Pepstatin A alters host cell autophagic machinery and leads to a decrease in influenza A virus production.
Identifieur interne : 000437 ( Ncbi/Curation ); précédent : 000436; suivant : 000438Pepstatin A alters host cell autophagic machinery and leads to a decrease in influenza A virus production.
Auteurs : Paola Matarrese [Italie] ; Lucia Nencioni ; Paola Checconi ; Laura Ciarlo ; Lucrezia Gambardella ; Barbara Ascione ; Rossella Sgarbanti ; Enrico Garaci ; Walter Malorni ; Anna Teresa PalamaraSource :
- Journal of cellular physiology [ 1097-4652 ] ; 2011.
Descripteurs français
- KwdFr :
- Antiviraux (pharmacologie), Apoptose (), Autophagie (), Cathepsine A (antagonistes et inhibiteurs), Cathepsine A (métabolisme), Cathepsine D (antagonistes et inhibiteurs), Cathepsine D (métabolisme), Dipeptides (pharmacologie), Facteurs temps, Humains, Inhibiteurs de protéases (pharmacologie), Interactions hôte-pathogène (), Lignée cellulaire tumorale, Lysosomes (), Lysosomes (enzymologie), Lysosomes (virologie), Pepstatines (pharmacologie), Potentiel de membrane mitochondriale (), Protéines virales (métabolisme), Régulation négative, Réplication virale (), Sous-type H1N1 du virus de la grippe A (), Sous-type H1N1 du virus de la grippe A (croissance et développement), Sous-type H1N1 du virus de la grippe A (pathogénicité).
- MESH :
- antagonistes et inhibiteurs : Cathepsine A, Cathepsine D.
- croissance et développement : Sous-type H1N1 du virus de la grippe A.
- enzymologie : Lysosomes.
- métabolisme : Cathepsine A, Cathepsine D, Protéines virales.
- pathogénicité : Sous-type H1N1 du virus de la grippe A.
- pharmacologie : Antiviraux, Dipeptides, Inhibiteurs de protéases, Pepstatines.
- virologie : Lysosomes.
- Apoptose, Autophagie, Facteurs temps, Humains, Interactions hôte-pathogène, Lignée cellulaire tumorale, Lysosomes, Potentiel de membrane mitochondriale, Régulation négative, Réplication virale, Sous-type H1N1 du virus de la grippe A.
English descriptors
- KwdEn :
- Antiviral Agents (pharmacology), Apoptosis (drug effects), Autophagy (drug effects), Cathepsin A (antagonists & inhibitors), Cathepsin A (metabolism), Cathepsin D (antagonists & inhibitors), Cathepsin D (metabolism), Cell Line, Tumor, Dipeptides (pharmacology), Down-Regulation, Host-Pathogen Interactions (drug effects), Humans, Influenza A Virus, H1N1 Subtype (drug effects), Influenza A Virus, H1N1 Subtype (growth & development), Influenza A Virus, H1N1 Subtype (pathogenicity), Lysosomes (drug effects), Lysosomes (enzymology), Lysosomes (virology), Membrane Potential, Mitochondrial (drug effects), Pepstatins (pharmacology), Protease Inhibitors (pharmacology), Time Factors, Viral Proteins (metabolism), Virus Replication (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Cathepsin A, Cathepsin D.
- chemical , metabolism : Cathepsin A, Cathepsin D, Viral Proteins.
- chemical , pharmacology : Antiviral Agents, Dipeptides, Pepstatins, Protease Inhibitors.
- drug effects : Apoptosis, Autophagy, Host-Pathogen Interactions, Influenza A Virus, H1N1 Subtype, Lysosomes, Membrane Potential, Mitochondrial, Virus Replication.
- enzymology : Lysosomes.
- growth & development : Influenza A Virus, H1N1 Subtype.
- pathogenicity : Influenza A Virus, H1N1 Subtype.
- virology : Lysosomes.
- Cell Line, Tumor, Down-Regulation, Humans, Time Factors.
Abstract
Autophagy is a survival mechanism that can take place in cells under metabolic stress and through which cells can recycle waste material. Disturbances in autophagic processes appear to be associated with a number of human pathologies, including viral infections. It has been hypothesized that viruses can subvert autophagy in order to penetrate the host cell and replicate. Because it has been suggested that autophagy is involved in influenza A virus replication, we analyzed the effects of two inhibitors of lysosomal proteases on the cellular control of influenza A virus replication. In particular, we used biochemical and morphological analyses to evaluate the modulation of influenza A/Puerto Rico/8/34 H1N1 virus production in the presence of CA074 and Pepstatin A, inhibitors of cathepsin proteases B and D, respectively. We found that Pepstatin A, but not CA074, significantly hindered influenza virus replication, probably by modulating host cell autophagic/apoptotic responses. These results are of potential interest to provide useful insights into the molecular pathways exploited by the influenza in order to replicate and to identify further cellular factors as targets for the development of innovative antiviral strategies.
