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Open AccessArticle

Species-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses

1
Division of Microbiology and Animal Hygiene, Department of Animal Sciences, University of Goettingen, Burckhardtweg 2, 37077 Goettingen, Germany
2
German Primate Center, Leibniz-Institute for Primate Research, Unit of Infection Models, Kellnerweg 4, 37077 Goettingen, Germany
3
Unit of Animal Health and Safety of Animal Products, Institute for Studies and Promotion of Animal Exports, University of Khartoum, 13314 Shambat, P.O. Box 32; 11115 Khartoum North, Sudan
4
Helmholtz Centre for Infection Research, Inhoffenstraße 7, 38124 Braunschweig, Germany
5
Brody Medical School, East Carolina University, Greenville, NC 27834, USA
6
Institute for Animal Sciences, Livestock Infectiology and Environmental Hygiene, University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany
*
Author to whom correspondence should be addressed.
Passed away during the final stages of completion of this manuscript.
Viruses 2019, 11(6), 493; https://doi.org/10.3390/v11060493
Received: 29 April 2019 / Revised: 25 May 2019 / Accepted: 28 May 2019 / Published: 29 May 2019
(This article belongs to the Section Animal Viruses)
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. View Full-Text
Keywords: Vaccinia virus A27 protein homologs; epitope mapping; phylogenetic epitope variation; neutralizing antibodies Vaccinia virus A27 protein homologs; epitope mapping; phylogenetic epitope variation; neutralizing antibodies
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Ahsendorf, H.P.; Gan, L.L.; Eltom, K.H.; Abd El Wahed, A.; Hotop, S.-K.; Roper, R.L.; Beutling, U.; Broenstrup, M.; Stahl-Hennig, C.; Hoelzle, L.E.; Czerny, C.-P. Species-Specific Conservation of Linear Antigenic Sites on Vaccinia Virus A27 Protein Homologs of Orthopoxviruses. Viruses 2019, 11, 493.

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