Publications by authors named "A Jungbauer"
Article Synopsis
- Highly purified virus preparations are crucial for determining the activity and potency of viruses, necessitating simple and efficient purification methods in early research phases.* -
- The study focused on using heparin affinity chromatography for purifying a sensitive strain of the measles virus, achieving high capture rates of infectious virus while experimenting with endonuclease treatments to reduce DNA impurities.* -
- The combination of Capto™ Heparin with M-SAN endonuclease resulted in a notable yield of 62% purity and significantly lower DNA contamination, suggesting this method is suitable for measles virus production in a scalable manufacturing process.*
Current influenza virus vaccines poorly display key neuraminidase (NA) epitopes and do not robustly induce NA-reactive antibodies; instead, they focus on the induction of hemagglutinin (HA)-reactive antibodies. Next-generation influenza vaccines should be optimized in order to activate NA-reactive B cells and to induce a broadly cross-reactive and protective antibody response. We aimed at enhancing the immunogenicity of the NA on vaccines by two strategies: (i) modifying the HA:NA ratio of the vaccine preparation and (ii) exposing epitopes on the lateral surface or beneath the head of the NA by extending the NA stalk.
View Article and Find Full Text PDFAdvances in affinity chromatography now make it possible to analyze immunoglobulin G from plasma and its fractions with a simple chromatographic method. Ligands derived from camelid antibodies have been developed which have affinity to all 4 subclasses of human IgG without a cross reactivity to other immunoglobulins. The commercially available Capture Select FcXL is the basis for a simple method for direct quantification of immunoglobulin G from plasma or from fractions from cold ethanol precipitation.
View Article and Find Full Text PDFArticle Synopsis
- Secretory immunoglobulin A (sIgA) is being explored for use in therapies related to the gut, with current research focused on its purification from Chinese hamster ovary (CHO) cell cultures.
- Researchers used aqueous two-phase systems (ATPS) in their study to purify sIgA monoclonal antibodies (mAbs), analyzing factors like pH and PEG concentration to optimize the process.
- The results indicated that under specific conditions, sIgA mAbs predominantly ended up in the PEG phase, and the method demonstrated potential for efficient and cost-effective manufacturing of sIgA biotherapeutics.
Staphylococcal protein-A affinity chromatography has been optimized for antibody purification, achieving a current capacity of up to 90 mg/ml in packed bed. The morphology of the particles, the number of antibodies bound per ligand and the spatial arrangement of the ligands were assessed by in-situ Small-angle X-ray scattering (SAXS) and scanning electron microscopy (SEM) combined with measurement of adsorption isotherms. We employed SAXS measurements to probe the nanoscale structure of the chromatographic resin.
View Article and Find Full Text PDF