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Int. J. Mol. Sci. 2021, 22(6), 3020; https://doi.org/10.3390/ijms22063020 Abstract A detailed workflow to analyze the physicochemical characteristics of mammalian matrix metalloproteinase (MMP-9) protein species obtained from protein aggregates (inclusion bodies—IBs) was followed. MMP-9 was recombinantly produced in the prokaryotic microbial cell factories Clearcoli (an engineered form of Escherichia coli) and Lactococcus lactis, mainly forming part of IBs and partially recovered under non-denaturing conditions. After the purification by affinity chromatography of solubilized MMP-9, four protein peaks were obtained. However, so far, the different conformational protein species forming part of IBs have not been isolated and characterized. Therefore, with the aim to li

Journal of Extracellular Vesicles  Volume 10, Issue 5 e12058 https://onlinelibrary.wiley.com/doi/10.1002/jev2.12058 Abstract In the present study the use of extracellular vesicles (EVs) as vehicles for therapeutic enzymes in lysosomal storage disorders was explored. EVs were isolated from mammalian cells overexpressing alpha‐galactosidase A (GLA) or N‐sulfoglucosamine sulfohydrolase (SGSH) enzymes, defective in Fabry and Sanfilippo A diseases, respectively. Direct purification of EVs from cell supernatants was found to be a simple and efficient method to obtain highly active GLA and SGSH proteins, even after EV lyophilization. Likewise, EVs carrying GLA (EV‐GLA) were rapidly uptaken and reached the lysosomes in cellular models of Fabry disease, restoring lysosomal function

Nucleic Acids Research, gkab150, https://doi.org/10.1093/nar/gkab150 Abstract LuxR is a TetR family master quorum sensing (QS) regulator activating or repressing expression of hundreds of genes that control collective behaviors in Vibrios with underlying mechanism unknown. To illuminate how this regulator controls expression of various target genes, we applied ChIP-seq and DNase I-seq technologies. Vibrio alginolyticus LuxR controls expression of ∼280 genes that contain either symmetric palindrome (repDNA) or asymmetric (actDNA) binding motifs with different binding profiles. The median number of LuxR binding sites for activated genes are nearly double for that of repressed genes. Crystal structures of LuxR in complex with the respective repDNA and actDNA motifs revealed a new

En un artículo publicado hoy en la revista Proceedings of the National Academy of Sciences of the United States of America (PNAS) investigadores del IRTA-Instituto de Biotecnología y Biomedicina (IBB), en la Universidad Autónoma de Barcelona (UAB), del Consejo Superior de Investigaciones Científicas (CSIC) y de la Universidad de Bergen e Instituto de Investigación Marina de Noruega, presentan el descubrimiento y evolución de una nueva vía intracelular de defensa al estrés osmótico que se activa en los espermatozoides de peces cuando se liberan al medio acuático. Este mecanismo consiste en el rápido transporte de un canal molecular de agua (acuaporina) a la mitocondria de los espermatozoides, donde actúa como un canal de salida del peróxido de hidrógeno (H2O2), peroxiporina, durante

Carratalá et al. Microb Cell Fact (2021) 20:30 https://doi.org/10.1186/s12934-021-01524-3 Abstract Background: Protein aggregation is a biological event observed in expression systems in which the recombinant protein is produced under stressful conditions surpassing the homeostasis of the protein quality control system. In addition, protein aggregation is also related to conformational diseases in animals as transmissible prion diseases or non-transmissible neurodegenerative diseases including Alzheimer, Parkinson’s disease, amyloidosis and multiple system atrophy among others. At the molecular level, the presence of aggregation-prone domains in protein molecules act as seeding igniters to induce the accumulation of protein molecules in protease-resistant clusters by inter