ABSTRACT
Alzheimer's disease is the most prominent neurodegenerative disease and has no efficient therapies available so far. Immunotherapy against amyloid-ß (Aß) peptide is one of the currently tested therapeutic approaches. Here we have reviewed the available structural knowledge about antibodies tested as passive anti-Aß immunotherapy in clinical trials. The therapeutic anti-Aß antibodies differ in their epitope specificity and in recognition and affinity to different Aß species present in vivo (Tab. 1, Fig. 1, Ref. 17).
Subject(s)
Alzheimer Disease/drug therapy , Amyloid beta-Peptides/antagonists & inhibitors , Antibodies/therapeutic use , Immunotherapy/methods , Alzheimer Disease/metabolism , Amyloid beta-Peptides/immunology , Amyloid beta-Peptides/metabolism , Antibodies, Monoclonal/therapeutic use , Antibodies, Monoclonal, Humanized/therapeutic use , HumansABSTRACT
Antibodies are broadly used in clinical and basic research. Many of monoclonal antibodies are successfully adopted for therapeutic and diagnostic targeting of viral pathogens. Efficacy of antiviral neutralizing or protective antibodies depends on their ability to recognize epitopes interfering with viral infection. However, viruses are able to incessantly change their antigenic determinants to escape surveillance of humoral immune system and therefore the successful antiviral therapies require continuous development. Characterization of interactions of antibodies with prevalently conformational viral epitopes is important for understanding antibody mode of action and can help to identify conserved regions that may be exploited in designing new vaccines and virus neutralizing antibodies. In this article, we are reviewing techniques in use for characterization of conformational epitopes of monoclonal antibodies with focus on viruses.
