Peptide matching between Epstein–Barr virus and human proteins. Issue 3 (6th August 2013)

• Record Type: Journal Article
• Authors: Capone, Giovanni; Calabrò, Michele; Lucchese, Guglielmo; Fasano, Candida; Girardi, Bruna; Polimeno, Lorenzo; Kanduc, Darja
• Is Part Of: Pathogens and disease. Volume 69:Issue 3(2013:Dec.)
• Page Start: 205
• Page End: 212
• Publication Date: 2013-08-06
• Subjects: Medical microbiology -- Periodicals; Pathogenic microorganisms -- Periodicals; Communicable diseases -- Microbiology -- Periodicals; Communicable diseases -- Pathogenesis -- Periodicals; Host-parasite relationships -- Periodicals; Systems biology -- Periodicals; 616.904105
• DOI: 10.1111/2049-632X.12066
• Languages: English
• ISSNs: 2049-632X

Abstract

<abstract abstract-type="main" id="fim12066-abs-0001"> <title>Abstract</title> <p>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.</p> </abstract>