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Among the antimicrobial molecules produced by epithelial cells, DEFB4 is inducible in response to proinflammatory signals such as cytokines and bacterial molecules. Nontypeable Haemophilus influenzae (NTHi) is an important human pathogen that exacerbates chronic obstructive pulmonary disease in adult and causes otitis media and sinusitis in children. Previously, we have demonstrated that DEFB4 effectively kills NTHi and is induced by NTHi via TLR2 signaling. The 5'-flanking region of DEFB4 contains several NF-κB binding motifs, but their NTHi-specific activity remains unclear. In this study, we aimed to elucidate molecular mechanism involved in DEFB4 regulation, focusing on the role of the distal NF-κB binding motif of DEFB4 responding to NTHi. Here, we show that the human middle ear epithelial cells up-regulate DEFB4 expression in response to NTHi via NF-κB activation mediated by IκKα/β-IκBα signaling. Deletion of the distal NF-κB binding motif led to a significant reduction in NTHi-induced DEFB4 up-regulation. A heterologous construct containing the distal NF-κB binding motif was found to increase the promoter activity in response to NTHi, indicating a NTHi-responding enhancer activity of the distal NF-κB binding motif. Furthermore, electrophoretic mobility shift assays and chromatin immunoprecipitation assays showed that the p65 domain of NF-κB binds to the distal NF-κB binding motif in response to NTHi. Taken together, our results suggest that NTHi-induced binding of p65 NF-κB to the distal NF-κB binding motif of DEFB4 enhances NTHi-induced DEFB4 regulation in epithelial cells.
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http://dx.doi.org/10.1016/j.bbrc.2013.12.091 | DOI Listing |
Biotechnol Lett
September 2025
Department of Chemical Engineering, Hongik University, Sangsu-dong, Mapo-gu, Seoul, 04066, Republic of Korea.
The cell surface display system employs carrier proteins to present target proteins on the outer membrane of cells. This system enables functional proteins to be exposed on the exterior of living cells without cell lysis, allowing direct interaction with the surrounding environment. A major limitation of conventional approaches is the difficulty in displaying large-sized enzymes or antibodies, despite their critical roles in applications requiring functional domains that must remain intact, such as catalytic or antigen-binding sites.
View Article and Find Full Text PDFOpen Biol
September 2025
National Brain Research Centre, Manesar, Haryana, India.
E3 ubiquitin ligases regulate the cellular proteome proteasome-dependent protein degradation; however, there exist limited studies outlining their non-canonical functions. RNA-binding ubiquitin ligases (RBULs) represent a subset of E3 ligases that harbour RNA-binding domains, making them uniquely positioned to function as both RNA-binding proteins and E3 ligases. Our initial microarray screen for E3 ligases from mouse cortical neural progenitor cells identified MEX3B, a known RNA-binding ubiquitin ligase, to be differentially expressed.
View Article and Find Full Text PDFAm J Hum Genet
September 2025
Department of Clinical Genetics, Erasmus MC, University Medical Center Rotterdam, PO Box 2040, Rotterdam 3000 CA, the Netherlands.
Microtubule-actin cross-linking factor 1 (MACF1) is a large protein of the spectraplakin family, which is essential for brain development. MACF1 interacts with microtubules through the growth arrest-specific 2 (Gas2)-related (GAR) domain. Heterozygous MACF1 missense variants affecting the zinc-binding residues in this domain result in a distinctive cortical and brain stem malformation.
View Article and Find Full Text PDFMol Pharmacol
August 2025
Institute of Pharmacology and Toxicology, Faculty of Veterinary Medicine, Biomedical Research Center Seltersberg, Justus Liebig University of Giessen, Giessen, Germany. Electronic address:
The myristoylated preS1 domain (myr-preS1) of the hepatitis B virus (HBV) large surface protein is essential for binding to the receptor protein, Na/taurocholate co-transporting polypeptide (NTCP), and for the subsequent internalization of the virus-receptor complex. NTCP, which is expressed in hepatocytes, plays a physiological role in hepatic bile acid transport. Recent cryo-electron microscopy structures of the myr-preS1-NTCP complex were used to analyze virus-receptor interactions at the molecular level.
View Article and Find Full Text PDFCarbohydr Res
September 2025
Laboratory for Biochemistry & Glycobiology, Ghent University, Department of Biotechnology, Ghent, Belgium. Electronic address:
Lectins are carbohydrate-binding proteins which play key roles in various biological processes, including cell signaling, pathogen recognition and development. Previous research conducted on ricin-B lectin domains and carbohydrate-binding modules of family 13 (CBM13) illustrated the striking resemblances between these two groups of protein domains. In this study, we report on the discovery, identification and putative biochemical characteristics of a ricin-B-like domain that is unique for GH27 enzymes from land plants, identified in the OsAPSE enzyme from Japanese rice (Oryza sativa L.
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