Publications by authors named "Tala Azzam"
Endo-β-N-acetylglucosaminidases (ENGases) that specifically hydrolyze the Asn297-linked glycan on immunoglobulin G (IgG) antibodies, the major molecular determinant of fragment crystallizable (Fc) γ receptor (FcγR) binding, are exceedingly rare. All previously characterized IgG-specific ENGases are multi-domain proteins secreted as an immune evasion strategy by Streptococcus pyogenes strains. Here, using in silico analysis and mass spectrometry techniques, we identified a family of single-domain ENGases secreted by pathogenic corynebacterial species that exhibit strict specificity for IgG antibodies.
View Article and Find Full Text PDFRedesigning protein-protein interfaces is an important tool for developing therapeutic strategies. Interfaces can be redesigned by in silico screening, which allows for efficient sampling of a large protein space before experimental validation. However, computational costs limit the number of combinations that can be reasonably sampled.
View Article and Find Full Text PDFArticle Synopsis
- Antibody-based drugs, especially IgG monoclonal antibodies, are widely used to treat various diseases such as cancer and autoimmune disorders, owing to their specialized therapeutic properties.
- The efficacy and functionality of IgG antibodies are influenced by specific modifications in their sugar structures (glycoforms), which affect how they interact with other cells and proteins in the body.
- To improve the effectiveness of these antibodies, researchers are exploring advanced engineering methods to create antibodies with customized glycoforms through techniques like using engineered cell lines and glycoengineering approaches.