Absence of elevated anti–α-synuclein and anti-EBV latent membrane protein antibodies in PD

We recently demonstrated that commercially available monoclonal antibodies generated against the latent membrane protein 1 (LMP1) of Epstein–Barr virus (EBV) cross-react with the neuronal protein α-synuclein.1 LMP1 is a virally encoded protein expressed during EBV latency. Up to 22% of healthy EBV-seropositive individuals generate a humoral immune response against this protein as part of a lifelong immune surveillance of EBV.2,3⇓ Whether this cross-reaction has any biological relevance remains to be determined. There is growing evidence for a primary role of α-synuclein aggregation in the pathogenesis of PD.4 Insoluble α-synuclein filaments accumulate in brains of patients with PD. Recombinant α-synuclein protein can assemble in elongated filaments with ultrastructural features similar to those of Lewy body filaments observed in situ. In light of this as well as the fact that EBV latently infects approximately 90% of the human population worldwide and represents the target of a lifelong immune response, we were interested in exploring the possibility that molecular mimicry between EBV (and specifically the LMP1 protein) and α-synuclein could be involved in the pathogenesis or progression of …