Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication.
Identifieur interne : 000318 ( PubMed/Curation ); précédent : 000317; suivant : 000319Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication.
Auteurs : Takashi Suzuki [Japon] ; Tadanobu Takahashi ; Chao-Tan Guo ; Kazuya I-P Jwa Hidari ; Daisei Miyamoto ; Hideo Goto ; Yoshihiro Kawaoka ; Yasuo SuzukiSource :
- Journal of virology [ 0022-538X ] ; 2005.
Descripteurs français
- KwdFr :
- Acides sialiques (pharmacologie), Animaux, Antienzymes (pharmacologie), Chiens, Concentration en ions d'hydrogène, Endocytose, Grippe humaine (virologie), Guanidines, Humains, Lignée cellulaire, Mâle, Pyrannes, Réplication virale (), Réplication virale (génétique), Réplication virale (physiologie), Sialidase (antagonistes et inhibiteurs), Sialidase (génétique), Sialidase (métabolisme), Souris, Souris de lignée C57BL, Stabilité enzymatique, Transfection, Virus de la grippe A (), Virus de la grippe A (enzymologie), Virus de la grippe A (génétique), Virus de la grippe A (physiologie), Zanamivir.
- MESH :
- antagonistes et inhibiteurs : Sialidase.
- enzymologie : Virus de la grippe A.
- génétique : Réplication virale, Sialidase, Virus de la grippe A.
- métabolisme : Sialidase.
- pharmacologie : Acides sialiques, Antienzymes.
- physiologie : Réplication virale, Virus de la grippe A.
- virologie : Grippe humaine.
- Animaux, Chiens, Concentration en ions d'hydrogène, Endocytose, Guanidines, Humains, Lignée cellulaire, Mâle, Pyrannes, Réplication virale, Souris, Souris de lignée C57BL, Stabilité enzymatique, Transfection, Virus de la grippe A, Zanamivir.
English descriptors
- KwdEn :
- Animals, Cell Line, Dogs, Endocytosis, Enzyme Inhibitors (pharmacology), Enzyme Stability, Guanidines, Humans, Hydrogen-Ion Concentration, Influenza A virus (drug effects), Influenza A virus (enzymology), Influenza A virus (genetics), Influenza A virus (physiology), Influenza, Human (virology), Male, Mice, Mice, Inbred C57BL, Neuraminidase (antagonists & inhibitors), Neuraminidase (genetics), Neuraminidase (metabolism), Pyrans, Sialic Acids (pharmacology), Transfection, Virus Replication (drug effects), Virus Replication (genetics), Virus Replication (physiology), Zanamivir.
- MESH :
- chemical , antagonists & inhibitors : Neuraminidase.
- chemical , genetics : Neuraminidase.
- chemical , metabolism : Neuraminidase.
- chemical , pharmacology : Enzyme Inhibitors, Sialic Acids.
- drug effects : Influenza A virus, Virus Replication.
- enzymology : Influenza A virus.
- genetics : Influenza A virus, Virus Replication.
- physiology : Influenza A virus, Virus Replication.
- virology : Influenza, Human.
- Animals, Cell Line, Dogs, Endocytosis, Enzyme Stability, Guanidines, Humans, Hydrogen-Ion Concentration, Male, Mice, Mice, Inbred C57BL, Pyrans, Transfection, Zanamivir.
Abstract
N2 neuraminidase (NA) genes of the 1957 and 1968 pandemic influenza virus strains possessed avian-like low-pH stability of sialidase activity, unlike most epidemic strains. We generated four reverse-genetics viruses from a genetic background of A/WSN/33 (H1N1) that included parental N2 NAs of 1968 pandemic (H3N2) and epidemic (H2N2) strains or their counterpart N2 NAs in which the low-pH stability of the sialidase activity was changed by substitutions of one or two amino acid residues. We found that the transfectant viruses bearing low-pH-stable sialidase (WSN/Stable-NAs) showed 25- to 80-times-greater ability to replicate in Madin-Darby canine kidney (MDCK) cells than did the transfectant viruses bearing low-pH-unstable sialidase (WSN/Unstable-NAs). Enzymatic activities of WSN/Stable-NAs were detected in endosomes of MDCK cells after 90 min of virus internalization by in situ fluorescent detection with 5-bromo-4-chloro-indole-3-yl-alpha-N-acetylneuraminic acid and Fast Red Violet LB. Inhibition of sialidase activity of WSN/Stable-NAs on the endocytic pathway by pretreatment with 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid (zanamivir) resulted in a significant decrease in progeny viruses. In contrast, the enzymatic activities of WSN/Unstable-NAs, the replication of which had no effect on pretreatment with zanamivir, were undetectable in cells under the same conditions. Hemadsorption assays of transfectant-virus-infected cells revealed that the low-pH stability of the sialidase had no effect on the process of removal of sialic acid from hemagglutinin in the Golgi regions. Moreover, high titers of viruses were recovered from the lungs of mice infected with WSN/Stable-NAs on day 3 after intranasal inoculation, but WSN/Unstable-NAs were cleared from the lungs of the mice. These results indicate that sialidase activity in late endosome/lysosome traffic enhances influenza A virus replication.
