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Abstract

Gp41 peptide antigen of the HIV-1 envelope (TP41-1:TPRGPDRPEGIEEEGGERDR, a highly conserved region) was enzymatically degraded by the antibody light chain 41S-2-L after an induction period. The peptide bond between Glu14 and Gly15 was cleaved early in the reaction. When EDTA was added in the induction period, it inhibited the degradation of TP41-1 thus ceasing the catalytic activity of 41S-2-L. In contrast, when EDTA was added after the induction period, only a small reduction in the catalytic activity was observed. These observations suggest that metal ions are important in stimulating catalytic activity early in the reaction.

Metal-dependent amyloid β-degrading catalytic antibody construct

“…The possibility of applying co-dependence on a metal for identifying high-activity catabodies suitable for medical application, however, has not been examined adequately. Two groups reported metal-activated proteolysis by catabodies directed to HIV proteins and an autoantigen (Hifumi et al 2000; Polosukhina et al 2006; Baranova et al 2010). Like IgV 2E6, these catabodies utilize the serine protease catalytic mechanism, but their metal-dependency appears to be less strict.…”