causing doubts about the therapeutic accidentalness of presently existing drugs. Novel antimicrobial interventions deserve development as conventional antibiotics are incapable of keeping pace with bacteria evolution. Various promising approaches to combat MDR infections are discussed in this review.
View Article and Find Full Text PDFMol Biol Rep
September 2025
Department of Biotechnology, Daegu University, Gyeongsan, 38453, Republic of Korea.
Background: Bacterial pathogen-associated molecular patterns (PAMPs), specifically lipopolysaccharide (LPS) from Gram-negative bacteria (E. coli, P. aeruginosa) and lipoteichoic acid (LTA) from Gram-positive bacteria (S.
View Article and Find Full Text PDFJ Immunoassay Immunochem
September 2025
Área Inmunología, Departamento de Biociencias (DEPBIO), Facultad de Química, Universidad de la República, Montevideo, Uruguay.
Immunoassays are complementary diagnostic tools in human cystic echinococcosis (CE) despite sensitivity/specificity limitations, and synthetic peptides have been suggested to potentially overcome disadvantages reported for traditional antigens. Herein, a systematic study comparing the immunodiagnostic performance of AgB1 versus synthetic peptides derived from its sequence was carried out. Thus, a eukaryotic-expressed recombinant AgB1 was assessed, together with a reported synthetic peptide (p176, N-terminal portion of AgB1) and two new peptides within p176 (namely pB1a and pB1b) corresponding to predicted linear B-cell epitopes.
View Article and Find Full Text PDFScience
September 2025
RIKEN Center for Sustainable Resource Science, RIKEN-TRIP, Yokohama, Japan.
Plants deploy a diverse array of pattern recognition receptors (PRRs), which perceive microbe-associated molecular patterns to activate immune responses. Leucine-rich repeat receptor-like kinase subgroup XII (LRR-RLK-XII) represents one of the largest PRR families owing to lineage-specific diversification. Through bioinformatics and synthetic biology approaches, we characterized LRR-RLK-XIIs from 285 plant species and identified a receptor, "SCORE," that perceives cold shock protein (CSP) peptides.
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