DOI: 10.1128/JVI.79.18.11705-11715.2005
PubMed: 16140748
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We generated four reverse-genetics viruses from a genetic background of A/WSN/33 (H1N1) that included parental N2 NAs of 1968 pandemic (H3N2) and epidemic (H2N2) strains or their counterpart N2 NAs in which the low-pH stability of the sialidase activity was changed by substitutions of one or two amino acid residues. We found that the transfectant viruses bearing low-pH-stable sialidase (WSN/Stable-NAs) showed 25- to 80-times-greater ability to replicate in Madin-Darby canine kidney (MDCK) cells than did the transfectant viruses bearing low-pH-unstable sialidase (WSN/Unstable-NAs). Enzymatic activities of WSN/Stable-NAs were detected in endosomes of MDCK cells after 90 min of virus internalization by in situ fluorescent detection with 5-bromo-4-chloro-indole-3-yl-alpha-N-acetylneuraminic acid and Fast Red Violet LB. Inhibition of sialidase activity of WSN/Stable-NAs on the endocytic pathway by pretreatment with 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid (zanamivir) resulted in a significant decrease in progeny viruses. In contrast, the enzymatic activities of WSN/Unstable-NAs, the replication of which had no effect on pretreatment with zanamivir, were undetectable in cells under the same conditions. Hemadsorption assays of transfectant-virus-infected cells revealed that the low-pH stability of the sialidase had no effect on the process of removal of sialic acid from hemagglutinin in the Golgi regions. Moreover, high titers of viruses were recovered from the lungs of mice infected with WSN/Stable-NAs on day 3 after intranasal inoculation, but WSN/Unstable-NAs were cleared from the lungs of the mice. These results indicate that sialidase activity in late endosome/lysosome traffic enhances influenza A virus replication.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16140748</PMID><DateCompleted><Year>2005</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>79</Volume><Issue>18</Issue><PubDate><Year>2005</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication.</ArticleTitle><Pagination><MedlinePgn>11705-15</MedlinePgn></Pagination><Abstract><AbstractText>N2 neuraminidase (NA) genes of the 1957 and 1968 pandemic influenza virus strains possessed avian-like low-pH stability of sialidase activity, unlike most epidemic strains. We generated four reverse-genetics viruses from a genetic background of A/WSN/33 (H1N1) that included parental N2 NAs of 1968 pandemic (H3N2) and epidemic (H2N2) strains or their counterpart N2 NAs in which the low-pH stability of the sialidase activity was changed by substitutions of one or two amino acid residues. We found that the transfectant viruses bearing low-pH-stable sialidase (WSN/Stable-NAs) showed 25- to 80-times-greater ability to replicate in Madin-Darby canine kidney (MDCK) cells than did the transfectant viruses bearing low-pH-unstable sialidase (WSN/Unstable-NAs). Enzymatic activities of WSN/Stable-NAs were detected in endosomes of MDCK cells after 90 min of virus internalization by in situ fluorescent detection with 5-bromo-4-chloro-indole-3-yl-alpha-N-acetylneuraminic acid and Fast Red Violet LB. Inhibition of sialidase activity of WSN/Stable-NAs on the endocytic pathway by pretreatment with 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid (zanamivir) resulted in a significant decrease in progeny viruses. In contrast, the enzymatic activities of WSN/Unstable-NAs, the replication of which had no effect on pretreatment with zanamivir, were undetectable in cells under the same conditions. Hemadsorption assays of transfectant-virus-infected cells revealed that the low-pH stability of the sialidase had no effect on the process of removal of sialic acid from hemagglutinin in the Golgi regions. Moreover, high titers of viruses were recovered from the lungs of mice infected with WSN/Stable-NAs on day 3 after intranasal inoculation, but WSN/Unstable-NAs were cleared from the lungs of the mice. These results indicate that sialidase activity in late endosome/lysosome traffic enhances influenza A virus replication.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Shizuoka, School of Pharmaceutical Sciences and COE Program in the 21st Century, Shizuoka 422-8526, Japan. Suzukit@u-shizuoka-ken.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takahashi</LastName><ForeName>Tadanobu</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Chao-Tan</ForeName><Initials>CT</Initials></Author><Author ValidYN="Y"><LastName>Hidari</LastName><ForeName>Kazuya I-P Jwa</ForeName><Initials>KI</Initials></Author><Author ValidYN="Y"><LastName>Miyamoto</LastName><ForeName>Daisei</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Goto</LastName><ForeName>Hideo</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Kawaoka</LastName><ForeName>Yoshihiro</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Yasuo</ForeName><Initials>Y</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006146">Guanidines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011714">Pyrans</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012794">Sialic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.18</RegistryNumber><NameOfSubstance UI="D009439">Neuraminidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>L6O3XI777I</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009980" MajorTopicYN="N">Influenza A virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007251" MajorTopicYN="N">Influenza, Human</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009439" MajorTopicYN="N">Neuraminidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011714" MajorTopicYN="N">Pyrans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012794" MajorTopicYN="N">Sialic Acids</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" 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