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Aglycosylated chimeric mouse/human IgG1 antibody retains some effector function
H Dorai1, B M Mueller, R A Reisfeld
1Abbott Biotech, Inc., Needham Heights, MA 02194.
The N-linked carbohydrate attachment site of human IgG1 Ab has been eliminated by site-directed mutagenesis. Effector functions of aglycosylated Ab was then compared to its native counterpart. Aglycosylated Ab failed to exhibit any ADCC activity, but a significant level of CDC activity was retained by the aglycosylated Ab. These observations differ from those reported previously. Serum half-life and biodistribution of aglycosylated Ab in mice were comparable to the native Ab. Together, these results show that some, but not all, effector functions of a human IgG1 Ab are affected by aglycosylation.
The N-linked carbohydrate attachment site of human IgG1 Ab has been eliminated by site-directed mutagenesis. Effector functions of aglycosylated Ab was then compared to its native counterpart. Aglycosylated Ab failed to exhibit any ADCC activity, but a significant level of CDC activity was retained by the aglycosylated Ab. These observations differ from those reported previously. Serum half-life and biodistribution of aglycosylated Ab in mice were comparable to the native Ab. Together, these results show that some, but not all, effector functions of a human IgG1 Ab are affected by aglycosylation.