Abstract
The hinge region is a short sequence of the heavy chains (H) of antibodies linking the Fab (Fragment antigen binding) region to the Fc (Fragment crystallisable) region. The functional properties of the four IgG subclasses partly result from the sequence differences of their hinge regions as some amino acids of the lower hinge region are located within or in the close vicinity of the C1q and FcγR binding sites on the IgG H chains. In addition, the hinge is susceptible to proteolytic cleavage by many proteases present in tumor and/or inflammatory microenvironment capable of affecting functional responses. Thus, an optimal format of the hinge region remains a major challenge for the development of new therapeutic antibodies.
Highlights
The hinge region is a short sequence of the heavy chains (H) of antibodies linking the Fab (Fragment antigen binding) region to the Fc (Fragment crystallisable) region
The functional properties of the four IgG subclasses partly result from the sequence differences of their hinge regions as some amino acids of the lower hinge region are located within or in the close vicinity of the C1q and FcgR binding sites on the IgG H chains
The hinge is susceptible to proteolytic cleavage by many proteases present in tumor and/or inflammatory microenvironment capable of affecting functional responses
Summary
> La région charnière est une courte séquence des chaînes lourdes (H) d’anticorps liant le Fab (fragment antigen binding) au Fc (fragment crystallisable). Les propriétés fonctionnelles des quatre sous-classes d’immunoglobulines d’isotype G (IgG) résultent en partie des différences de séquence de leurs régions charnières. Le format optimal de la charnière reste donc un défi majeur pour le développement de nouveaux anticorps thérapeutiques. Actuellement, les AcM thérapeutiques sont utilisés dans diverses pathologies et agissent selon différents mécanismes (agonisme/antagonisme, neutralisation, cytotoxicité) résultant de leur dualité structurale et des nombreux formats développés par ingénierie. Le choix du format optimal demeure un enjeu majeur dans le développement des nouveaux AcM. Les AcM thérapeutiques ayant obtenu à ce jour une autorisation de mise sur le marché (AMM) ont dans leur grande majorité une structure d’immunoglobuline G (IgG) humaine intégrale et possèdent ainsi une dualité.
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