Open Vet J. Mol. doi: 10.1038/nature12328, Lu, L., Liu, Q., Zhu, Y., Chan, K. H., Qin, L., Li, Y., et al. 2007 Apr;6(2):241-53. doi: 10.1586/14760584.6.2.241. PLoS One 9:e112602. Viruses 5, 2679–2689. Nat. Highly conserved regions within the spike proteins of human coronaviruses 229E and NL63 determine recognition of their respective cellular receptors. doi: 10.1016/s0140-6736(03)13413-7, Nyon, M. P., Du, L., Tseng, C. K., Seid, C. A., Pollet, J., Naceanceno, K. S., et al. Cell. doi: 10.1016/j.vaccine.2009.05.073, Zhong, N. S., Zheng, B. J., Li, Y. M., Poon, L. L., Xie, Z. H., Chan, K. H., et al. In addition, immunodominant M protein peptides (M1-31 and M132-161) identified using convalescent-phase sera of SARS patients and immunized mouse and rabbit sera have immunogenicity to elicit specific IgG antibodies in rabbits (He et al., 2005b). Riedmann EM, Kyd JM, Cripps AW, Lubitz W. Expert Rev Vaccines. Genetic variability of human coronavirus OC43-, 229E-, and NL63-like strains and their association with lower respiratory tract infections of hospitalized infants and immunocompromised patients. The entry of human CoVs relies on the interaction between viral and cellular membrane proteins. Boosted expression of the SARS-CoV nucleocapsid protein in tobacco and its immunogenicity in mice. First, addition of an intron splicing enhancer to the truncated SARS-CoV S protein fragments results in better enhancement of protein expression in mammalian cells than the exon splicing enhancers, and different cells may result in different fold increase of protein expression (Chang et al., 2006). (2014). doi: 10.3390/v12020130, Lu, G., Hu, Y., Wang, Q., Qi, J., Gao, F., Li, Y., et al. Immunisations can never be completely safe and there is always a risk of some side-effect. Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. It is critical to rapidly design and develop effective vaccines to prevent infection of this new coronavirus. 112, 24–31. doi: 10.1073/pnas.58.6.2268, Menachery, V. D., Mitchell, H. D., Cockrell, A. S., Gralinski, L. E., Yount, BL Jr, Graham, R. L., et al. doi: 10.1371/journal.pone.0081587, Du, L., Ma, C., and Jiang, S. (2013b). (2018). Human monoclonal antibodies against highly conserved HR1 and HR2 domains of the SARS-CoV spike protein are more broadly neutralizing. Although subunit vaccines based on the full-length S protein may elicit potent immune responses and/or protection, studies have found that antibodies induced by some of these vaccines mediate enhancement of viral infection in vitro, as in the case of SARS-CoV (Kam et al., 2007; Jaume et al., 2012), raising safety concerns for the development of full-length S protein-based subunit vaccines against SARS-CoV and MERS-CoV. Zhou, P., Yang, X. L., Wang, X. G., Hu, B., Zhang, L., Zhang, W., et al. Med. Emerg. This RBD protein induced long-term, high-level SARS-CoV S-specific antibodies and neutralizing antibodies that could be maintained for 12 months after immunization, protecting most of the vaccinated mice against SARS-CoV infection (Du et al., 2007). Adenoviral expression of a truncated S1 subunit of SARS-CoV spike protein results in specific humoral immune responses against SARS-CoV in rats. Identification of T-cell epitopes of SARS-coronavirus for development of peptide-based vaccines and cellular immunity assessment methods. 18(Suppl. Virus Res. (2020). Virol. Immunother. A line immunoassay utilizing recombinant nucleocapsid proteins for detection of antibodies to human coronaviruses. Biol. Lancet 361, 1773–1778. It is noted that the wild-type MERS-CoV RBD proteins consisting of the identified critical neutralizing domain confer partial protection of hDPP4-transgenic (hDPP4-Tg) mice from MERS-CoV infection without causing immunological toxicity or eosinophilic immune enhancement (Tai et al., 2016; Wang Y. et al., 2017; Nyon et al., 2018); nevertheless, a structurally designed mutant version of such RBD protein with a non-neutralizing epitope masked (T579N) preserves intact conformation and significantly improves overall neutralizing activity and protective efficacy, resulting in the full protection of hDPP4-Tg mice against high-dose MERS-CoV challenge (Du et al., 2016a). Nature [Epub ahead of print]. Advances in MERS-CoV vaccines and therapeutics based on the receptor-binding domain. 11, 1016–1020. Studies have revealed that a plant-expressed SARS-CoV N protein conjugated with Freund’s adjuvant elicited specific IgG antibodies, including IgG1 and IgG2a subtypes, and cellular immune responses in mice, whereas another E. coli-expressed N protein conjugated with Montanide ISA-51 and cysteine-phosphate-guanine (CpG) adjuvants induced specific IgG antibodies toward a Th1 (IgG2a)-type response in mice (Liu et al., 2006; Zheng et al., 2009).

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