DOI: 10.1002/jcp.22696
PubMed: 21344392
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pubmed:21344392Le document en format XML
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Palamara</name></author></analytic><series><title level="j">Journal of cellular physiology</title><idno type="eISSN">1097-4652</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (pharmacology)</term><term>Apoptosis (drug effects)</term><term>Autophagy (drug effects)</term><term>Cathepsin A (antagonists & inhibitors)</term><term>Cathepsin A (metabolism)</term><term>Cathepsin D (antagonists & inhibitors)</term><term>Cathepsin D (metabolism)</term><term>Cell Line, Tumor</term><term>Dipeptides (pharmacology)</term><term>Down-Regulation</term><term>Host-Pathogen Interactions (drug effects)</term><term>Humans</term><term>Influenza A Virus, H1N1 Subtype (drug effects)</term><term>Influenza A Virus, H1N1 Subtype (growth & development)</term><term>Influenza A Virus, H1N1 Subtype (pathogenicity)</term><term>Lysosomes (drug effects)</term><term>Lysosomes (enzymology)</term><term>Lysosomes (virology)</term><term>Membrane Potential, Mitochondrial (drug effects)</term><term>Pepstatins (pharmacology)</term><term>Protease Inhibitors (pharmacology)</term><term>Time Factors</term><term>Viral Proteins (metabolism)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux (pharmacologie)</term><term>Apoptose ()</term><term>Autophagie ()</term><term>Cathepsine A (antagonistes et inhibiteurs)</term><term>Cathepsine A (métabolisme)</term><term>Cathepsine D (antagonistes et inhibiteurs)</term><term>Cathepsine D (métabolisme)</term><term>Dipeptides (pharmacologie)</term><term>Facteurs temps</term><term>Humains</term><term>Inhibiteurs de protéases (pharmacologie)</term><term>Interactions hôte-pathogène ()</term><term>Lignée cellulaire tumorale</term><term>Lysosomes ()</term><term>Lysosomes (enzymologie)</term><term>Lysosomes (virologie)</term><term>Pepstatines (pharmacologie)</term><term>Potentiel de membrane mitochondriale ()</term><term>Protéines virales (métabolisme)</term><term>Régulation négative</term><term>Réplication virale ()</term><term>Sous-type H1N1 du virus de la grippe A ()</term><term>Sous-type H1N1 du virus de la grippe A (croissance et développement)</term><term>Sous-type H1N1 du virus de la grippe A (pathogénicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Cathepsin A</term><term>Cathepsin D</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cathepsin A</term><term>Cathepsin D</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Dipeptides</term><term>Pepstatins</term><term>Protease Inhibitors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" 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scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Influenza A Virus, H1N1 Subtype</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Sous-type H1N1 du virus de la grippe A</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antiviraux</term><term>Dipeptides</term><term>Inhibiteurs de protéases</term><term>Pepstatines</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Lysosomes</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Lysosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Down-Regulation</term><term>Humans</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Apoptose</term><term>Autophagie</term><term>Facteurs temps</term><term>Humains</term><term>Interactions hôte-pathogène</term><term>Lignée cellulaire tumorale</term><term>Lysosomes</term><term>Potentiel de membrane mitochondriale</term><term>Régulation négative</term><term>Réplication virale</term><term>Sous-type H1N1 du virus de la grippe A</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Autophagy is a survival mechanism that can take place in cells under metabolic stress and through which cells can recycle waste material. Disturbances in autophagic processes appear to be associated with a number of human pathologies, including viral infections. It has been hypothesized that viruses can subvert autophagy in order to penetrate the host cell and replicate. Because it has been suggested that autophagy is involved in influenza A virus replication, we analyzed the effects of two inhibitors of lysosomal proteases on the cellular control of influenza A virus replication. In particular, we used biochemical and morphological analyses to evaluate the modulation of influenza A/Puerto Rico/8/34 H1N1 virus production in the presence of CA074 and Pepstatin A, inhibitors of cathepsin proteases B and D, respectively. We found that Pepstatin A, but not CA074, significantly hindered influenza virus replication, probably by modulating host cell autophagic/apoptotic responses. These results are of potential interest to provide useful insights into the molecular pathways exploited by the influenza in order to replicate and to identify further cellular factors as targets for the development of innovative antiviral strategies.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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