Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection.
Identifieur interne : 002575 ( PubMed/Curation ); précédent : 002574; suivant : 002576Protease-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
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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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16116101</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>102</Volume><Issue>35</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>30</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection.</ArticleTitle><Pagination><MedlinePgn>12543-7</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Matsuyama</LastName><ForeName>Shutoku</ForeName><Initials>S</Initials><AffiliationInfo><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.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ujike</LastName><ForeName>Makoto</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Morikawa</LastName><ForeName>Shigeru</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Tashiro</LastName><ForeName>Masato</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Taguchi</LastName><ForeName>Fumihiro</ForeName><Initials>F</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>08</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D010447">Peptide Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.36</RegistryNumber><NameOfSubstance UI="D010196">Pancreatic Elastase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045169" MajorTopicYN="N">Severe Acute Respiratory Syndrome</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000209" MajorTopicYN="Y">etiology</QualifierName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013820" MajorTopicYN="N">Thermolysin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014357" 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