AMPK-Mediated Inhibition of mTOR Kinase Is Circumvented during Immediate-Early Times of Human Cytomegalovirus Infection

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Published inJournal of Virology Vol. 81; no. 7; pp. 3649 - 3651
Main Authors KUDCHODKAR, Sagar B, DEL PRETE, Gregory Q, MAGUIRE, Tobi G, ALWINE, James C
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.04.2007
Subjects
AMP-Activated Protein Kinases
Biological and medical sciences
Cells, Cultured
Cytomegalovirus - physiology
Fundamental and applied biological sciences. Psychology
Human cytomegalovirus
Humans
Microbial Viability
Microbiology
Miscellaneous
Multienzyme Complexes - genetics
Multienzyme Complexes - metabolism
Protein Kinase Inhibitors - metabolism
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Signal Transduction
Time Factors
TOR Serine-Threonine Kinases
Virology
Virus-Cell Interactions
Infection
Virus
Enzyme
Kinase
Herpesviridae
Transferases
Viral disease
cAMP-dependent protein kinase
Betaherpesvirinae
Human cytomegalovirus
Virology
Online AccessGet full text

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Abstract 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       
AbstractList Human cytomegalovirus (HCMV) infection increases synthetic rates in infected cells. The resulting increase in energy utilization could potentially increase the AMP:ATP ratio, causing activation of 5'-AMP-activated protein kinase (AMPK). Activated AMPK promotes inhibition of mammalian target of rapamycin (mTOR) kinase, which could be deleterious to the viral infection. Using the AMPK-activating drug 5-amino-4-imidazolecarboxamide ribose (AICAR), we showed that, by 12 h post-HCMV infection, inhibition of mTOR by AMPK is circumvented. However, growth curves showed that progeny virion production is inhibited when AICAR is added, suggesting other inhibitory effects of AICAR or activated AMPK.
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       
ABSTRACT Human cytomegalovirus (HCMV) infection increases synthetic rates in infected cells. The resulting increase in energy utilization could potentially increase the AMP:ATP ratio, causing activation of 5′-AMP-activated protein kinase (AMPK). Activated AMPK promotes inhibition of mammalian target of rapamycin (mTOR) kinase, which could be deleterious to the viral infection. Using the AMPK-activating drug 5-amino-4-imidazolecarboxamide ribose (AICAR), we showed that, by 12 h post-HCMV infection, inhibition of mTOR by AMPK is circumvented. However, growth curves showed that progeny virion production is inhibited when AICAR is added, suggesting other inhibitory effects of AICAR or activated AMPK.
Author Sagar B. Kudchodkar
Gregory Q. Del Prete
Tobi G. Maguire
James C. Alwine
AuthorAffiliation Department of Cancer Biology, Abramson Family Cancer Research Institute, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6142
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  organization: Department of Cancer Biology, Abramson Family Cancer Research Institute, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6142, United States
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Keywords Infection
Virus
Enzyme
Kinase
Herpesviridae
Transferases
Viral disease
cAMP-dependent protein kinase
Betaherpesvirinae
Human cytomegalovirus
Virology
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Corresponding author. Mailing address: 314 Biomedical Research Building, 421 Curie Blvd., University of Pennsylvania, Philadelphia, PA 19104-6142. Phone: (215) 898-3256. Fax: (215) 573-3888. E-mail: alwine@mail.med.upenn.edu.
These authors contributed equally to this work.
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Human cytomegalovirus (HCMV) infection increases synthetic rates in infected cells. The resulting increase in energy utilization could potentially increase the...
ABSTRACT Human cytomegalovirus (HCMV) infection increases synthetic rates in infected cells. The resulting increase in energy utilization could potentially...
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SubjectTerms AMP-Activated Protein Kinases
Biological and medical sciences
Cells, Cultured
Cytomegalovirus - physiology
Fundamental and applied biological sciences. Psychology
Human cytomegalovirus
Humans
Microbial Viability
Microbiology
Miscellaneous
Multienzyme Complexes - genetics
Multienzyme Complexes - metabolism
Protein Kinase Inhibitors - metabolism
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Signal Transduction
Time Factors
TOR Serine-Threonine Kinases
Virology
Virus-Cell Interactions
Title AMPK-Mediated Inhibition of mTOR Kinase Is Circumvented during Immediate-Early Times of Human Cytomegalovirus Infection
URI http://jvi.asm.org/content/81/7/3649.abstract
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