Ricerc@Sapienza

Abstract EBV (Epstein Barr Virus) has been associated with numerous autoimmune syndromes in epidemiologic studies. In this work immunoglobulin G response to EBV antigens similar to antigens from host proteins was analyzed using a laser printed microarray (PEPperprint.com). IgG response to overlapping peptides derived from immunologically important EBV proteins including ZEBRA (BZLF-1 encoded protein), BALF-2 recombinase expressed primarily during the viral lytic replication cycle, and EBNA-1 (Epstein Barr Virus Nuclear Antigen) expressed during the viral latency cycle respectively were characterized. These viral proteins have domains shared with host DNA–binding proteins in the human immune response that may cross-react through “molecular mimicry” triggering antinuclear and other autoantibodies. IgG response to conserved “A/T hooks” in EBV-encoded proteins such as EBNA-1 and the BALF-2 recombinase related to host DNA–binding proteins including RAG-1 recombinase and histones, and EBV-encoded virokines such as the IL-10 homologue BCRF-1 suggest further directions for clinical research. Proteomic “molecular fingerprints” of the immune response to viral proteins is relatively inexpensive and potentially useful in monitoring autoantibody production and response to therapy.