Activation of the 2-5OAS/RNase L pathway in CVB1 or HAV/18f infected FRhK-4 cells does not require induction of OAS1 or OAS2 expression

Activation of the 2-5OAS/RNase L pathway in CVB1 or HAV/18f infected FRhK-4 cells does not require induction of OAS1 or OAS2 expression

Abstract The latent, constitutively expressed protein RNase L is activated in coxsackievirus and HAV strain 18f infected FRhK-4 cells. Endogenous oligoadenylate synthetase (OAS) from uninfected and virus infected cell extracts synthesizes active forms of the triphosphorylated 2-5A oligomer (the only...

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Bibliographic Details
Published in:Virology (New York, N.Y.) Vol. 388; no. 1; pp. 169 - 184
Main Authors: Kulka, Michael, Calvo, Mona S, Ngo, Diana T, Wales, Samantha Q, Goswami, Biswendu B
Format: Journal Article
Language:English
Published: United States Elsevier Inc 25-05-2009
Subjects:
2',5'-Oligoadenylate Synthetase - metabolism
2-5A
60 APPLIED LIFE SCIENCES
Animals
Antiviral
Cell Line
Coxsackievirus
Cytopathogenic Effect, Viral
DIGESTIVE SYSTEM DISEASES
DISEASES
Endoribonucleases - metabolism
Enterovirus B, Human - physiology
Enzyme Activation - physiology
Enzyme Induction - physiology
ENZYMES
ESTERASES
HEPATITIS
Hepatitis A virus
Hepatitis A virus - physiology
HYDROLASES
Infectious Disease
Interferons
Kidney - cytology
LIGASES
Macaca mulatta
MICROORGANISMS
NUCLEASES
Oligoadenylate synthetase
ORGANIC COMPOUNDS
PARASITES
PHOSPHODIESTERASES
PROTEINS
RNA, Double-Stranded
RNA-ASE
RNase L
VIRUSES
2-5A
Coxsackievirus
Antiviral
Oligoadenylate synthetase
Hepatitis A virus
RNase L
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Summary:Abstract The latent, constitutively expressed protein RNase L is activated in coxsackievirus and HAV strain 18f infected FRhK-4 cells. Endogenous oligoadenylate synthetase (OAS) from uninfected and virus infected cell extracts synthesizes active forms of the triphosphorylated 2-5A oligomer (the only known activator of RNase L) in vitro and endogenous 2-5A is detected in infected cell extracts. However, only the largest OAS isoform, OAS3, is readily detected throughout the time course of infection. While IFNβ treatment results in an increase in the level of all three OAS isoforms in FRhK-4 cells, IFNβ pretreatment does not affect the temporal onset or enhancement of RNase L activity nor inhibit virus replication. Our results indicate that CVB1 and HAV/18f activate the 2-5OAS/RNase L pathway in FRhK-4 cells during permissive infection through endogenous levels of OAS, but contrary to that reported for some picornaviruses, CVB1 and HAV/18f replication is insensitive to this activated antiviral pathway.
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ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2009.03.014