Hepatitis mutants of mouse hepatitis virus strain A59.
Identifieur interne : 003518 ( PubMed/Curation ); précédent : 003517; suivant : 003519Hepatitis mutants of mouse hepatitis virus strain A59.
Auteurs : S T Hingley [États-Unis] ; J L Gombold ; E. Lavi ; S R WeissSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1995.
Descripteurs français
- KwdFr :
- Animaux, Encéphale (virologie), Foie (virologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Gènes viraux, Hépatite virale animale (virologie), Infections à coronavirus (virologie), Mutation, Protéines de l'enveloppe virale (génétique), Réplication virale, Souris, Souris de lignée C57BL, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (pathogénicité), Virus de l'hépatite murine (physiologie).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- pathogénicité : Virus de l'hépatite murine.
- physiologie : Virus de l'hépatite murine.
- virologie : Encéphale, Foie, Hépatite virale animale, Infections à coronavirus.
- Animaux, Glycoprotéine de spicule des coronavirus, Gènes viraux, Mutation, Réplication virale, Souris, Souris de lignée C57BL.
English descriptors
- KwdEn :
- Animals, Brain (virology), Coronavirus Infections (virology), Genes, Viral, Hepatitis, Viral, Animal (virology), Liver (virology), Membrane Glycoproteins (genetics), Mice, Mice, Inbred C57BL, Murine hepatitis virus (genetics), Murine hepatitis virus (pathogenicity), Murine hepatitis virus (physiology), Mutation, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Virus Replication.
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : Murine hepatitis virus.
- pathogenicity : Murine hepatitis virus.
- physiology : Murine hepatitis virus.
- virology : Brain, Coronavirus Infections, Hepatitis, Viral, Animal, Liver.
- Animals, Genes, Viral, Mice, Mice, Inbred C57BL, Mutation, Spike Glycoprotein, Coronavirus, Virus Replication.
Abstract
MHV-A59 causes acute meningoencephalitis and hepatitis in susceptible mice, and a persistent productive, but nonlytic, infection of cultured glial cells. We have shown previously that viruses isolated from persistently infected glial cell cultures have a fusion-defective phenotype and were impaired in their abilities to cause hepatitis compared to wild-type MHV-A59. Two mutants chosen for detailed study, B11 and C12, display two distinct hepatitis phenotypes. The ability of B11 to replicate in the liver was dependent on infectious dose and route of inoculation, while C12 consistently displayed decreased liver titers regardless of dose and route of inoculation. Sequence analysis of wild-type, mutant and revertant S proteins indicates that 1) a mutation in the N terminal subunit of S, resulting in a glutamine to leucine amino acid substitution (Q159L), may affect ability to cause hepatitis and 2) a cleavage site mutation (H716D) which determines fusogenicity is not responsible for the altered hepatitis phenotype. Sequence analysis indicated that hepatitis-producing revertants did not revert at mutation Q159L, although it is possible that a mutation in the heptad repeat domain of S2 may compensate for the mutation in S1. Since B11, C12 and a nonattenuated fusion mutant (B12) have identical S protein sequences, there must be additional mutations outside of S which influence both virulence and ability to replicate in the liver.
