Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion.
Identifieur interne : 002598 ( PubMed/Corpus ); précédent : 002597; suivant : 002599Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion.
Auteurs : Chad M. Petit ; Jeffrey M. Melancon ; Vladimir N. Chouljenko ; Robin Colgrove ; Michael Farzan ; David M. Knipe ; K G KousoulasSource :
- Virology [ 0042-6822 ] ; 2005.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Fusion, Cell Membrane (chemistry), Chlorocebus aethiops, Immunohistochemistry, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Membrane Glycoproteins (physiology), Molecular Sequence Data, Point Mutation, Protein Structure, Tertiary, Protein Transport, SARS Virus (genetics), SARS Virus (physiology), Sequence Deletion, Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (physiology), Viral Fusion Proteins (analysis).
- MESH :
- chemical , analysis : Viral Fusion Proteins.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : Cell Membrane.
- chemical , genetics : Membrane Glycoproteins, SARS Virus, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, SARS Virus, Viral Envelope Proteins.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Fusion, Chlorocebus aethiops, Immunohistochemistry, Membrane Fusion, Molecular Sequence Data, Point Mutation, Protein Structure, Tertiary, Protein Transport, Sequence Deletion, Spike Glycoprotein, Coronavirus, Vero Cells.
Abstract
The SARS-coronavirus (SARS-CoV) is the etiological agent of severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. To delineate functional domains of the SARS-CoV S glycoprotein, single point mutations, cluster-to-lysine and cluster-to-alanine mutations, as well as carboxyl-terminal truncations were investigated in transient expression experiments. Mutagenesis of either the coiled-coil domain of the S glycoprotein amino terminal heptad repeat, the predicted fusion peptide, or an adjacent but distinct region, severely compromised S-mediated cell-to-cell fusion, while intracellular transport and cell-surface expression were not adversely affected. Surprisingly, a carboxyl-terminal truncation of 17 amino acids substantially increased S glycoprotein-mediated cell-to-cell fusion suggesting that the terminal 17 amino acids regulated the S fusogenic properties. In contrast, truncation of 26 or 39 amino acids eliminating either one or both of the two endodomain cysteine-rich motifs, respectively, inhibited cell fusion in comparison to the wild-type S. The 17 and 26 amino-acid deletions did not adversely affect S cell-surface expression, while the 39 amino-acid truncation inhibited S cell-surface expression suggesting that the membrane proximal cysteine-rich motif plays an essential role in S cell-surface expression. Mutagenesis of the acidic amino-acid cluster in the carboxyl terminus of the S glycoprotein as well as modification of a predicted phosphorylation site within the acidic cluster revealed that this amino-acid motif may play a functional role in the retention of S at cell surfaces. This genetic analysis reveals that the SARS-CoV S glycoprotein contains extracellular domains that regulate cell fusion as well as distinct endodomains that function in intracellular transport, cell-surface expression, and cell fusion.
DOI: 10.1016/j.virol.2005.06.046
PubMed: 16099010
Links to Exploration step
pubmed:16099010Le document en format XML
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<front><div type="abstract" xml:lang="en">The SARS-coronavirus (SARS-CoV) is the etiological agent of severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. To delineate functional domains of the SARS-CoV S glycoprotein, single point mutations, cluster-to-lysine and cluster-to-alanine mutations, as well as carboxyl-terminal truncations were investigated in transient expression experiments. Mutagenesis of either the coiled-coil domain of the S glycoprotein amino terminal heptad repeat, the predicted fusion peptide, or an adjacent but distinct region, severely compromised S-mediated cell-to-cell fusion, while intracellular transport and cell-surface expression were not adversely affected. Surprisingly, a carboxyl-terminal truncation of 17 amino acids substantially increased S glycoprotein-mediated cell-to-cell fusion suggesting that the terminal 17 amino acids regulated the S fusogenic properties. In contrast, truncation of 26 or 39 amino acids eliminating either one or both of the two endodomain cysteine-rich motifs, respectively, inhibited cell fusion in comparison to the wild-type S. The 17 and 26 amino-acid deletions did not adversely affect S cell-surface expression, while the 39 amino-acid truncation inhibited S cell-surface expression suggesting that the membrane proximal cysteine-rich motif plays an essential role in S cell-surface expression. Mutagenesis of the acidic amino-acid cluster in the carboxyl terminus of the S glycoprotein as well as modification of a predicted phosphorylation site within the acidic cluster revealed that this amino-acid motif may play a functional role in the retention of S at cell surfaces. This genetic analysis reveals that the SARS-CoV S glycoprotein contains extracellular domains that regulate cell fusion as well as distinct endodomains that function in intracellular transport, cell-surface expression, and cell fusion.</div>
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<Abstract><AbstractText>The SARS-coronavirus (SARS-CoV) is the etiological agent of severe acute respiratory syndrome (SARS). The SARS-CoV spike (S) glycoprotein mediates membrane fusion events during virus entry and virus-induced cell-to-cell fusion. To delineate functional domains of the SARS-CoV S glycoprotein, single point mutations, cluster-to-lysine and cluster-to-alanine mutations, as well as carboxyl-terminal truncations were investigated in transient expression experiments. Mutagenesis of either the coiled-coil domain of the S glycoprotein amino terminal heptad repeat, the predicted fusion peptide, or an adjacent but distinct region, severely compromised S-mediated cell-to-cell fusion, while intracellular transport and cell-surface expression were not adversely affected. Surprisingly, a carboxyl-terminal truncation of 17 amino acids substantially increased S glycoprotein-mediated cell-to-cell fusion suggesting that the terminal 17 amino acids regulated the S fusogenic properties. In contrast, truncation of 26 or 39 amino acids eliminating either one or both of the two endodomain cysteine-rich motifs, respectively, inhibited cell fusion in comparison to the wild-type S. The 17 and 26 amino-acid deletions did not adversely affect S cell-surface expression, while the 39 amino-acid truncation inhibited S cell-surface expression suggesting that the membrane proximal cysteine-rich motif plays an essential role in S cell-surface expression. Mutagenesis of the acidic amino-acid cluster in the carboxyl terminus of the S glycoprotein as well as modification of a predicted phosphorylation site within the acidic cluster revealed that this amino-acid motif may play a functional role in the retention of S at cell surfaces. This genetic analysis reveals that the SARS-CoV S glycoprotein contains extracellular domains that regulate cell fusion as well as distinct endodomains that function in intracellular transport, cell-surface expression, and cell fusion.</AbstractText>
