Publications by authors named "Julia Anzengruber"
Purpose: To explore how the natural heterogeneity of human coagulation factor VIII (FVIII) and the processing of its B-domain specifically modulate protein aggregation.
Methods: Recombinant FVIII (rFVIII) molecular species containing 70% or 20% B-domain, and B-domain-deleted rFVIII (BDD-rFVIII), were separated from full-length recombinant FVIII (FL-rFVIII). Purified human plasma-derived FVIII (pdFVIII) was used as a comparator.
Article Synopsis
- Lactobacillus buchneri CD034 has a unique two-dimensional S-layer on its surface, but understanding how this layer connects to the cell wall is still unclear.
- Researchers identified lipoteichoic acid as a key component of the bacterium's cell wall, which may play a role in this binding process.
- The study used advanced techniques like NMR and single-molecule force spectroscopy to reveal that the S-layer protein and lipoteichoic acid directly interact, providing insights into the structural integrity of Lactobacillus cell walls.
Article Synopsis
- Peanut allergy is a serious IgE-mediated condition with no current treatment, leading to research on potential vaccines targeting the most potent allergen, Ara h 2.
- A fusion protein combining the S-layer protein from Lactobacillus and a peptide derived from Ara h 2 was developed and tested for its ability to inhibit IgE binding in allergic patients.
- Results showed that while the fusion protein recognized IgE in many cases, it did not trigger a significant allergic response, suggesting this peptide-based vaccine approach could be viable but may require multiple allergen peptides for broader protection.
Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.
Microbiology (Reading)
August 2014
Bacterial cell wall hydrolases are essential for peptidoglycan remodelling in regard to bacterial cell growth and division. In this study, peptidoglycan hydrolases (PGHs) of different Lactobacillus buchneri strains were investigated. First, the genome sequence of L.
View Article and Find Full Text PDFBased on the previous demonstration of surface (S-) layer protein glycosylation in Lactobacillus buchneri 41021/251 and because of general advantages of lactic acid bacteria for applied research, protein glycosylation in this bacterial species was investigated in detail. The cell surface of L. buchneri CD034 is completely covered with an oblique 2D crystalline array (lattice parameters, a = 5.
View Article and Find Full Text PDFSurface (S)-layer proteins are model systems for studying protein glycosylation in bacteria and simultaneously hold promises for the design of novel, glyco-functionalized modules for nanobiotechnology due to their 2D self-assembly capability. Understanding the mechanism governing S-layer glycan biosynthesis in the Gram-positive bacterium CCM 2051 is necessary for the tailored glyco-functionalization of its S-layer. Here, the putative oligosaccharyl:S-layer protein transferase WsfB from the S-layer glycosylation gene locus is characterized.
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