Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein.
Identifieur interne : 001154 ( Ncbi/Checkpoint ); précédent : 001153; suivant : 001155Rescue of vector-expressed fowl plague virus hemagglutinin in biologically active form by acidotropic agents and coexpressed M2 protein.
Auteurs : M. Ohuchi [Allemagne] ; A. Cramer ; M. Vey ; R. Ohuchi ; W. Garten ; H D KlenkSource :
- Journal of virology [ 0022-538X ] ; 1994.
Descripteurs français
- KwdFr :
- Animaux, Cellules cultivées, Chlorure d'ammonium (pharmacologie), Concentration en ions d'hydrogène, Données de séquences moléculaires, Fusion cellulaire (), Glycoprotéine hémagglutinine du virus influenza, Hémagglutinines virales (biosynthèse), Hémagglutinines virales (génétique), Hémagglutinines virales (isolement et purification), Protéines de fusion virale (biosynthèse), Protéines de fusion virale (génétique), Protéines de la matrice virale (biosynthèse), Protéines de la matrice virale (génétique), Protéines de la matrice virale (pharmacologie), Protéines membranaires (biosynthèse), Protéines recombinantes (biosynthèse), Séquence nucléotidique, Technique d'immunofluorescence, Transport biologique, Virus de la grippe A (génétique), Virus de la grippe A (métabolisme), Virus simien 40 (génétique).
- MESH :
- biosynthèse : Hémagglutinines virales, Protéines de fusion virale, Protéines de la matrice virale, Protéines membranaires, Protéines recombinantes.
- génétique : Hémagglutinines virales, Protéines de fusion virale, Protéines de la matrice virale, Virus de la grippe A, Virus simien 40.
- isolement et purification : Hémagglutinines virales.
- métabolisme : Virus de la grippe A.
- pharmacologie : Chlorure d'ammonium, Protéines de la matrice virale.
- Animaux, Cellules cultivées, Concentration en ions d'hydrogène, Données de séquences moléculaires, Fusion cellulaire, Glycoprotéine hémagglutinine du virus influenza, Séquence nucléotidique, Technique d'immunofluorescence, Transport biologique.
English descriptors
- KwdEn :
- Ammonium Chloride (pharmacology), Animals, Base Sequence, Biological Transport, Cell Fusion (drug effects), Cells, Cultured, Chlorocebus aethiops, Fluorescent Antibody Technique, Hemagglutinin Glycoproteins, Influenza Virus, Hemagglutinins, Viral (biosynthesis), Hemagglutinins, Viral (genetics), Hemagglutinins, Viral (isolation & purification), Hydrogen-Ion Concentration, Influenza A virus (genetics), Influenza A virus (metabolism), Membrane Proteins (biosynthesis), Molecular Sequence Data, Recombinant Proteins (biosynthesis), Simian virus 40 (genetics), Viral Fusion Proteins (biosynthesis), Viral Fusion Proteins (genetics), Viral Matrix Proteins (biosynthesis), Viral Matrix Proteins (genetics), Viral Matrix Proteins (pharmacology).
- MESH :
- chemical , biosynthesis : Hemagglutinins, Viral, Membrane Proteins, Recombinant Proteins, Viral Fusion Proteins, Viral Matrix Proteins.
- chemical , genetics : Hemagglutinins, Viral, Viral Fusion Proteins, Viral Matrix Proteins.
- chemical , isolation & purification : Hemagglutinins, Viral.
- chemical , pharmacology : Ammonium Chloride, Viral Matrix Proteins.
- drug effects : Cell Fusion.
- genetics : Influenza A virus, Simian virus 40.
- metabolism : Influenza A virus.
- Animals, Base Sequence, Biological Transport, Cells, Cultured, Chlorocebus aethiops, Fluorescent Antibody Technique, Hemagglutinin Glycoproteins, Influenza Virus, Hydrogen-Ion Concentration, Molecular Sequence Data.
Abstract
The hemagglutinin of the Rostock strain of fowl plague virus was expressed in CV-1 cells by a simian virus 40 vector, and its stability in the exocytotic transport process was examined by a fusion assay. A 50-fold increase in the fusion activity of the hemagglutinin was observed when expression occurred in the presence of ammonium chloride, Tris-HCl, or high doses of amantadine. When chloroquine, another acidotropic agent, was used, the hemagglutinin exposed at the cell surface had to be activated by trypsin, because intracellular cleavage was inhibited by this compound. Hemagglutinin mutants resistant to intracellular cleavage did not require acidotropic agents for full expression of fusion activity, when treated with trypsin after arrival at the cell surface. These results indicate that fowl plague virus hemagglutinin expressed by a simian virus 40 vector is denatured in the acidic milieu of the exocytotic pathway and that cleavage is a major factor responsible for the pH instability. Coexpression with the M2 protein also markedly enhanced the fusion activity of the hemagglutinin, and this effect was inhibited by low doses of amantadine. These results support the concept that M2, known to have ion channel function, protects the hemagglutinin from denaturation by raising the pH in the exocytotic transport system. The data also stress the importance of acidotropic agents or coexpressed M2 for the structural and functional integrity of vector-expressed hemagglutinin.
