Stahl-Hennig, Christiane

[["dc.bibliographiccitation.artnumber","493"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Viruses"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Ahsendorf, Henrike"],["dc.contributor.author","Gan, Li"],["dc.contributor.author","Eltom, Kamal"],["dc.contributor.author","Abd El Wahed, Ahmed"],["dc.contributor.author","Hotop, Sven-Kevin"],["dc.contributor.author","Roper, Rachel"],["dc.contributor.author","Beutling, Ulrike"],["dc.contributor.author","Broenstrup, Mark"],["dc.contributor.author","Stahl-Hennig, Christiane"],["dc.contributor.author","Hoelzle, Ludwig"],["dc.contributor.author","Czerny, Claus-Peter"],["dc.date.accessioned","2019-07-09T11:51:50Z"],["dc.date.available","2019-07-09T11:51:50Z"],["dc.date.issued","2019"],["dc.description.abstract","The 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."],["dc.identifier.doi","10.3390/v11060493"],["dc.identifier.pmid","31146446"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16205"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60022"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","630"],["dc.title","Species-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3648"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Hansen, Sören"],["dc.contributor.author","Hotop, Sven-Kevin"],["dc.contributor.author","Faye, Oumar"],["dc.contributor.author","Ndiaye, Oumar"],["dc.contributor.author","Böhlken-Fascher, Susanne"],["dc.contributor.author","Pessôa, Rodrigo"],["dc.contributor.author","Hufert, Frank"],["dc.contributor.author","Stahl-Hennig, Christiane"],["dc.contributor.author","Frank, Ronald"],["dc.contributor.author","Czerny, Claus-Peter"],["dc.contributor.author","Schmidt-Chanasit, Jonas"],["dc.contributor.author","Sanabani, Sabri S."],["dc.contributor.author","Sall, Amadou A."],["dc.contributor.author","Niedrig, Matthias"],["dc.contributor.author","Brönstrup, Mark"],["dc.contributor.author","Fritz, Hans-Joachim"],["dc.contributor.author","Abd El Wahed, Ahmed"],["dc.date.accessioned","2019-07-09T11:50:13Z"],["dc.date.available","2019-07-09T11:50:13Z"],["dc.date.issued","2019"],["dc.description.abstract","Zika virus (ZIKV) is a mosquito-borne flavivirus. Homologous proteins of different flaviviruses display high degrees of sequence identity, especially within subgroups. This leads to extensive immunological cross-reactivity and corresponding problems for developing a ZIKV-specific serological assay. In this study, peptide microarrays were employed to identify individual ZIKV antibody targets with promise in differential diagnosis. A total of 1643 overlapping oligopeptides were synthesized and printed onto glass slides. Together, they encompass the full amino acid sequences of ZIKV proteomes of African, Brazilian, USA, and French Polynesian origins. The resulting ZIKV scanning microarray chips were used to screen three pools of sera from recent Zika outbreaks in Senegal and Cape Verde, in Brazil, and from overseas travelers returning to the EU. Together with a mixed pool of well characterized, archived sera of patients suffering from infections by dengue, yellow fever, tick-borne encephalitis, and West Nile viruses, a total of 42 sera went into the study. Sixty-eight antibody target regions were identified. Most of which were hitherto unknown. Alignments and sequence comparisons revealed 13 of which could be classified as bona fide ZIKV-specific. These identified antibody target regions constitute a founding set of analytical tools for serological discrimination of ZIKV from other flaviviruses."],["dc.identifier.doi","10.1038/s41598-019-40224-2"],["dc.identifier.pmid","30842564"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15882"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59723"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","630"],["dc.title","Diagnosing Zika virus infection against a background of other flaviviruses: Studies in high resolution serological analysis."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]