Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for its fusion activity.
Identifieur interne : 006582 ( Main/Exploration ); précédent : 006581; suivant : 006583Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for its fusion activity.
Auteurs : R. Stauber [Allemagne] ; M. Pfleiderer ; S. SiddellSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1993.
Descripteurs français
- KwdFr :
- Animaux, Astrocytome, Cellules HeLa (microbiologie), Cellules cancéreuses en culture (microbiologie), Données de séquences moléculaires, Effet cytopathogène viral, Endopeptidases (métabolisme), Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Humains, Maturation post-traductionnelle des protéines, Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Souris, Séquence d'acides aminés, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (physiologie).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- microbiologie : Cellules HeLa, Cellules cancéreuses en culture.
- métabolisme : Endopeptidases, Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- physiologie : Virus de l'hépatite murine.
- Animaux, Astrocytome, Données de séquences moléculaires, Effet cytopathogène viral, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Humains, Maturation post-traductionnelle des protéines, Souris, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Astrocytoma, Cell Fusion, Cytopathogenic Effect, Viral, Endopeptidases (metabolism), HeLa Cells (microbiology), Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Molecular Sequence Data, Murine hepatitis virus (genetics), Murine hepatitis virus (physiology), Protein Processing, Post-Translational, Spike Glycoprotein, Coronavirus, Tumor Cells, Cultured (microbiology), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Endopeptidases, Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : Murine hepatitis virus.
- microbiology : HeLa Cells, Tumor Cells, Cultured.
- physiology : Murine hepatitis virus.
- Amino Acid Sequence, Animals, Astrocytoma, Cell Fusion, Cytopathogenic Effect, Viral, Humans, Mice, Molecular Sequence Data, Protein Processing, Post-Translational, Spike Glycoprotein, Coronavirus.
Abstract
The surface glycoprotein (S) of the murine hepatitis coronavirus MHV normally undergoes proteolytic cleavage during transport to the cell surface. To determine whether the cleavage of the MHV-JHM S glycoprotein is required to activate its ability to fuse cellular membranes, the protease recognition sequence in a cDNA copy of the S gene was altered from Arg-Arg-Ala-Arg-Arg into Ser-Val-Ser-Gly-Gly by site directed mutagenesis. The mutated and wild type S genes were expressed by means of recombinant vaccinia viruses and it could be shown that the mutated S protein was not cleaved when it was expressed in mouse DBT cells, in contrast to the wild type S protein. Nevertheless, the non-cleaved S protein induced extensive syncytium formation in mouse DBT cells. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus, proteolytic cleavage is not an absolute requirement for its fusion function.
DOI: 10.1007/978-1-4615-2996-5_26
PubMed: 8209724
Affiliations:
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Le document en format XML
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Stauber</name><affiliation wicri:level="4"><nlm:affiliation>Institut für Virologie, Universität Würzburg.</nlm:affiliation><country>Allemagne</country><placeName><settlement type="city">Wurtzbourg</settlement><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region></placeName><orgName type="university">Université de Wurtzbourg</orgName></affiliation></author><author><name sortKey="Pfleiderer, M" sort="Pfleiderer, M" uniqKey="Pfleiderer M" first="M" last="Pfleiderer">M. Pfleiderer</name></author><author><name sortKey="Siddell, S" sort="Siddell, S" uniqKey="Siddell S" first="S" last="Siddell">S. Siddell</name></author></analytic><series><title level="j">Advances in experimental medicine and biology</title><idno type="ISSN">0065-2598</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Astrocytoma</term><term>Cell Fusion</term><term>Cytopathogenic Effect, Viral</term><term>Endopeptidases (metabolism)</term><term>HeLa Cells (microbiology)</term><term>Humans</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Molecular Sequence Data</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (physiology)</term><term>Protein Processing, Post-Translational</term><term>Spike Glycoprotein, Coronavirus</term><term>Tumor Cells, Cultured (microbiology)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Astrocytome</term><term>Cellules HeLa (microbiologie)</term><term>Cellules cancéreuses en culture (microbiologie)</term><term>Données de séquences moléculaires</term><term>Effet cytopathogène viral</term><term>Endopeptidases (métabolisme)</term><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Souris</term><term>Séquence d'acides aminés</term><term>Virus de l'hépatite murine (génétique)</term><term>Virus de l'hépatite murine (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Endopeptidases</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Cellules HeLa</term><term>Cellules cancéreuses en culture</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>HeLa Cells</term><term>Tumor Cells, Cultured</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endopeptidases</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Astrocytoma</term><term>Cell Fusion</term><term>Cytopathogenic Effect, Viral</term><term>Humans</term><term>Mice</term><term>Molecular Sequence Data</term><term>Protein Processing, Post-Translational</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Astrocytome</term><term>Données de séquences moléculaires</term><term>Effet cytopathogène viral</term><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Souris</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The surface glycoprotein (S) of the murine hepatitis coronavirus MHV normally undergoes proteolytic cleavage during transport to the cell surface. To determine whether the cleavage of the MHV-JHM S glycoprotein is required to activate its ability to fuse cellular membranes, the protease recognition sequence in a cDNA copy of the S gene was altered from Arg-Arg-Ala-Arg-Arg into Ser-Val-Ser-Gly-Gly by site directed mutagenesis. The mutated and wild type S genes were expressed by means of recombinant vaccinia viruses and it could be shown that the mutated S protein was not cleaved when it was expressed in mouse DBT cells, in contrast to the wild type S protein. Nevertheless, the non-cleaved S protein induced extensive syncytium formation in mouse DBT cells. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus, proteolytic cleavage is not an absolute requirement for its fusion function.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Bavière</li><li>District de Basse-Franconie</li></region><settlement><li>Wurtzbourg</li></settlement><orgName><li>Université de Wurtzbourg</li></orgName></list><tree><noCountry><name sortKey="Pfleiderer, M" sort="Pfleiderer, M" uniqKey="Pfleiderer M" first="M" last="Pfleiderer">M. Pfleiderer</name><name sortKey="Siddell, S" sort="Siddell, S" uniqKey="Siddell S" first="S" last="Siddell">S. Siddell</name></noCountry><country name="Allemagne"><region name="Bavière"><name sortKey="Stauber, R" sort="Stauber, R" uniqKey="Stauber R" first="R" last="Stauber">R. Stauber</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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