Peptide matching between Epstein-Barr virus and human proteins

Epstein-Barr virus proteins were examined for amino acid sequence matching to human proteins at the decapeptide level. We report that numerous EBV peptides of different length (from 10- to 13-mer) are present in 28 human proteins. The viral vs. human peptide overlap mainly involves the glycine-rich region allocated in the NH2 terminus of Epstein-Barr nuclear antigen 1 protein and host cellular components that play crucial roles in basic biochemical pathways, such as chromatin remodeling, RNA splicing, transmission across chemical/electrical synapses, and neurogenesis, and that, when altered, may characterize various pathologies such as immunodeficiency, systemic lupus erythematosus, myelination, and speech disorders. The present results might contribute to understand and define the (physio) pathological relationships and interactions occurring between EBV and the human host. This article describes a high level of peptide similarity between human proteins and proteins encoded by the Epstein Barr virus (EBV), in particular in the glycine-alanine (GA) repeat region of the nuclear antigen 1 of EBV (EBNA1). Some of the human proteins that share similarities with EBV are implicated in brain development and function. These similarities could contribute to preventing immune recognition of EBV and form the basis for molecular mimicry in autoimmune diseases.