SrasV1, PubMed, Checkpoint, bibRecord, 001801

Role of spike protein endodomains in regulating coronavirus entry.

Identifieur interne : 001801 ( PubMed/Checkpoint ); précédent : 001800; suivant : 001802

Role of spike protein endodomains in regulating coronavirus entry.

Auteurs : Ana Shulla [États-Unis] ; Tom Gallagher

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2009.

RBID : pubmed:19801669

Descripteurs français

KwdFr :
- Acide palmitique (), Animaux, Cellules HeLa, Coronavirus (pathogénicité), Cystéine (), Données de séquences moléculaires, Fibroblastes (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (physiologie), Humains, Liaison aux protéines, Lipides (), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (physiologie), Souris, Structure tertiaire des protéines, Séquence d'acides aminés.
MESH :
- métabolisme : Fibroblastes.
- pathogénicité : Coronavirus.
- physiologie : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- Acide palmitique, Animaux, Cellules HeLa, Cystéine, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Lipides, Protéines de l'enveloppe virale, Souris, Structure tertiaire des protéines, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Coronavirus (pathogenicity), Cysteine (chemistry), Fibroblasts (metabolism), HeLa Cells, Humans, Lipids (chemistry), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (physiology), Mice, Molecular Sequence Data, Palmitic Acid (chemistry), Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (physiology).
MESH :
- chemical , chemistry : Cysteine, Lipids, Membrane Glycoproteins, Palmitic Acid, Viral Envelope Proteins.
- metabolism : Fibroblasts.
- pathogenicity : Coronavirus.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- Amino Acid Sequence, Animals, HeLa Cells, Humans, Mice, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus.

Abstract

Enveloped viruses enter cells by viral glycoprotein-mediated binding to host cells and subsequent fusion of virus and host cell membranes. For the coronaviruses, viral spike (S) proteins execute these cell entry functions. The S proteins are set apart from other viral and cellular membrane fusion proteins by their extensively palmitoylated membrane-associated tails. Palmitate adducts are generally required for protein-mediated fusions, but their precise roles in the process are unclear. To obtain additional insights into the S-mediated membrane fusion process, we focused on these acylated carboxyl-terminal intravirion tails. Substituting alanines for the cysteines that are subject to palmitoylation had effects on both S incorporation into virions and S-mediated membrane fusions. In specifically dissecting the effects of endodomain mutations on the fusion process, we used antiviral heptad repeat peptides that bind only to folding intermediates in the S-mediated fusion process and found that mutants lacking three palmitoylated cysteines remained in transitional folding states nearly 10 times longer than native S proteins. This slower refolding was also reflected in the paucity of postfusion six-helix bundle configurations among the mutant S proteins. Viruses with fewer palmitoylated S protein cysteines entered cells slowly and had reduced specific infectivities. These findings indicate that lipid adducts anchoring S proteins into virus membranes are necessary for the rapid, productive S protein refolding events that culminate in membrane fusions. These studies reveal a previously unappreciated role for covalently attached lipids on the endodomains of viral proteins eliciting membrane fusion reactions.

DOI: 10.1074/jbc.M109.043547
PubMed: 19801669

Affiliations:

