| Literature DB >> 17485143 |
Anthony Kusalik1, Miķelis Bickis, Christopher Lewis, Ying Li, Guglielmo Lucchese, Francesco M Marincola, Darja Kanduc.
Abstract
Alignment of protein sequences is fundamental in analyzing homology, evolutionary events and functional relationships. Searching for the epitopic peptide platform underlying hepatitis C virus (HCV) infection and autoimmune phenomena, we have used sequence-sequence peptide matching to compare the HCV polyprotein sequence to the human proteome. The following results were obtained: (1) pentamers from HCV polyprotein have a widespread and high level of similarity to a large number of human proteins (19,605 human proteins, that is 57.6% of the human proteome); (2) remarkable similarity between the two proteomes persists even using longer peptide motifs as probes for identity scanning; (3) only a limited number of HCV pentameric fragments have no similarity to the human host, so representing molecular sequence signatures of the virus. We conclude that the widespread sharing of numerous perfect exact matches between HCV and human proteomes might explain HCV persistence in humans.Entities:
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Year: 2007 PMID: 17485143 DOI: 10.1016/j.peptides.2007.04.001
Source DB: PubMed Journal: Peptides ISSN: 0196-9781 Impact factor: 3.750