Coronaviruses represent current and emerging threats for many species, including humans. Middle East respiratory syndrome-related coronavirus (MERS-CoV) is responsible for sporadic infections in mostly Middle Eastern countries, with occasional transfer elsewhere. A key step in the MERS-CoV replication cycle is the fusion of the virus and host cell membranes mediated by the virus spike protein, S. The location of the fusion peptide within the MERS S protein has not been precisely mapped. We used isolated peptides and giant unilamellar vesicles (GUV) to demonstrate membrane binding for a peptide located near the N-terminus of the S2 domain. Key residues required for activity were mapped by amino acid replacement and their relevance in vitro tested by their introduction into recombinant MERS S protein expressed in mammalian cells. Mutations preventing membrane binding in vitro also abolished S-mediated syncytium formation consistent with the identified peptide acting as the fusion peptide for the S protein of MERS-CoV.
【저자키워드】 coronavirus, peptide, MERS, Spike protein, membrane, fusion assay, 【초록키워드】 S protein, threat, Infection, in vitro, virus, MERS-CoV, Replication, humans, fusion peptide, binding, Amino acid, Middle East, host cell membrane, residue, transfer, mammalian cells, middle, N-terminus, virus spike protein, S2 domain, syncytium formation, Giant, Vesicle, responsible, tested, required, expressed, the S protein, mapped, acting, 【제목키워드】 fusion, the Spike,