SrasV1, PubMed, Curation, bibRecord, 003540

Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2.

Identifieur interne : 003540 ( PubMed/Curation ); précédent : 003539; suivant : 003541

Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2.

Auteurs : F. Taguchi [Japon]

Source :

Journal of virology [ 0022-538X ] ; 1993.

RBID : pubmed:8437210

Descripteurs français

KwdFr :
- Animaux, Cellules cultivées, Coronaviridae (génétique), Coronaviridae (métabolisme), Données de séquences moléculaires, Endopeptidases (métabolisme), Expression des gènes, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines (génétique), Glycoprotéines (métabolisme), Glycoprotéines membranaires, Maturation post-traductionnelle des protéines, Mutagenèse dirigée, Protéines de fusion virale (génétique), Protéines de fusion virale (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Relation structure-activité, Souris, Séquence d'acides aminés, Séquence nucléotidique, Tests aux précipitines, Transfection, Virus de la vaccine (génétique).
MESH :

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Cell Fusion, Cells, Cultured, Coronaviridae (genetics), Coronaviridae (metabolism), Endopeptidases (metabolism), Gene Expression, Glycoproteins (genetics), Glycoproteins (metabolism), Membrane Glycoproteins, Mice, Molecular Sequence Data, Mutagenesis, Site-Directed, Precipitin Tests, Protein Processing, Post-Translational, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Transfection, Vaccinia virus (genetics), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Fusion Proteins (genetics), Viral Fusion Proteins (metabolism).
MESH :
- chemical , genetics : Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- chemical , metabolism : Endopeptidases, Glycoproteins, Viral Envelope Proteins, Viral Fusion Proteins.
- genetics : Coronaviridae, Vaccinia virus.
- metabolism : Coronaviridae.
- Amino Acid Sequence, Animals, Base Sequence, Cell Fusion, Cells, Cultured, Gene Expression, Membrane Glycoproteins, Mice, Molecular Sequence Data, Mutagenesis, Site-Directed, Precipitin Tests, Protein Processing, Post-Translational, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Transfection.

Abstract

The fusogenic properties of the uncleaved spike (S) protein of murine coronavirus JHMV variant cl-2 were studied by expressing the S protein with a deleted putative cleavage site. The amino acid sequence of the putative cleavage site, Arg-Arg-Ala-Arg-Arg, was replaced by Arg-Thr-Ala-Leu-Glu by in vitro mutagenesis of the cl-2 S protein cDNA. Recombinant vaccinia viruses containing the cl-2 S cDNA [RVV t(+)] or the mutated cDNA [RVV t(-)] were constructed and monitored for fusion formation and cleavage of the expressed S proteins. When cultured DBT cells were infected with RVV t(+) at a multiplicity of infection of 0.5, fusion formation was first observed at 10 to 12 h postinoculation and spread throughout the whole culture by 20 to 24 h postinoculation. In cells infected with RVV t(-) under the same conditions, fusion formation appeared by 12 to 14 h. This result represented a 2- to 4-h delay in the onset of fusion, compared with its appearance in cells expressing the wild-type S protein. By 25 to 30 h, most of the cells infected by RVV t(-) had fused. By immunoprecipitation and Western blotting (immunoblotting), the 170-kDa S protein was detected in DBT cells expressing the wild-type S protein and the mutated S protein. However, interestingly, the cleavage products of the S protein, S1 and S2, were not detected in RVV t(-)-infected cells, producing the mutated S protein, even though fusion was clearly visible. Both products were, of course, detected in RVV t(+)-infected DBT cells, producing the wild-type S protein. The same results concerning the fusion formation and cleavage properties of the S proteins were reproduced by the transiently expressed S proteins. These results suggest that the cleavage event in the S protein of murine coronavirus JHMV is not a prerequisite for fusion formation but that it does facilitate fusion formation.

