Abstract
Bispecific antibodies (bsAbs) are molecules that simultaneously bind two different antigens (Ags). bsAbs represent a very active field in tumor immunotherapy with more than one hundred molecules currently being tested. More specifically, they have elicited a great interest in the setting of non-Hodgkin’s lymphoma (NHLs), where they could represent a viable option for more fragile patients or those resistant to other conventional therapies. This review aims to give a brief overview of the different available bsAb formats and their mechanisms of action, pinpointing the differences between IgG-like and non-IgG-like classes and will then focus on those in advanced clinical development for NHLs.
Highlights
Over decades of research on the pharmacology of bsAbs, with continuous efforts towards improving their properties, two different formats have been introduced in clinical use: on one hand there are single chain fragment variable-based Abs, which present no no fragment crystallizable (Fc) and are known as “non-IgG-like”; on the other hand, there are bsAbs based on the full length IgG molecule, known as “IgG-like
One can obtain a different number of Fab regions on different Abs by adding more Ag-binding units to either the amino- or carboxy-terminus of the light and/or heavy chains of monospecific Abs through short linkers. These Ag-binding units can consist in single chain fragment variable (scFv), unpaired variable light or heavy chains, or other protein constructs; and they can have the same or different structures, increasing valency or widening the range of specificities [27,28]
They employ scFv fragments of two different monoclonal Abs connected by a peptide linker, allowing them to maintain the binding activity of each Ab when assembled [31]
Summary
Bispecific antibodies (bsAbs) are antibodies (Abs) or Ab-derived structures that exhibit two different binding sites, and can link two different antigens (Ags) [1]. Their history started back in the 1960s, when initial attempts demonstrated how Abs presenting two identical Ag binding domains could be combined [2,3,4]. It was only afterwords, due to the refinement of different approaches, that they were introduced into clinical scenarios [5,6].
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