Characterization of a Highly Conserved Domain within the Severe Acute Respiratory Syndrome Coronavirus Spike Protein S2 Domain with Characteristics of a Viral Fusion Peptide

• DOI: 10.1128/jvi.00079-09
• Publication Date: 2009-05-14T00:26:14Z
• Authors: Ikenna G. Madu; Shoshannah L. Roth; Sandrine Belouzard; Gary R. Whittaker
• Keywords: Coronavirus; Cleavage (geology); Cell fusion

Many viral fusion proteins are primed by proteolytic cleavage near their peptides. While the coronavirus (CoV) spike (S) protein is known to be cleaved at S1/S2 boundary, this site not closely linked a peptide. However, second has been identified in severe acute respiratory syndrome CoV (SARS-CoV) S2 domain (R797). Here, we investigated whether internal of exposes We show that residues immediately C-terminal SARS-CoV SFIEDLLFNKVTLADAGF very highly conserved across all CoVs. Mutagenesis studies these S, followed cell-cell and pseudotyped virion infectivity assays, showed critical role for L803, L804, F805 membrane fusion. Mutation most N-terminal residue (S798) had little or no effect on Biochemical analyses synthetic peptides corresponding proposed peptide also an important region indicated presence alpha-helical structure. propose within novel which may Coronaviridae.