Diagnosis of previous C. jejuni infections in GBS patients are mostly based on serological findings. However, there are not consensus what kind of antigen should be used in the serological assays. In our study we used ELISA with four different antigen preparations for investigation of specific antibodies to C. jejuni in serum samples obtained from 6 children with GBS. In all patients the high level of IgA and IgG antibodies to LPS were diagnosed. The antibodies in particular classes of immunoglobulins to recombinant proteins (Mikrogen), termostabile antigen and whole-cell antigen (Virion/Serion) of C. jejuni were diagnosed only in some of the children with GBS. However, in comparison to the control groups, the ELISA with recombinant proteins was most specific. Moreover, in two of the patients a characteristic decline of the level of antibodies to recombinant proteins in sera obtained in acute and chronic phase of disease have been observed. The results of this study showed that serodiagnosis, specially based on recombinant antigens, may be a reliable marker of recent or previous infection caused by C. jejuni in patients with GBS.
Download full-text PDF |
Source |
---|
Microb Biotechnol
January 2025
Institute of Bio- and Geosciences, IBG-1: Biotechnology, Forschungszentrum Jülich GmbH, Jülich, Germany.
Glucose is the most abundant monosaccharide and a principal substrate in biotechnological production processes. In Pseudomonas, this sugar is either imported directly into the cytosol or first oxidised to gluconate in the periplasm. While gluconate is taken up via a proton-driven symporter, the import of glucose is mediated by an ABC-type transporter, and hence both require energy.
View Article and Find Full Text PDFSci Rep
January 2025
Johnson & Johnson, Therapeutics Discovery, Spring House, PA, USA.
Solution-based affinity assays are used for the selection and characterization of proteins that could be developed into therapeutic molecules. However, these assays have limitations for cell-surface proteins as in most cases their purification requires detergent solubilization and are unlikely to assume conformations in solution that resemble their native states in cell membranes. This report describes a novel electrochemiluminescence-based method, called MSD-CAT, for the affinity analysis of antibodies binding to cell-surface receptors.
View Article and Find Full Text PDFSignal Transduct Target Ther
January 2025
Laboratory of Aging Research and Cancer Drug Target, State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, No. 17, Block 3, Southern Renmin Road, Chengdu, Sichuan, 610041, People's Republic of China.
The newly emerged variants of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) demonstrate resistance to present therapeutic antibodies as well as the capability to evade vaccination-elicited antibodies. JN.1 sublineages were demonstrated as one of the most immune-evasive variants, showing higher neutralization resistance compared to XBB.
View Article and Find Full Text PDFPLoS Pathog
January 2025
Department of Microbiology, Faculty of Science, University of Manitoba, Winnipeg, Manitoba, Canada.
RNA viruses have evolved numerous strategies to overcome host resistance and immunity, including the use of multifunctional proteases that not only cleave viral polyproteins during virus replication but also deubiquitinate cellular proteins to suppress ubiquitin (Ub)-mediated antiviral mechanisms. Here, we report an approach to attenuate the infection of Arabidopsis thaliana by Turnip Yellow Mosaic Virus (TYMV) by suppressing the polyprotein cleavage and deubiquitination activities of the TYMV protease (PRO). Performing selections using a library of phage-displayed Ub variants (UbVs) for binding to recombinant PRO yielded several UbVs that bound the viral protease with nanomolar affinities and blocked its function.
View Article and Find Full Text PDFJ Phys Chem Lett
January 2025
State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.
The Ni-N(His) coordination bond, formed between the nickel ion and histidine residues, is essential for recombinant protein purification, especially in Ni-NTA-based systems for selectively binding polyhistidine-tagged (Histag) proteins. While previous studies have explored its bond strength in a synthetic Ni-NTA-Histag system, the influence of the surrounding protein structure remains less understood. In this study, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to quantify the Ni-N(His) bond strength in calprotectin, a biologically relevant protein system.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!