DOI: 10.1007/978-1-4615-1899-0_92
PubMed: 8830545
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Lavi</name></author><author><name sortKey="Weiss, S R" sort="Weiss, S R" uniqKey="Weiss S" first="S R" last="Weiss">S R Weiss</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:8830545</idno><idno type="pmid">8830545</idno><idno type="doi">10.1007/978-1-4615-1899-0_92</idno><idno type="wicri:Area/PubMed/Corpus">003518</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003518</idno><idno type="wicri:Area/PubMed/Curation">003518</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">003518</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Hepatitis mutants of mouse hepatitis virus strain A59.</title><author><name sortKey="Hingley, S T" sort="Hingley, S T" uniqKey="Hingley S" first="S T" last="Hingley">S T Hingley</name><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology and Immunology, Philadelphia College of Osteopathic Medicine, Pennsylvania, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Philadelphia College of Osteopathic Medicine, Pennsylvania</wicri:regionArea></affiliation></author><author><name sortKey="Gombold, J L" sort="Gombold, J L" uniqKey="Gombold J" first="J L" last="Gombold">J L Gombold</name></author><author><name sortKey="Lavi, E" sort="Lavi, E" uniqKey="Lavi E" first="E" last="Lavi">E. 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We have shown previously that viruses isolated from persistently infected glial cell cultures have a fusion-defective phenotype and were impaired in their abilities to cause hepatitis compared to wild-type MHV-A59. Two mutants chosen for detailed study, B11 and C12, display two distinct hepatitis phenotypes. The ability of B11 to replicate in the liver was dependent on infectious dose and route of inoculation, while C12 consistently displayed decreased liver titers regardless of dose and route of inoculation. Sequence analysis of wild-type, mutant and revertant S proteins indicates that 1) a mutation in the N terminal subunit of S, resulting in a glutamine to leucine amino acid substitution (Q159L), may affect ability to cause hepatitis and 2) a cleavage site mutation (H716D) which determines fusogenicity is not responsible for the altered hepatitis phenotype. Sequence analysis indicated that hepatitis-producing revertants did not revert at mutation Q159L, although it is possible that a mutation in the heptad repeat domain of S2 may compensate for the mutation in S1. Since B11, C12 and a nonattenuated fusion mutant (B12) have identical S protein sequences, there must be additional mutations outside of S which influence both virulence and ability to replicate in the liver.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8830545</PMID><DateCompleted><Year>1996</Year><Month>10</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0065-2598</ISSN><JournalIssue CitedMedium="Print"><Volume>380</Volume><PubDate><Year>1995</Year></PubDate></JournalIssue><Title>Advances in experimental medicine and biology</Title><ISOAbbreviation>Adv. Exp. Med. Biol.</ISOAbbreviation></Journal><ArticleTitle>Hepatitis mutants of mouse hepatitis virus strain A59.</ArticleTitle><Pagination><MedlinePgn>577-82</MedlinePgn></Pagination><Abstract><AbstractText>MHV-A59 causes acute meningoencephalitis and hepatitis in susceptible mice, and a persistent productive, but nonlytic, infection of cultured glial cells. We have shown previously that viruses isolated from persistently infected glial cell cultures have a fusion-defective phenotype and were impaired in their abilities to cause hepatitis compared to wild-type MHV-A59. Two mutants chosen for detailed study, B11 and C12, display two distinct hepatitis phenotypes. The ability of B11 to replicate in the liver was dependent on infectious dose and route of inoculation, while C12 consistently displayed decreased liver titers regardless of dose and route of inoculation. Sequence analysis of wild-type, mutant and revertant S proteins indicates that 1) a mutation in the N terminal subunit of S, resulting in a glutamine to leucine amino acid substitution (Q159L), may affect ability to cause hepatitis and 2) a cleavage site mutation (H716D) which determines fusogenicity is not responsible for the altered hepatitis phenotype. Sequence analysis indicated that hepatitis-producing revertants did not revert at mutation Q159L, although it is possible that a mutation in the heptad repeat domain of S2 may compensate for the mutation in S1. Since B11, C12 and a nonattenuated fusion mutant (B12) have identical S protein sequences, there must be additional mutations outside of S which influence both virulence and ability to replicate in the liver.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hingley</LastName><ForeName>S T</ForeName><Initials>ST</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Philadelphia College of Osteopathic Medicine, Pennsylvania, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gombold</LastName><ForeName>J L</ForeName><Initials>JL</Initials></Author><Author ValidYN="Y"><LastName>Lavi</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Weiss</LastName><ForeName>S R</ForeName><Initials>SR</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Adv Exp Med Biol</MedlineTA><NlmUniqueID>0121103</NlmUniqueID><ISSNLinking>0065-2598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578553">MHV surface projection glycoprotein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C578557">spike glycoprotein, SARS-CoV</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="N">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018352" MajorTopicYN="N">Coronavirus Infections</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005814" MajorTopicYN="Y">Genes, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006524" MajorTopicYN="N">Hepatitis, Viral, Animal</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000821" MajorTopicYN="Y">virology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008810" MajorTopicYN="N">Mice, Inbred C57BL</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="Y">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="Y">Virus Replication</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8830545</ArticleId><ArticleId IdType="doi">10.1007/978-1-4615-1899-0_92</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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