États-Unis

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pubmed:19801669

Le document en format XML

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<front><div type="abstract" xml:lang="en">Enveloped viruses enter cells by viral glycoprotein-mediated binding to host cells and subsequent fusion of virus and host cell membranes. For the coronaviruses, viral spike (S) proteins execute these cell entry functions. The S proteins are set apart from other viral and cellular membrane fusion proteins by their extensively palmitoylated membrane-associated tails. Palmitate adducts are generally required for protein-mediated fusions, but their precise roles in the process are unclear. To obtain additional insights into the S-mediated membrane fusion process, we focused on these acylated carboxyl-terminal intravirion tails. Substituting alanines for the cysteines that are subject to palmitoylation had effects on both S incorporation into virions and S-mediated membrane fusions. In specifically dissecting the effects of endodomain mutations on the fusion process, we used antiviral heptad repeat peptides that bind only to folding intermediates in the S-mediated fusion process and found that mutants lacking three palmitoylated cysteines remained in transitional folding states nearly 10 times longer than native S proteins. This slower refolding was also reflected in the paucity of postfusion six-helix bundle configurations among the mutant S proteins. Viruses with fewer palmitoylated S protein cysteines entered cells slowly and had reduced specific infectivities. These findings indicate that lipid adducts anchoring S proteins into virus membranes are necessary for the rapid, productive S protein refolding events that culminate in membrane fusions. These studies reveal a previously unappreciated role for covalently attached lipids on the endodomains of viral proteins eliciting membrane fusion reactions.</div>
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<ReferenceList><Reference><Citation>Cell. 1994 Jan 28;76(2):383-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8293471</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Crit Rev Biochem Mol Biol. 2008 May-Jun;43(3):189-219</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18568847</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2008 Jul 1;47(26):6802-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18540634</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Mar;82(6):2989-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18184706</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2008 Apr 8;105(14):5384-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18378904</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2008 Jun;82(11):5417-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18353944</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2002 Sep 13;297(5588):1877-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12228719</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Dec;76(23):11819-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12414924</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 Jan;77(2):830-40</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12502799</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 2003 Mar;14(3):926-38</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12631714</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2003 May 30;300(5624):1394-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730500</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2003;72:175-207</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14527322</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2003 Nov;77(21):11312-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14557617</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4240-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15010527</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 May 14;279(20):20836-49</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14996844</ArticleId>
</ArticleIdList>
</Reference>
<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>
<Reference><Citation>J Biol Chem. 2004 Jul 16;279(29):30514-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15123674</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2008 Jul;15(7):675-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18596814</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2008 Jul;15(7):690-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18596815</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2009 Feb 13;386(1):14-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19121325</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Aug;83(15):7411-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19439480</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Feb;74(3):1393-406</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10627550</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 Apr;74(7):3264-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10708443</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2000 Mar 30;269(1):212-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10725213</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2000 May;74(10):4634-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10775599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2000;69:531-69</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10966468</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 2000 Oct 16;151(2):413-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11038187</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13523-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11095714</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2000 Nov 10;103(4):679-89</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11106737</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2001 Mar;75(6):2792-802</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11222703</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13925-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11717449</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 2001;494:205-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11774470</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 May;76(9):4603-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11932425</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1994 Jan;124(1-2):55-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8294506</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1994 Aug 1;202(2):814-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8030244</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9871-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7568235</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biol. 1995 Oct;131(2):339-49</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7593163</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1996 Jan;70(1):248-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8523533</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1995 Dec 20;214(2):453-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8553547</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1997 Apr;71(4):3129-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9060676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1998 Feb;72(2):1224-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9445022</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1998 Apr;72(4):3278-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9525655</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Biol. 1998 Apr;5(4):276-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9546217</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1998 May 29;93(5):681-4</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9630213</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1998 Oct 10;250(1):140-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9770428</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1999 Feb 5;274(6):3910-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9920947</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Biol Cell. 1999 Jun;10(6):1821-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10359599</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1999 Sep;73(9):7441-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10438834</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Jan;79(1):106-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15596806</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Curr Top Microbiol Immunol. 2005;287:133-59</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15609511</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):17958-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15604146</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2005 Apr 10;334(2):306-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15780881</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2005 Jun 10;308(5728):1643-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15831716</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15964978</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Oct;79(19):12231-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16160149</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Nov;79(21):13673-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16227287</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Feb;80(3):1280-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16415005</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Feb;80(3):1302-10</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16415007</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2006 Jun;80(12):5768-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16731916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2006 Jun 15;441(7095):847-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16728975</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Struct Biol. 2006 Aug;155(2):162-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16765058</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 2006;581:163-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17037525</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2007 Feb 15;445(7129):732-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17301785</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 2007 Apr 10;360(2):264-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17134730</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Mol Life Sci. 2007 Apr;64(7-8):850-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17429580</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2008 Feb;9(2):112-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18216768</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Sep;78(18):9904-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15331724</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Membr Biol. 2004 May 1;199(1):1-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15366419</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Mol Biol. 2005;292:187-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15507709</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Infect Immun. 1972 Oct;6(4):501-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4564284</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1973 Apr;52(2):456-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4705382</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1978 Jul;14(3):725-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">210957</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Am J Vet Res. 1981 Mar;42(3):368-77</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6267960</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1981 Oct;78(10):6023-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6947213</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1983 Dec;131(2):296-307</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6318433</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Cell Biol. 1984 Mar;33(2):281-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6325194</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1987 Aug 20;196(4):963-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3681988</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Nov;64(11):5367-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2170676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Dec;64(12):6314-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2243396</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 May;65(5):2491-500</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1901916</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Gene. 1991 Dec 15;108(2):193-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1660837</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Role of spike protein endodomains in regulating coronavirus entry.

Role of spike protein endodomains in regulating coronavirus entry.

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