Open AccessPeptide matching between Epstein–Barr virus and human proteins
Author(s) -
Capone Giovanni,
Calabrò Michele,
Lucchese Guglielmo,
Fasano Candida,
Girardi Bruna,
Polimeno Lorenzo,
Kanduc Darja
Publication year - 2013
Publication title -
pathogens and disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.983
H-Index - 105
ISSN - 2049-632X
DOI - 10.1111/2049-632x.12066
Subject(s) - biology , chromatin , rna splicing , epstein–barr virus , virus , peptide sequence , rna , virology , microbiology and biotechnology , genetics , computational biology , dna , gene
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 NH 2 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.