About this Research Topic
Antibody therapeutics are now well established as drugs of major commercial and medical importance in the treatment of arthritis, cancer, and other diseases. Bacterial superantigens, such as Protein A, have been used in antibody purification and other applications, which rely on their ability to bind to a wide range of antibodies. However, their antibody binding behavior can be complex. For example, recent research has shown that antibody framework regions (FWRs) and complementarity-determining regions (CDRs), and even the heavy chain constant region (CH) in Trastuzumab can play a synergistic role in superantigen binding without loss of specificity to the original Her2 antigen. Such non-conventional, additional superantigen interactions may play a role in antibody-based disease pathogenesis, as well as the success and effectiveness of therapeutic antibodies.
Given the role of superantigens such as Protein A, G, and L in antibody purification, it is important to examine if superantigen products by both natural flora or pathogens can influence the efficacy and effectiveness of antibody therapeutics or underlie disease pathogenesis, especially given that antibody-microbial interactions can occur e.g. Staphylococcus aureus colonization of nasal cavities may produce Protein A and lead to disease pathogenesis in allergic rhinitis patients. In fact, this Protein A- VH3 interaction was found to be influenced by a combination of CDR2 and VH3 in Trastuzumab. With several possible effects and uses, antibody-microbial interactions can therefore influence disease pathogenesis as well as play a role in therapeutic off-targets and success.
Recent advances have shown that the binding of antibody regions to microbial products involves myriad factors, with effects on biological function, antibody purification, and disease pathogenesis. Through structural analysis, mutations can be made in antibodies that abolish such microbial protein binding, although they are distal from the actual binding site. There is much to understand and investigate in how the natural antibody repertoire can display varying effects on the binding of a whole range of microbial products.
In addition, antibody evasion methods employed by some microbial pathogens can lead to the discovery of novel superantigens which may be exploited for antibody purification. This also implicates the study of how the microorganisms can escape antibody-based responses that can reveal disease pathogenicity.
The scope of this Research Topic is to gather a comprehensive list of articles related to “Antibody-Microbial interactions”. The Research Topic will cover various aspects spanning from basic, translational, and clinical research related to the area. We welcome the submission of Original Research Articles, Reviews, Mini-Reviews, and Clinical Trials covering, but not limited to, the following topics:
1. Non-canonical antibody-microbial product interactions
2. The effect of antibody engineering on non-canonical antibody-microbial protein interactions.
3. Novel non-antigen based antibody-receptor-microbial interactions
4. Effects of the non-canonical antigen-based antibody-microbial interactions
5. Protein engineering of the microbial proteins for novel antibody/IgFcR interactions
6. The role of non-canonical antibody-microbial interactions in disease pathogenesis.
7. Clinical/Animal model clues of antibody-microbial product interactions via colonization.
8. Novel superantigens and their characterization/effects.
Keywords: Antibody engineering, Superantigens, Antibody-Microbial interactions, Antibody evasion
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