Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection.
Identifieur interne : 004707 ( Main/Exploration ); précédent : 004706; suivant : 004708Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection.
Auteurs : Shutoku Matsuyama [Japon] ; Makoto Ujike ; Shigeru Morikawa ; Masato Tashiro ; Fumihiro TaguchiSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux, Bacillus thermoproteolyticus neutral proteinase (pharmacologie), Cellules Vero, Pancreatic elastase (pharmacologie), Peptide hydrolases (métabolisme), Poumon (enzymologie), Poumon (virologie), Réplication virale (), Syndrome respiratoire aigu sévère (enzymologie), Syndrome respiratoire aigu sévère (virologie), Syndrome respiratoire aigu sévère (étiologie), Trypsine (pharmacologie), Virulence (), Virulence (physiologie), Virus du SRAS (), Virus du SRAS (génétique), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- enzymologie : Poumon, Syndrome respiratoire aigu sévère.
- génétique : Virus du SRAS.
- métabolisme : Peptide hydrolases.
- pathogénicité : Virus du SRAS.
- pharmacologie : Bacillus thermoproteolyticus neutral proteinase, Pancreatic elastase, Trypsine.
- physiologie : Virulence, Virus du SRAS.
- virologie : Poumon, Syndrome respiratoire aigu sévère.
- étiologie : Syndrome respiratoire aigu sévère.
- Animaux, Cellules Vero, Réplication virale, Virulence, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Lung (enzymology), Lung (virology), Pancreatic Elastase (pharmacology), Peptide Hydrolases (metabolism), SARS Virus (drug effects), SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Severe Acute Respiratory Syndrome (enzymology), Severe Acute Respiratory Syndrome (etiology), Severe Acute Respiratory Syndrome (virology), Thermolysin (pharmacology), Trypsin (pharmacology), Vero Cells, Virulence (drug effects), Virulence (physiology), Virus Replication (drug effects).
- MESH :
- chemical , metabolism : Peptide Hydrolases.
- chemical , pharmacology : Pancreatic Elastase, Thermolysin, Trypsin.
- drug effects : SARS Virus, Virulence, Virus Replication.
- enzymology : Lung, Severe Acute Respiratory Syndrome.
- etiology : Severe Acute Respiratory Syndrome.
- genetics : SARS Virus.
- pathogenicity : SARS Virus.
- physiology : SARS Virus, Virulence.
- virology : Lung, Severe Acute Respiratory Syndrome.
- Animals, Chlorocebus aethiops, Vero Cells.
Abstract
A unique coronavirus severe acute respiratory syndrome-coronavirus (SARS-CoV) was revealed to be a causative agent of a life-threatening SARS. Although this virus grows in a variety of tissues that express its receptor, the mechanism of the severe respiratory illness caused by this virus is not well understood. Here, we report a possible mechanism for the extensive damage seen in the major target organs for this disease. A recent study of the cell entry mechanism of SARS-CoV reveals that it takes an endosomal pathway. We found that proteases such as trypsin and thermolysin enabled SARS-CoV adsorbed onto the cell surface to enter cells directly from that site. This finding shows that SARS-CoV has the potential to take two distinct pathways for cell entry, depending on the presence of proteases in the environment. Moreover, the protease-mediated entry facilitated a 100- to 1,000-fold higher efficient infection than did the endosomal pathway used in the absence of proteases. These results suggest that the proteases produced in the lungs by inflammatory cells are responsible for high multiplication of SARS-CoV, which results in severe lung tissue damage. Likewise, elastase, a major protease produced in the lungs during inflammation, also enhanced SARS-CoV infection in cultured cells.
