| How a single amino acid change may alter the immunological information of a peptide. | |
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MedLine Citation:
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PMID: 22202001 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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What types of amino acid substitutions are functionally tolerated in an epitope? This question is of importance because the immunogenicity, pathogenicity, and therapeutic potential of a peptide can be determined by a single amino acid change. As an example, a single amino acid change in the encephalitogenic myelin oligodendrocyte glycoprotein WYRSPFSRVV peptide confers the capacity to ameliorate and reverse experimental autoimmune encephalomyelitis. Currently, no rule is available to predict/explain the functional outcomes of amino acid changes. To address this issue, we examined the role of single amino acid changes in immune responses by applying proteomic similarity analyses to available data. We found that the loss or gain of immunological information in a peptide epitope following an amino acid substitution often is related to a gain or loss in the proteomic similarity. Rare, but significant epitopic sequences become immunologically insignificant when an amino acid change makes them common, repeated sequences. This study confirms that low similarity to the host proteome is a major factor in modulating the immune epitope repertoire. |
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Authors:
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Guglielmo Lucchese; Animesh Amart Sinha; Darja Kanduc |
Publication Detail:
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Type: Journal Article Date: 2012-01-01 |
Journal Detail:
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Title: Frontiers in bioscience (Elite edition) Volume: 4 ISSN: 1945-0508 ISO Abbreviation: Front Biosci (Elite Ed) Publication Date: 2012 |
Date Detail:
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Created Date: 2011-12-28 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101485240 Medline TA: Front Biosci (Elite Ed) Country: United States |
Other Details:
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Languages: eng Pagination: 1843-52 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, University of Bari, Italy. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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