Species-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses.
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Authors
Ahsendorf, Henrike PGan, Li L
Eltom, Kamal H
Abd El Wahed, Ahmed
Hotop, Sven-Kevin
Roper, Rachel L
Beutling, Ulrike
Broenstrup, Mark
Stahl-Hennig, Christiane
Hoelzle, Ludwig E
Czerny, Claus-Peter
Issue Date
2019-05-29
Metadata
Show full item recordAbstract
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.Citation
Viruses. 2019 May 29;11(6). pii: v11060493. doi: 10.3390/v11060493.Affiliation
HZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.Publisher
MPDIJournal
ViorusesPubMed ID
31146446Type
ArticleLanguage
enISSN
1999-4915ae974a485f413a2113503eed53cd6c53
10.3390/v11060493
Scopus Count
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- Creative Commons
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