DOI: 10.1073/pnas.0503203102
PubMed: 16116101
Affiliations:
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Le document en format XML
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last="Matsuyama">Shutoku Matsuyama</name><affiliation wicri:level="1"><nlm:affiliation>Division of Respiratory Viral Diseases and SARS, Department of Virology III, Special Pathogens Laboratory, National Institute of Infectious Diseases, Murayama Branch, Gakuen 4-7-1, Musashi-Murayama, Tokyo 208-0011, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Respiratory Viral Diseases and SARS, Department of Virology III, Special Pathogens Laboratory, National Institute of Infectious Diseases, Murayama Branch, Gakuen 4-7-1, Musashi-Murayama, Tokyo 208-0011</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Ujike, Makoto" sort="Ujike, Makoto" uniqKey="Ujike M" first="Makoto" last="Ujike">Makoto Ujike</name></author><author><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name></author><author><name sortKey="Tashiro, Masato" sort="Tashiro, Masato" uniqKey="Tashiro M" first="Masato" last="Tashiro">Masato Tashiro</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Lung (enzymology)</term><term>Lung (virology)</term><term>Pancreatic Elastase (pharmacology)</term><term>Peptide Hydrolases (metabolism)</term><term>SARS Virus (drug effects)</term><term>SARS Virus (genetics)</term><term>SARS Virus (pathogenicity)</term><term>SARS Virus (physiology)</term><term>Severe Acute Respiratory Syndrome (enzymology)</term><term>Severe Acute Respiratory Syndrome (etiology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Thermolysin (pharmacology)</term><term>Trypsin (pharmacology)</term><term>Vero Cells</term><term>Virulence (drug effects)</term><term>Virulence (physiology)</term><term>Virus Replication (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Bacillus thermoproteolyticus neutral proteinase (pharmacologie)</term><term>Cellules Vero</term><term>Pancreatic elastase (pharmacologie)</term><term>Peptide hydrolases (métabolisme)</term><term>Poumon (enzymologie)</term><term>Poumon (virologie)</term><term>Réplication virale ()</term><term>Syndrome respiratoire aigu sévère (enzymologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Syndrome respiratoire aigu sévère (étiologie)</term><term>Trypsine (pharmacologie)</term><term>Virulence ()</term><term>Virulence (physiologie)</term><term>Virus du SRAS ()</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (pathogénicité)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Pancreatic Elastase</term><term>Thermolysin</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>SARS Virus</term><term>Virulence</term><term>Virus Replication</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Lung</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="etiology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peptide hydrolases</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Bacillus thermoproteolyticus neutral proteinase</term><term>Pancreatic elastase</term><term>Trypsine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virulence</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term><term>Virulence</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Lung</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="étiologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Réplication virale</term><term>Virulence</term><term>Virus du SRAS</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A unique coronavirus severe acute respiratory syndrome-coronavirus (SARS-CoV) was revealed to be a causative agent of a life-threatening SARS. Although this virus grows in a variety of tissues that express its receptor, the mechanism of the severe respiratory illness caused by this virus is not well understood. Here, we report a possible mechanism for the extensive damage seen in the major target organs for this disease. A recent study of the cell entry mechanism of SARS-CoV reveals that it takes an endosomal pathway. We found that proteases such as trypsin and thermolysin enabled SARS-CoV adsorbed onto the cell surface to enter cells directly from that site. This finding shows that SARS-CoV has the potential to take two distinct pathways for cell entry, depending on the presence of proteases in the environment. Moreover, the protease-mediated entry facilitated a 100- to 1,000-fold higher efficient infection than did the endosomal pathway used in the absence of proteases. These results suggest that the proteases produced in the lungs by inflammatory cells are responsible for high multiplication of SARS-CoV, which results in severe lung tissue damage. Likewise, elastase, a major protease produced in the lungs during inflammation, also enhanced SARS-CoV infection in cultured cells.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name><name sortKey="Tashiro, Masato" sort="Tashiro, Masato" uniqKey="Tashiro M" first="Masato" last="Tashiro">Masato Tashiro</name><name sortKey="Ujike, Makoto" sort="Ujike, Makoto" uniqKey="Ujike M" first="Makoto" last="Ujike">Makoto Ujike</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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