Abstract
The spike projecting from the virion of mouse hepatitis virus (MHV) is composed of a spike (S) glycoprotein with 180 to 200 kDa. The S protein is cleaved into N-terminal S1 and C-terminal S2 subunits. The S1 forms the globular part of the spike and the S2 its stalk portion. An important biological function of the S protein is binding to the virus receptor, which is mediated by a domain located in the N terminal 330 residues of the S1 (S1N330) (Kubo et al., 1994). Virus-cell fusion is also mediated by the S protein (Collins et al., 1982). Various regions in the S2 are involved in fusion activity. A candidate fusion peptide was reported to reside in the S2 (Luo and Weiss, 1998).
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Taguchi, F., Shimazaki, Y.K. (2001). Involvement in Fusion Activity of an Epitope in the S2 Subunit of Murine Coronavirus Spike Protein. In: Lavi, E., Weiss, S.R., Hingley, S.T. (eds) The Nidoviruses. Advances in Experimental Medicine and Biology, vol 494. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1325-4_34
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