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<ReferenceList><Reference><Citation>Nature. 2003 Nov 27;426(6965):450-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14647384</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Science. 1992 Nov 6;258(5084):917-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1439803</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2003 Jan;77(2):841-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12502800</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell. 1998 Dec 23;95(7):871-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9875840</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Exp Med. 2000 Jul 3;192(1):11-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10880522</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Science. 2003 Jun 13;300(5626):1763-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12746549</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 1997 May 22;387(6631):426-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9163431</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Cell Biol. 2000 Oct 16;151(2):413-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11038187</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Annu Rev Biochem. 2001;70:777-810</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11395423</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 Oct;78(19):10328-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15367599</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proteomics. 2004 Feb;4(2):492-504</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14760722</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1987 Aug 20;196(4):963-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3681988</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell Res. 2004 Oct;14(5):400-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15450134</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1953-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690092</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2003 Jan;77(2):830-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12502799</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8455-60</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15150417</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1948-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12748314</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 Jun;78(11):5913-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15140989</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Methods Mol Biol. 1996;57:177-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8850005</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Cell Biol. 1996 Oct;135(1):73-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8858164</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 2003 Aug 29;331(5):991-1004</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12927536</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2004 May 14;279(20):20836-49</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14996844</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Mol Cell. 1998 Nov;2(5):605-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9844633</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Annu Rev Cell Dev Biol. 1996;12:627-61</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8970739</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Gen Virol. 1993 Feb;74 ( Pt 2):183-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8381459</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2003 Jan;77(1):167-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12477822</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 1995 Jul 10;210(2):264-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7618266</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8709-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15161975</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>EMBO J. 1998 Aug 17;17(16):4572-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9707417</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>N Engl J Med. 2003 May 15;348(20):1967-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12690091</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell. 1997 Apr 18;89(2):263-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9108481</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Struct Biol. 1995 Dec;2(12):1075-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8846219</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2002 Sep 30;301(2):322-333</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12359434</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 May;78(10):5347-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15113914</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Mol Biol. 1999 Dec 17;294(5):1351-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10600390</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2004 Nov 19;279(47):49414-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15345712</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1996 Oct;70(10):6563-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8794291</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nature. 1994 Sep 1;371(6492):37-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8072525</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2000 Mar 30;269(1):212-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10725213</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9217-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15197264</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Mol Cell. 1999 Mar;3(3):309-19</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10198633</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 Sep;78(18):9904-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15331724</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1993 Aug;67(8):4504-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8392595</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1999 May;73(5):4372-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10196335</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1997 Dec;71(12):9427-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9371603</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>EMBO J. 2001 Aug 1;20(15):4024-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11483506</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12303-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9356444</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Mol Cell Proteomics. 2003 May;2(5):346-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12775768</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell. 2001 Apr 6;105(1):137-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11301009</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 1995 Dec 20;214(2):453-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8553547</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2004 Oct 15;279(42):43661-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15304515</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1998 May 26;95(11):6032-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9600912</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1995 Nov;69(11):7045-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7474124</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Lancet. 2003 Apr 19;361(9366):1319-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12711465</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
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