PMC:7228307 / 4491-5746 JSONTXT

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.

Many therapeutic mAbs depend, to varying degrees, on FcγR function (Figure 1, Table 1) for their mechanism of action (MOA) and/or their pharmacokinetic properties. For some mAbs interaction with FcγR is central to their MOA, such as the destruction of a target cell by antibody‐dependent cell‐mediated cytotoxicity (ADCC; Figure 1a) or antibody‐dependent cell‐mediated phagocytosis (phagocytosis or ADCP; Figure 1b). This also includes mAbs that may harness the inhibitory action of FcγRIIb to modulate the proinflammatory responses of immunoreceptor tyrosine activation motif (ITAM)‐dependent receptor signaling complexes (Figure 1c). For other mAbs, FcγR may play a secondary role, such as the removal or “sweeping” of all immune complexes formed by cytokine or virus‐specific neutralizing antibodies or of opsonized fragments of lysed target cells which in antigen‐presenting cells may also feed the antigen into the antigen‐presentation pathways (Figure 1d). In addition, FcγRs, particularly FcγRIIb (Figure 1e), are also key participants in the MOA of immune‐stimulating agonistic mAbs or apoptotic mAbs by acting as a scaffold for the additional cross‐linking of mAbs already bound to a cellular target, thereby inducing a signal in the target cell.