2.50
Hdl Handle:
http://hdl.handle.net/2436/30202
Title:
Characterization of anti-myosin monoclonal antibodies.
Authors:
Nelson, Paul N.; Astley, S.J.; Roden, Denise A.; Waldron, E.E.; Baig, K.M.; Caforio, A.L.; Koutedakis, Yiannis; Perera, Shantha; Spry, C.
Abstract:
The characterization of monoclonal antibodies (MAbs) with regard to reactivity and specificity is important for the successful application as a molecular probe and/or diagnostic reagent. Furthermore, it is recognized that some monoclonal reagents perform well in some assay systems but not others. In this study, the reactivity profiles of two anti-myosin MAbs (H1 and DH2, raised against human cardiac myosin) were evaluated in enzyme-linked immunosorbent assay (ELISA), slot-blotting, and immunocytochemistry. Both antibodies performed well in slot-blotting against myosin heavy chain preparations from cardiac and skeletal muscle and from non-human sources. In general, MAb H1 demonstrated strong to moderate reactivity in all assay systems, whilst MAb DH2 faired poorly in ELISA. MAb H1 also showed reactivity to synthetic peptides of myosin, one of which possessed a motif (ERRDA, single amino acid code) that was found in other human and nonhuman myosin protein sequences that could explain its cross-reactive profile. Intriguingly, this motif was found on viral and other pathogenic agents associated with myocarditis. Hence, it is speculated that this region could give some credence to the mechanism of molecular mimicry associated with some cardiac diseases. Overall, MAb H1 may serve as a useful probe of myosin structure.
Citation:
Hybridoma, 24(6): 314-318
Publisher:
New Rochelle (NY): Mary Ann Liebert, Inc.
Journal:
Hybridoma
Issue Date:
2005
URI:
http://hdl.handle.net/2436/30202
DOI:
10.1089/hyb.2005.24.314
PubMed ID:
16332199
Additional Links:
http://www.liebertonline.com/doi/abs/10.1089/hyb.2005.24.314; http://direct.bl.uk/bld/PlaceOrder.do?UIN=178812929&ETOC=RN&from=searchengine
Type:
Article
Language:
en
ISSN:
1554-0014
Appears in Collections:
Molecular Immunology Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorNelson, Paul N.-
dc.contributor.authorAstley, S.J.-
dc.contributor.authorRoden, Denise A.-
dc.contributor.authorWaldron, E.E.-
dc.contributor.authorBaig, K.M.-
dc.contributor.authorCaforio, A.L.-
dc.contributor.authorKoutedakis, Yiannis-
dc.contributor.authorPerera, Shantha-
dc.contributor.authorSpry, C.-
dc.date.accessioned2008-06-19T15:20:31Z-
dc.date.available2008-06-19T15:20:31Z-
dc.date.issued2005-
dc.identifier.citationHybridoma, 24(6): 314-318en
dc.identifier.issn1554-0014-
dc.identifier.pmid16332199-
dc.identifier.doi10.1089/hyb.2005.24.314-
dc.identifier.urihttp://hdl.handle.net/2436/30202-
dc.description.abstractThe characterization of monoclonal antibodies (MAbs) with regard to reactivity and specificity is important for the successful application as a molecular probe and/or diagnostic reagent. Furthermore, it is recognized that some monoclonal reagents perform well in some assay systems but not others. In this study, the reactivity profiles of two anti-myosin MAbs (H1 and DH2, raised against human cardiac myosin) were evaluated in enzyme-linked immunosorbent assay (ELISA), slot-blotting, and immunocytochemistry. Both antibodies performed well in slot-blotting against myosin heavy chain preparations from cardiac and skeletal muscle and from non-human sources. In general, MAb H1 demonstrated strong to moderate reactivity in all assay systems, whilst MAb DH2 faired poorly in ELISA. MAb H1 also showed reactivity to synthetic peptides of myosin, one of which possessed a motif (ERRDA, single amino acid code) that was found in other human and nonhuman myosin protein sequences that could explain its cross-reactive profile. Intriguingly, this motif was found on viral and other pathogenic agents associated with myocarditis. Hence, it is speculated that this region could give some credence to the mechanism of molecular mimicry associated with some cardiac diseases. Overall, MAb H1 may serve as a useful probe of myosin structure.en
dc.language.isoenen
dc.publisherNew Rochelle (NY): Mary Ann Liebert, Inc.en
dc.relation.urlhttp://www.liebertonline.com/doi/abs/10.1089/hyb.2005.24.314en
dc.relation.urlhttp://direct.bl.uk/bld/PlaceOrder.do?UIN=178812929&ETOC=RN&from=searchengineen
dc.subjectMonoclonal antibodiesen
dc.subjectMolecular Biologyen
dc.subjectELISAen
dc.subjectBlotting, Sloten
dc.subjectMyosinen
dc.subjectHearten
dc.subject.meshAmino Acid Motifsen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAnimalsen
dc.subject.meshAntibodies, Monoclonalen
dc.subject.meshAntibody Specificityen
dc.subject.meshCardiac Myosinsen
dc.subject.meshCross Reactionsen
dc.subject.meshEnzyme-Linked Immunosorbent Assayen
dc.subject.meshHumansen
dc.subject.meshHybridomasen
dc.subject.meshImmunohistochemistryen
dc.subject.meshMolecular Sequence Dataen
dc.titleCharacterization of anti-myosin monoclonal antibodies.en
dc.typeArticleen
dc.identifier.journalHybridomaen

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