PubMed: 8289394
Affiliations:
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Garten</name></author><author><name sortKey="Klenk, H D" sort="Klenk, H D" uniqKey="Klenk H" first="H D" last="Klenk">H D Klenk</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ammonium Chloride (pharmacology)</term><term>Animals</term><term>Base Sequence</term><term>Biological Transport</term><term>Cell Fusion (drug effects)</term><term>Cells, Cultured</term><term>Chlorocebus aethiops</term><term>Fluorescent Antibody Technique</term><term>Hemagglutinin Glycoproteins, Influenza Virus</term><term>Hemagglutinins, Viral (biosynthesis)</term><term>Hemagglutinins, Viral (genetics)</term><term>Hemagglutinins, Viral (isolation & purification)</term><term>Hydrogen-Ion Concentration</term><term>Influenza A virus (genetics)</term><term>Influenza A virus (metabolism)</term><term>Membrane Proteins (biosynthesis)</term><term>Molecular Sequence Data</term><term>Recombinant Proteins (biosynthesis)</term><term>Simian virus 40 (genetics)</term><term>Viral Fusion Proteins (biosynthesis)</term><term>Viral Fusion Proteins (genetics)</term><term>Viral Matrix Proteins (biosynthesis)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Chlorure d'ammonium (pharmacologie)</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Fusion cellulaire ()</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Hémagglutinines virales (biosynthèse)</term><term>Hémagglutinines virales (génétique)</term><term>Hémagglutinines virales (isolement et purification)</term><term>Protéines de fusion virale (biosynthèse)</term><term>Protéines de fusion virale (génétique)</term><term>Protéines de la matrice virale (biosynthèse)</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (pharmacologie)</term><term>Protéines membranaires (biosynthèse)</term><term>Protéines recombinantes (biosynthèse)</term><term>Séquence nucléotidique</term><term>Technique d'immunofluorescence</term><term>Transport biologique</term><term>Virus de la grippe A (génétique)</term><term>Virus de la grippe A (métabolisme)</term><term>Virus simien 40 (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Hemagglutinins, Viral</term><term>Membrane Proteins</term><term>Recombinant Proteins</term><term>Viral Fusion Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hemagglutinins, Viral</term><term>Viral Fusion Proteins</term><term>Viral Matrix 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cultivées</term><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Fusion cellulaire</term><term>Glycoprotéine hémagglutinine du virus influenza</term><term>Séquence nucléotidique</term><term>Technique d'immunofluorescence</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The hemagglutinin of the Rostock strain of fowl plague virus was expressed in CV-1 cells by a simian virus 40 vector, and its stability in the exocytotic transport process was examined by a fusion assay. A 50-fold increase in the fusion activity of the hemagglutinin was observed when expression occurred in the presence of ammonium chloride, Tris-HCl, or high doses of amantadine. When chloroquine, another acidotropic agent, was used, the hemagglutinin exposed at the cell surface had to be activated by trypsin, because intracellular cleavage was inhibited by this compound. Hemagglutinin mutants resistant to intracellular cleavage did not require acidotropic agents for full expression of fusion activity, when treated with trypsin after arrival at the cell surface. These results indicate that fowl plague virus hemagglutinin expressed by a simian virus 40 vector is denatured in the acidic milieu of the exocytotic pathway and that cleavage is a major factor responsible for the pH instability. Coexpression with the M2 protein also markedly enhanced the fusion activity of the hemagglutinin, and this effect was inhibited by low doses of amantadine. These results support the concept that M2, known to have ion channel function, protects the hemagglutinin from denaturation by raising the pH in the exocytotic transport system. The data also stress the importance of acidotropic agents or coexpressed M2 for the structural and functional integrity of vector-expressed hemagglutinin.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Cramer, A" sort="Cramer, A" uniqKey="Cramer A" first="A" last="Cramer">A. Cramer</name><name sortKey="Garten, W" sort="Garten, W" uniqKey="Garten W" first="W" last="Garten">W. Garten</name><name sortKey="Klenk, H D" sort="Klenk, H D" uniqKey="Klenk H" first="H D" last="Klenk">H D Klenk</name><name sortKey="Ohuchi, R" sort="Ohuchi, R" uniqKey="Ohuchi R" first="R" last="Ohuchi">R. Ohuchi</name><name sortKey="Vey, M" sort="Vey, M" uniqKey="Vey M" first="M" last="Vey">M. Vey</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Ohuchi, M" sort="Ohuchi, M" uniqKey="Ohuchi M" first="M" last="Ohuchi">M. Ohuchi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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