NDLI: Sub-epitopic dissection of HCV E1315–328HRMAWDMMMNWSPT sequence by similarity analysis

Content Provider	Springer Nature Link
Author	Polime, L. Mittelman, A. Gennero, L. Ponzetto, A. Lucchese, G. Stufa, A. Kusalik, A. Kanduc, D.
Copyright Year	2007
Abstract	Our labs are focused on identifying amino acid sequences having the ability to react specifically with the functional binding site of a complementary antibody. Our epitopic definition is based on the analysis of the similarity level of antigenic amino acid sequences to the host proteome. Here, the similarity profile to the human proteome of an HCV E1 immunodominant epitope, i.e. the HCV E1315–328HRMAWDMMMNWSPT sequence, led to i) characterizing the immunoreactive HCV E1 315–328 region as a sequence endowed with a low level of similarity to human proteins; ii) defining 2 contiguous immunodominant linear determinants respectively located at the NH2 and COOH terminus of the conserved viral antigenic sequence. This study supports the hypothesis that low sequence similarity to the host’s proteome modulates the pool of epitopic amino acid sequences in a viral antigen, and appears of potential value in defining immunogenic viral peptide sequences to be used in immunotherapeutic approaches for HCV treatment.
Starting Page	479
Ending Page	484
Page Count	6
File Format	PDF
ISSN	09394451
Journal	Amino Acids
Volume Number	34
Issue Number	3
e-ISSN	14382199
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-04-26
Publisher Place	Vienna
Access Restriction	Subscribed
Subject Keyword	Biochemistry Analytical Chemistry Biochemical Engineering Life Sciences Proteomics Neurobiology
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Biochemistry Clinical Biochemistry

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