Document Detail


Mechanisms of autoinhibition of IRF-7 and a probable model for inactivation of IRF-7 by Kaposi's sarcoma-associated herpesvirus protein ORF45.
MedLine Citation:
PMID:  20980251     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
IRF-7 is the master regulator of type I interferon-dependent immune responses controlling both innate and adaptive immunity. Given the significance of IRF-7 in the induction of immune responses, many viruses have developed strategies to inhibit its activity to evade or antagonize host antiviral responses. We previously demonstrated that ORF45, a KSHV immediate-early protein as well as a tegument protein of virions, interacts with IRF-7 and inhibits virus-mediated type I interferon induction by blocking IRF-7 phosphorylation and nuclear translocation (Zhu, F. X., King, S. M., Smith, E. J., Levy, D. E., and Yuan, Y. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 5573-5578). In this report, we sought to reveal the mechanism underlying the ORF45-mediated inactivation of IRF-7. We found that ORF45 interacts with the inhibitory domain of IRF-7. The most striking feature in the IRF-7 inhibitory domain is two α-helices H3 and H4 that contain many hydrophobic residues and two β-sheets located between the helices that are also very hydrophobic. These hydrophobic subdomains mediate intramolecular interactions that keep the molecule in a closed (inactive) form. Mutagenesis studies confirm the contribution of the hydrophobic helices and sheets to the autoinhibition of IRF-7 in the absence of viral signal. The binding of ORF45 to the critical domain of IRF-7 leads to a hypothesis that ORF45 may maintain the IRF-7 molecule in the closed form and prevent it from being activated in response to viral infection.
Authors:
Narayanan Sathish; Fan Xiu Zhu; Ellis E Golub; Qiming Liang; Yan Yuan
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-10-27
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  286     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-01-03     Completed Date:  2011-01-31     Revised Date:  2012-02-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  746-56     Citation Subset:  IM    
Affiliation:
Department of Microbiology, University of Pennsylvania School of Dental Medicine, Philadelphia, Pennsylvania 19104, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
HEK293 Cells
Herpesvirus 8, Human* / physiology
Humans
Hydrophobic and Hydrophilic Interactions
Immediate-Early Proteins / metabolism*
Interferon Regulatory Factor-7 / antagonists & inhibitors*,  chemistry,  genetics,  metabolism*
Models, Molecular*
Molecular Sequence Data
Mutagenesis
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Deletion
Substrate Specificity
Transcriptional Activation
Grant Support
ID/Acronym/Agency:
R01 DE016680-07/DE/NIDCR NIH HHS; R01CA86839/CA/NCI NIH HHS; R01DE016680/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Immediate-Early Proteins; 0/Interferon Regulatory Factor-7; 0/ORF45 protein, Kaposi's sarcoma-associated herpesvirus

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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