Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus.
Identifieur interne : 006516 ( Main/Exploration ); précédent : 006515; suivant : 006517Point mutations in the S protein connect the sialic acid binding activity with the enteropathogenicity of transmissible gastroenteritis coronavirus.
Auteurs : C. Krempl [Allemagne] ; B. Schultze ; H. Laude ; G. HerrlerSource :
- Journal of virology [ 0022-538X ] ; 1997.
Descripteurs français
- KwdFr :
- Acides sialiques (métabolisme), Animaux, Cellules LLC-PK1, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Hémagglutinines (métabolisme), Lignée cellulaire, Mutation ponctuelle, Mâle, Poulets, Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (métabolisme), Sialidase (pharmacologie), Suidae, Virus de la gastroentérite transmissible (génétique), Virus de la gastroentérite transmissible (métabolisme), Virus de la gastroentérite transmissible (pathogénicité).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de la gastroentérite transmissible.
- métabolisme : Acides sialiques, Glycoprotéines membranaires, Hémagglutinines, Protéines de l'enveloppe virale, Récepteurs viraux, Virus de la gastroentérite transmissible.
- pathogénicité : Virus de la gastroentérite transmissible.
- pharmacologie : Sialidase.
- Animaux, Cellules LLC-PK1, Glycoprotéine de spicule des coronavirus, Lignée cellulaire, Mutation ponctuelle, Mâle, Poulets, Suidae.
English descriptors
- KwdEn :
- Animals, Cell Line, Chickens, Hemagglutinins (metabolism), LLC-PK1 Cells, Male, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Neuraminidase (pharmacology), Point Mutation, Receptors, Virus (metabolism), Sialic Acids (metabolism), Spike Glycoprotein, Coronavirus, Swine, Transmissible gastroenteritis virus (genetics), Transmissible gastroenteritis virus (metabolism), Transmissible gastroenteritis virus (pathogenicity), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Hemagglutinins, Membrane Glycoproteins, Receptors, Virus, Sialic Acids, Viral Envelope Proteins.
- chemical , pharmacology : Neuraminidase.
- genetics : Transmissible gastroenteritis virus.
- metabolism : Transmissible gastroenteritis virus.
- pathogenicity : Transmissible gastroenteritis virus.
- Animals, Cell Line, Chickens, LLC-PK1 Cells, Male, Point Mutation, Spike Glycoprotein, Coronavirus, Swine.
Abstract
Enteropathogenic transmissible gastroenteritis virus (TGEV), a porcine coronavirus, is able to agglutinate erythrocytes because of sialic acid binding activity. Competitive inhibitors that may mask the sialic acid binding activity can be inactivated by sialidase treatment of virions. Here, we show that TGEV virions with efficient hemagglutinating activity were also obtained when cells were treated with sialidase prior to infection. This method was used to analyze TGEV mutants for hemagglutinating activity. Recently, mutants with strongly reduced enteropathogenicity that have point mutations or a deletion of four amino acids within residues 145 to 155 of the S protein have been described. Here, we show that in addition to their reduced pathogenicity, these mutants also have lost hemagglutinating activity. These results connect sialic acid binding activity with the enteropathogenicity of TGEV.
PubMed: 9060696
Affiliations:
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Le document en format XML
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Krempl</name><affiliation wicri:level="1"><nlm:affiliation>Institut für Virologie, Philipps-Universität Marburg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Philipps-Universität Marburg</wicri:regionArea><wicri:noRegion>Philipps-Universität Marburg</wicri:noRegion><wicri:noRegion>Philipps-Universität Marburg</wicri:noRegion><wicri:noRegion>Philipps-Universität Marburg</wicri:noRegion></affiliation></author><author><name sortKey="Schultze, B" sort="Schultze, B" uniqKey="Schultze B" first="B" last="Schultze">B. Schultze</name></author><author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name></author><author><name sortKey="Herrler, G" sort="Herrler, G" uniqKey="Herrler G" first="G" last="Herrler">G. 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Competitive inhibitors that may mask the sialic acid binding activity can be inactivated by sialidase treatment of virions. Here, we show that TGEV virions with efficient hemagglutinating activity were also obtained when cells were treated with sialidase prior to infection. This method was used to analyze TGEV mutants for hemagglutinating activity. Recently, mutants with strongly reduced enteropathogenicity that have point mutations or a deletion of four amino acids within residues 145 to 155 of the S protein have been described. Here, we show that in addition to their reduced pathogenicity, these mutants also have lost hemagglutinating activity. These results connect sialic acid binding activity with the enteropathogenicity of TGEV.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Herrler, G" sort="Herrler, G" uniqKey="Herrler G" first="G" last="Herrler">G. Herrler</name><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name><name sortKey="Schultze, B" sort="Schultze, B" uniqKey="Schultze B" first="B" last="Schultze">B. Schultze</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Krempl, C" sort="Krempl, C" uniqKey="Krempl C" first="C" last="Krempl">C. Krempl</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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