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. 2020 Apr 23;9(2):255–274. doi: 10.1007/s40121-020-00300-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License, which permits any non-commercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder.To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc/4.0/

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Fig. 1 — Scheme of the structure of the spike (S) glycoprotein of the MERS coronavirus used in vaccine development (modified from [61]). The MERS coronavirus S glycoprotein is used predominantly in vaccine development for coronaviruses. The S glycoprotein induces high titers of neutralizing antibodies, and the protein has been frequently exploited in subunit vaccination. In nature, the S glycoprotein binds to the host cell receptor DPP4 (dipeptidyl peptidase 4) through the receptor-binding domain (RBD) of the S glycoprotein [62]. The S glycoprotein can be divided into two subunits, S1 and S2. The subunit S1 contains the RBD. The subunit S2 contains heptad repeat regions (HR1 and HR2) that the virus uses for membrane fusion and entry to the host cell. The S glycoprotein is a class I fusion protein, and it exists as a trimer, as depicted. DPP4 dipeptidyl peptidase 4, S1 S1 subunit of S, S2 S2 subunit of S, RBD receptor binding domain. TMD transmembrane domain