Abstract
Coronaviruses are enveloped RNA viruses that generally cause mild disease in humans. However, the recently emerged coronavirus that caused severe acute respiratory syndrome (SARS-CoV) is the most pathogenic human coronavirus discovered to date. The SARS-CoV spike (S) protein mediates virus entry by binding cellular receptors and inducing fusion between the viral envelope and the host cell membrane. Coronavirus S proteins are palmitoylated, which may affect function. Here, we created a non-palmitoylated SARS-CoV S protein by mutating all nine cytoplasmic cysteine residues. Palmitoylation of SARS-CoV S was required for partitioning into detergent-resistant membranes and for cell-cell fusion. Surprisingly, however, palmitoylation of S was not required for interaction with SARS-CoV M protein. This contrasts with the requirement for palmitoylation of mouse hepatitis virus S protein for interaction with M protein and may point to important differences in assembly and infectivity of these two coronaviruses.
Original language | English (US) |
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Pages (from-to) | 139-148 |
Number of pages | 10 |
Journal | Virology |
Volume | 405 |
Issue number | 1 |
DOIs | |
State | Published - Sep 2010 |
Keywords
- Coronavirus
- Detergent-resistant membranes
- Fusion
- Palmitoylation
- SARS-CoV
- Spike
- Trafficking
ASJC Scopus subject areas
- Virology