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Article: Screening and identification of mimotopes of the major shrimp allergen tropomyosin using one-bead-one-compound peptide libraries

TitleScreening and identification of mimotopes of the major shrimp allergen tropomyosin using one-bead-one-compound peptide libraries
Authors
Keywordsepitope
mimotope
OBOC peptide library
tropomyosin
Issue Date2017
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cmi/index.html
Citation
Cellular & Molecular Immunology, 2017, v. 14, p. 308-318 How to Cite?
AbstractThe one-bead-one-compound (OBOC) combinatorial peptide library is a powerful tool to identify ligand and receptor interactions. Here, we applied the OBOC library technology to identify mimotopes specific to the immunoglobulin E (IgE) epitopes of the major shellfish allergen tropomyosin. OBOC peptide libraries with 8-12 amino acid residues were screened with serum samples from patients with shellfish allergy for IgE mimotopes of tropomyosin. Twenty-five mimotopes were identified from the screening and their binding reactivity to tropomyosin-specific IgE was confirmed by peptide ELISA. These mimotopes could be divided into seven clusters based on sequence homology, and epitope mapping by EpiSearch of the clustered mimotopes was performed to characterize and confirm the validity of mimotopes. Five out of six of the predicted epitopes were found to overlap with previously identified epitopes of tropomyosin. To further confirm the mimicry potential of mimotopes, BALB/c mice were immunized with mimotopes conjugated to keyhole limpet hemocyanin and assayed for their capacity to induce tropomyosin-specific antibodies. BALB/c mice that received mimotope immunization were found to have an elevated level of tropomyosin-specific immunoglobulin G, but not mice that received an irrelevant mimotope. This study pioneers the successful application of the OBOC libraries using whole sera to screen and identify multiple shrimp allergen mimotopes and validates their mimicry potential using in vitro, in vivo, and in silico methods. © 2017 CSI and USTC. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/223228
ISSN
2017 Impact Factor: 7.551
2015 SCImago Journal Rankings: 1.898
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLeung, NYH-
dc.contributor.authorWai, CYY-
dc.contributor.authorHo, MHK-
dc.contributor.authorLiu, R-
dc.contributor.authorLam, KS-
dc.contributor.authorWang, JJ-
dc.contributor.authorShu, SA-
dc.contributor.authorChu, KH-
dc.contributor.authorLeung, PSC-
dc.date.accessioned2016-02-23T01:55:46Z-
dc.date.available2016-02-23T01:55:46Z-
dc.date.issued2017-
dc.identifier.citationCellular & Molecular Immunology, 2017, v. 14, p. 308-318-
dc.identifier.issn1672-7681-
dc.identifier.urihttp://hdl.handle.net/10722/223228-
dc.description.abstractThe one-bead-one-compound (OBOC) combinatorial peptide library is a powerful tool to identify ligand and receptor interactions. Here, we applied the OBOC library technology to identify mimotopes specific to the immunoglobulin E (IgE) epitopes of the major shellfish allergen tropomyosin. OBOC peptide libraries with 8-12 amino acid residues were screened with serum samples from patients with shellfish allergy for IgE mimotopes of tropomyosin. Twenty-five mimotopes were identified from the screening and their binding reactivity to tropomyosin-specific IgE was confirmed by peptide ELISA. These mimotopes could be divided into seven clusters based on sequence homology, and epitope mapping by EpiSearch of the clustered mimotopes was performed to characterize and confirm the validity of mimotopes. Five out of six of the predicted epitopes were found to overlap with previously identified epitopes of tropomyosin. To further confirm the mimicry potential of mimotopes, BALB/c mice were immunized with mimotopes conjugated to keyhole limpet hemocyanin and assayed for their capacity to induce tropomyosin-specific antibodies. BALB/c mice that received mimotope immunization were found to have an elevated level of tropomyosin-specific immunoglobulin G, but not mice that received an irrelevant mimotope. This study pioneers the successful application of the OBOC libraries using whole sera to screen and identify multiple shrimp allergen mimotopes and validates their mimicry potential using in vitro, in vivo, and in silico methods. © 2017 CSI and USTC. All rights reserved.-
dc.languageeng-
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/cmi/index.html-
dc.relation.ispartofCellular & Molecular Immunology-
dc.subjectepitope-
dc.subjectmimotope-
dc.subjectOBOC peptide library-
dc.subjecttropomyosin-
dc.titleScreening and identification of mimotopes of the major shrimp allergen tropomyosin using one-bead-one-compound peptide libraries-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1038/cmi.2015.83-
dc.identifier.pmid26364917-
dc.identifier.scopuseid_2-s2.0-85014651886-
dc.identifier.hkuros256750-
dc.identifier.volume14-
dc.identifier.spage308-
dc.identifier.epage318-
dc.identifier.isiWOS:000395929100008-
dc.publisher.placeChina-

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