Protease-Mediated Entry via the Endosome of Human Coronavirus 229E
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| Published in | Journal of Virology Vol. 83; no. 2; pp. 712 - 721 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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Washington, DC
American Society for Microbiology
15.01.2009
American Society for Microbiology (ASM) |
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| AbstractList | Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry. Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry.Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been fully elucidated. We found that HeLa cells infected with 229E via APN formed syncytia when treated with trypsin or other proteases but not in a low-pH environment, a finding consistent with syncytium formation by severe acute respiratory syndrome coronavirus (SARS-CoV). In addition, trypsin induced cleavage of the 229E S protein. By using infectious viruses and pseudotyped viruses bearing the 229E S protein, we found that its infection was profoundly blocked by lysosomotropic agents as well as by protease inhibitors that also prevented infection with SARS-CoV but not that caused by murine coronavirus mouse hepatitis virus strain JHMV, which enters cells directly from the cell surface. We found that cathepsin L (CPL) inhibitors blocked 229E infection the most remarkably among a variety of protease inhibitors tested. Furthermore, 229E infection was inhibited in CPL knockdown cells by small interfering RNA, compared with what was seen for a normal counterpart producing CPL. However, its inhibition was not so remarkable as that found with SARS-CoV infection, which seems to indicate that while CPL is involved in the fusogenic activation of 229E S protein in endosomal infection, not-yet-identified proteases could also play a part in that activity. We also found 229E virion S protein to be cleaved by CPL. Furthermore, as with SARS-CoV, 229E entered cells directly from the cell surface when cell-attached viruses were treated with trypsin. These findings suggest that 229E takes an endosomal pathway for cell entry and that proteases like CPL are involved in this mode of entry. |
| Author | Miyuki Kawase Shutoku Matsuyama Fumihiro Taguchi Kazuya Shirato |
| AuthorAffiliation | Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan |
| AuthorAffiliation_xml | – name: Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan |
| Author_xml | – sequence: 1 givenname: Miyuki surname: Kawase fullname: Kawase, Miyuki organization: Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan – sequence: 2 givenname: Kazuya surname: Shirato fullname: Shirato, Kazuya organization: Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan – sequence: 3 givenname: Shutoku surname: Matsuyama fullname: Matsuyama, Shutoku organization: Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan – sequence: 4 givenname: Fumihiro surname: Taguchi fullname: Taguchi, Fumihiro organization: Laboratory of Respiratory Viral Infections, Department of Virology III, National Institute of Infectious Diseases, Musashi-Murayama, 208-0011 Tokyo, Japan |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21151847$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/18971274$$D View this record in MEDLINE/PubMed |
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Mendeley... Human coronavirus 229E, classified as a group I coronavirus, utilizes human aminopeptidase N (APN) as a receptor; however, its entry mechanism has not yet been... |
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| SubjectTerms | Biological and medical sciences Cathepsin L Cathepsins - antagonists & inhibitors Cathepsins - metabolism Coronavirus 229E, Human - physiology Cysteine Endopeptidases - metabolism Endosomes - virology Fundamental and applied biological sciences. Psychology Gene Knockdown Techniques HeLa Cells Human coronavirus 229e Humans Hydrogen-Ion Concentration Membrane Glycoproteins - metabolism Microbiology Miscellaneous Murine coronavirus Murine hepatitis virus Murine hepatitis virus - physiology Peptide Hydrolases - metabolism RNA, Small Interfering - genetics RNA, Small Interfering - metabolism SARS coronavirus SARS Virus - physiology Spike Glycoprotein, Coronavirus Viral Envelope Proteins - metabolism Viral Plaque Assay Virology Virus Internalization Virus-Cell Interactions |
| Title | Protease-Mediated Entry via the Endosome of Human Coronavirus 229E |
| URI | http://jvi.asm.org/content/83/2/712.abstract https://www.ncbi.nlm.nih.gov/pubmed/18971274 https://www.proquest.com/docview/21499830 https://www.proquest.com/docview/66783753 https://pubmed.ncbi.nlm.nih.gov/PMC2612384 |
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