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Virology. 2009 Oct 25;393(2):265-71. doi: 10.1016/j.virol.2009.07.038. Epub 2009 Aug 29.

SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.

Author information

1
C4127 Veterinary Medical Center, Department of Microbiology and Immunology, Cornell University, Ithaca NY 14853, USA.

Abstract

The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1-S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822-C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell-cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.

PMID:
19717178
PMCID:
PMC3594805
DOI:
10.1016/j.virol.2009.07.038
[Indexed for MEDLINE]
Free PMC Article

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