Protease susceptibility of human A influenza virus polypeptides.
Identifieur interne : 002703 ( Main/Exploration ); précédent : 002702; suivant : 002704Protease susceptibility of human A influenza virus polypeptides.
Auteurs : L R Sabina ; M E Ewasyshyn ; R. Hills ; D A McleodSource :
- Acta virologica [ 0001-723X ] ; 1981.
Descripteurs français
- KwdFr :
- Animaux, Dénaturation des protéines, Embryon de poulet, Peptide hydrolases (métabolisme), Peptides (métabolisme), Phospholipase D (métabolisme), Protéines virales (métabolisme), Trypsine (métabolisme), Virus de la grippe A (immunologie), Virus de la grippe A (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- immunologie : Virus de la grippe A.
- métabolisme : Peptide hydrolases, Peptides, Phospholipase D, Protéines virales, Trypsine, Virus de la grippe A.
- Animaux, Dénaturation des protéines, Embryon de poulet, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Peptide Hydrolases, Peptides, Phospholipase D, Trypsin, Viral Proteins.
- immunology : Influenza A virus.
- metabolism : Influenza A virus.
- Animals, Chick Embryo, Electrophoresis, Polyacrylamide Gel, Protein Denaturation.
Abstract
The proteolytic susceptibility of polypeptides of four antigenically distinct subtypes of influenza a virus strains of human origin was studied. The extent of degradation of polypeptide molecules of strains A/PR/8/34 (H0N1) (PR), A/FM/1/47 (H1N1), A/Singapore/1/57 (H2N2) and A/Hong Kong/8/68 (H3N2), assessed by densitometry of gels after sodium dodecylsulfate polyacrylamide gel electrophoresis was variable by treatment with trypsin. Also, sequential treatment of PR strain initially with phospholipase D followed by proteases of different specificities suggested differences in susceptibility of surface and internal polypeptide molecules. The significance of these results is discussed.
PubMed: 6115561
Affiliations:
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Le document en format XML
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<series><title level="j">Acta virologica</title>
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<term>Chick Embryo</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Influenza A virus (immunology)</term>
<term>Influenza A virus (metabolism)</term>
<term>Peptide Hydrolases (metabolism)</term>
<term>Peptides (metabolism)</term>
<term>Phospholipase D (metabolism)</term>
<term>Protein Denaturation</term>
<term>Trypsin (metabolism)</term>
<term>Viral Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Dénaturation des protéines</term>
<term>Embryon de poulet</term>
<term>Peptide hydrolases (métabolisme)</term>
<term>Peptides (métabolisme)</term>
<term>Phospholipase D (métabolisme)</term>
<term>Protéines virales (métabolisme)</term>
<term>Trypsine (métabolisme)</term>
<term>Virus de la grippe A (immunologie)</term>
<term>Virus de la grippe A (métabolisme)</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term>
<term>Peptides</term>
<term>Phospholipase D</term>
<term>Trypsin</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Virus de la grippe A</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Influenza A virus</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Influenza A virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptide hydrolases</term>
<term>Peptides</term>
<term>Phospholipase D</term>
<term>Protéines virales</term>
<term>Trypsine</term>
<term>Virus de la grippe A</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Chick Embryo</term>
<term>Electrophoresis, Polyacrylamide Gel</term>
<term>Protein Denaturation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Dénaturation des protéines</term>
<term>Embryon de poulet</term>
<term>Électrophorèse sur gel de polyacrylamide</term>
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<front><div type="abstract" xml:lang="en">The proteolytic susceptibility of polypeptides of four antigenically distinct subtypes of influenza a virus strains of human origin was studied. The extent of degradation of polypeptide molecules of strains A/PR/8/34 (H0N1) (PR), A/FM/1/47 (H1N1), A/Singapore/1/57 (H2N2) and A/Hong Kong/8/68 (H3N2), assessed by densitometry of gels after sodium dodecylsulfate polyacrylamide gel electrophoresis was variable by treatment with trypsin. Also, sequential treatment of PR strain initially with phospholipase D followed by proteases of different specificities suggested differences in susceptibility of surface and internal polypeptide molecules. The significance of these results is discussed.</div>
</front>
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<name sortKey="Hills, R" sort="Hills, R" uniqKey="Hills R" first="R" last="Hills">R. Hills</name>
<name sortKey="Mcleod, D A" sort="Mcleod, D A" uniqKey="Mcleod D" first="D A" last="Mcleod">D A Mcleod</name>
<name sortKey="Sabina, L R" sort="Sabina, L R" uniqKey="Sabina L" first="L R" last="Sabina">L R Sabina</name>
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