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dc.contributor.authorAhsendorf, Henrike P
dc.contributor.authorGan, Li L
dc.contributor.authorEltom, Kamal H
dc.contributor.authorAbd El Wahed, Ahmed
dc.contributor.authorHotop, Sven-Kevin
dc.contributor.authorRoper, Rachel L
dc.contributor.authorBeutling, Ulrike
dc.contributor.authorBroenstrup, Mark
dc.contributor.authorStahl-Hennig, Christiane
dc.contributor.authorHoelzle, Ludwig E
dc.contributor.authorCzerny, Claus-Peter
dc.date.accessioned2019-07-08T14:46:57Z
dc.date.available2019-07-08T14:46:57Z
dc.date.issued2019-05-29
dc.identifier.citationViruses. 2019 May 29;11(6). pii: v11060493. doi: 10.3390/v11060493.en_US
dc.identifier.issn1999-4915
dc.identifier.pmid31146446
dc.identifier.doi10.3390/v11060493
dc.identifier.urihttp://hdl.handle.net/10033/621851
dc.description.abstractThe vaccinia virus (VACV) A27 protein and its homologs, which are found in a large number of members of the genus Orthopoxvirus (OPXV), are targets of viral neutralization by host antibodies. We have mapped six binding sites (epitopes #1A: aa 32-39, #1B: aa 28-33, #1C: aa 26-31, #1D: 28-34, #4: aa 9-14, and #5: aa 68-71) of A27 specific monoclonal antibodies (mAbs) using peptide arrays. MAbs recognizing epitopes #1A-D and #4 neutralized VACV Elstree in a complement dependent way (50% plaque-reduction: 12.5-200 µg/mL). Fusion of VACV at low pH was blocked through inhibition of epitope #1A. To determine the sequence variability of the six antigenic sites, 391 sequences of A27 protein homologs available were compared. Epitopes #4 and #5 were conserved among most of the OPXVs, while the sequential epitope complex #1A-D was more variable and, therefore, responsible for species-specific epitope characteristics. The accurate and reliable mapping of defined epitopes on immuno-protective proteins such as the A27 of VACV enables phylogenetic studies and insights into OPXV evolution as well as to pave the way to the development of safer vaccines and chemical or biological antivirals.en_US
dc.language.isoenen_US
dc.publisherMPDIen_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectVaccinia virus A27 protein homologsen_US
dc.subjectepitope mappingen_US
dc.subjectneutralizing antibodiesen_US
dc.subjectphylogenetic epitope variationen_US
dc.titleSpecies-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses.en_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalViorusesen_US
refterms.dateFOA2019-07-08T14:46:57Z
dc.source.journaltitleViruses


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