PubMed: 8437210

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<front><div type="abstract" xml:lang="en">The fusogenic properties of the uncleaved spike (S) protein of murine coronavirus JHMV variant cl-2 were studied by expressing the S protein with a deleted putative cleavage site. The amino acid sequence of the putative cleavage site, Arg-Arg-Ala-Arg-Arg, was replaced by Arg-Thr-Ala-Leu-Glu by in vitro mutagenesis of the cl-2 S protein cDNA. Recombinant vaccinia viruses containing the cl-2 S cDNA [RVV t(+)] or the mutated cDNA [RVV t(-)] were constructed and monitored for fusion formation and cleavage of the expressed S proteins. When cultured DBT cells were infected with RVV t(+) at a multiplicity of infection of 0.5, fusion formation was first observed at 10 to 12 h postinoculation and spread throughout the whole culture by 20 to 24 h postinoculation. In cells infected with RVV t(-) under the same conditions, fusion formation appeared by 12 to 14 h. This result represented a 2- to 4-h delay in the onset of fusion, compared with its appearance in cells expressing the wild-type S protein. By 25 to 30 h, most of the cells infected by RVV t(-) had fused. By immunoprecipitation and Western blotting (immunoblotting), the 170-kDa S protein was detected in DBT cells expressing the wild-type S protein and the mutated S protein. However, interestingly, the cleavage products of the S protein, S1 and S2, were not detected in RVV t(-)-infected cells, producing the mutated S protein, even though fusion was clearly visible. Both products were, of course, detected in RVV t(+)-infected DBT cells, producing the wild-type S protein. The same results concerning the fusion formation and cleavage properties of the S proteins were reproduced by the transiently expressed S proteins. These results suggest that the cleavage event in the S protein of murine coronavirus JHMV is not a prerequisite for fusion formation but that it does facilitate fusion formation.</div>
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<ArticleTitle>Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2.</ArticleTitle>
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<Abstract><AbstractText>The fusogenic properties of the uncleaved spike (S) protein of murine coronavirus JHMV variant cl-2 were studied by expressing the S protein with a deleted putative cleavage site. The amino acid sequence of the putative cleavage site, Arg-Arg-Ala-Arg-Arg, was replaced by Arg-Thr-Ala-Leu-Glu by in vitro mutagenesis of the cl-2 S protein cDNA. Recombinant vaccinia viruses containing the cl-2 S cDNA [RVV t(+)] or the mutated cDNA [RVV t(-)] were constructed and monitored for fusion formation and cleavage of the expressed S proteins. When cultured DBT cells were infected with RVV t(+) at a multiplicity of infection of 0.5, fusion formation was first observed at 10 to 12 h postinoculation and spread throughout the whole culture by 20 to 24 h postinoculation. In cells infected with RVV t(-) under the same conditions, fusion formation appeared by 12 to 14 h. This result represented a 2- to 4-h delay in the onset of fusion, compared with its appearance in cells expressing the wild-type S protein. By 25 to 30 h, most of the cells infected by RVV t(-) had fused. By immunoprecipitation and Western blotting (immunoblotting), the 170-kDa S protein was detected in DBT cells expressing the wild-type S protein and the mutated S protein. However, interestingly, the cleavage products of the S protein, S1 and S2, were not detected in RVV t(-)-infected cells, producing the mutated S protein, even though fusion was clearly visible. Both products were, of course, detected in RVV t(+)-infected DBT cells, producing the wild-type S protein. The same results concerning the fusion formation and cleavage properties of the S proteins were reproduced by the transiently expressed S proteins. These results suggest that the cleavage event in the S protein of murine coronavirus JHMV is not a prerequisite for fusion formation but that it does facilitate fusion formation.</AbstractText>
</Abstract>
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<ReferenceList><Reference><Citation>J Virol. 1985 Dec;56(3):904-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2999443</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1992 May;73 ( Pt 5):1065-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1316938</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1974 Feb;57(2):475-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4361457</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1981 Sep;113(2):503-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6267795</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1981 Mar;53(Pt 1):145-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7276911</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1981;142:133-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6278876</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1982 Jun;119(2):358-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6281979</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1983 Apr;64 (Pt 4):761-76</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6300299</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Adv Exp Med Biol. 1984;173:25-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6331116</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1984 Nov;65 ( Pt 11):1931-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6209363</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1985 May;54(2):429-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2985806</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1985 Dec;56(3):912-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2999444</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1986 Jun;58(3):869-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3701929</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1986 Aug;59(2):463-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3016306</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1986 Oct 23-29;323(6090):725-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3095663</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1987 Jan;68 ( Pt 1):47-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3027248</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1987 Oct;68 ( Pt 10):2639-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3312491</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1988 Jan;69 ( Pt 1):87-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2447229</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 1988 Apr 8;53(1):55-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2450679</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 1988 Dec;69 ( Pt 12):2939-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3058868</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1989 Mar;63(3):1408-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2464703</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Mar;169(1):127-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2538027</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Mar;169(1):233-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2538034</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Aug;171(2):493-502</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2548329</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Jan;64(1):339-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2403441</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1989 Dec;173(2):664-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2556846</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1990 Apr;175(2):372-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2183466</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Physiol. 1990;52:675-97</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2184772</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1990 Jun;64(6):3051-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1692350</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 Jan;65(1):254-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1985201</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1991 Feb;180(2):567-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1846489</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 Apr;65(4):1916-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1848311</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1991 Jul 1;88(13):5533-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1648219</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 Oct;65(10):5584-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1654453</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virus Res. 1991 Jun;20(1):45-58</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1656623</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1991 Dec;65(12):6881-91</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1719235</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Virology. 1992 Mar;187(1):178-88</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1310555</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1973 Dec;12(6):1457-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">4357516</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2.

Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2.

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