Extended Data Fig. 1: UB-312 derived antibodies preferentially bind aggregated αSyn and alter the kinetics of αSyn aggregation in the SAA. | Nature Medicine

Extended Data Fig. 1: UB-312 derived antibodies preferentially bind aggregated αSyn and alter the kinetics of αSyn aggregation in the SAA.

From: Target engagement and immunogenicity of an active immunotherapeutic targeting pathological α-synuclein: a phase 1 placebo-controlled trial

Extended Data Fig. 1

(a) Dot blot analyses indicate that IgG fractions and affinity purified antibodies collected from healthy volunteers post-immunization (week 17) preferentially bind aggregates of αSyn derived from patients with MSA or PD, as well as to aggregates of recombinant αSyn. (b) Post-immunization IgG fractions spiked into a buffer containing seeds delay the aggregation of αSyn. Data are means ± SEM. Samples were run in triplicate (c) Post-immunization IgG fractions spiked into a CSF sample from a patient with PD delay the aggregation of αSyn. Data are means ± SEM. Samples were run in duplicate. αSyn-SAA, alpha-synuclein seed amplification assay; Ab, antibody; CSF, cerebrospinal fluid; IgG, immunoglobulin G; MSA, multiple system atrophy; SEM, standard error of the mean; PD, Parkinson’s disease.

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